The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Proteins prepared by recombinant DNA technology.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The rate dynamics in chemical or physical systems.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Deletion of sequences of nucleic acids from the genetic material of an individual.
An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
Proteins found in any species of bacterium.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
The process of cleaving a chemical compound by the addition of a molecule of water.
Established cell cultures that have the potential to propagate indefinitely.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Transport proteins that carry specific substances in the blood or across cell membranes.
Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
The relationships of groups of organisms as reflected by their genetic makeup.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
An exocellulase with specificity for the hydrolysis of 1,4-beta-D-glucosidic linkages in CELLULOSE and cellotetraose. It catalyzes the hydrolysis of terminal non-reducing ends of beta-D-glucosides with release of CELLOBIOSE.
Physiologically inactive substances that can be converted to active enzymes.
Proteins found in any species of fungus.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Proteins obtained from ESCHERICHIA COLI.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
An enzyme that catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of polysaccharide chains with the release of beta-glucose. It is also able to hydrolyze 1,6-alpha-glucosidic bonds when the next bond in sequence is 1,4.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans.
Proteins produced from GENES that have acquired MUTATIONS.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Biochemical identification of mutational changes in a nucleotide sequence.
Polysaccharides consisting of xylose units.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
An essential amino acid. It is often added to animal feed.
Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
A genus of owlet moths of the family Noctuidae. These insects are used in molecular biology studies during all stages of their life cycle.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The branch of science that deals with the geometric description of crystals and their internal arrangement. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
The sum of the weight of all the atoms in a molecule.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A process whereby multiple RNA transcripts are generated from a single gene. Alternative splicing involves the splicing together of other possible sets of EXONS during the processing of some, but not all, transcripts of the gene. Thus a particular exon may be connected to any one of several alternative exons to form a mature RNA. The alternative forms of mature MESSENGER RNA produce PROTEIN ISOFORMS in which one part of the isoforms is common while the other parts are different.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. It is the second most abundant biopolymer on earth, found especially in INSECTS and FUNGI. When deacetylated it is called CHITOSAN.
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
The characteristic three-dimensional shape of a molecule.
A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
An enzyme that catalyzes the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. It also acts on ITP and dGTP. (From Enzyme Nomenclature, 1992) EC 4.6.1.2.
A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTICALES, containing uniflagellate zoospores.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
The class Insecta, in the phylum ARTHROPODA, whose members are characterized by division into three parts: head, thorax, and abdomen. They are the dominant group of animals on earth; several hundred thousand different kinds having been described. Three orders, HEMIPTERA; DIPTERA; and SIPHONAPTERA; are of medical interest in that they cause disease in humans and animals. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p1)
The accumulation of an electric charge on a object
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
A sequential pattern of amino acids occurring more than once in the same protein sequence.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
Proteins found in any species of protozoan.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.
The thermodynamic interaction between a substance and WATER.
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Methods for determining interaction between PROTEINS.
A guanine nucleotide exchange factor that is expressed primarily in neuronal tissue and may be specific for the Ha-ras homolog of the RAS PROTEINS.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Family of INSECT VIRUSES containing two subfamilies: Eubaculovirinae (occluded baculoviruses) and Nudibaculovirinae (nonoccluded baculoviruses). The Eubaculovirinae, which contain polyhedron-shaped inclusion bodies, have two genera: NUCLEOPOLYHEDROVIRUS and GRANULOVIRUS. Baculovirus vectors are used for expression of foreign genes in insects.
The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.
PROTEINS that specifically activate the GTP-phosphohydrolase activity of RAS PROTEINS.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

Phenotypic analysis of human glioma cells expressing the MMAC1 tumor suppressor phosphatase. (1/9378)

MMAC1, also known as PTEN or TEP-1, was recently identified as a gene commonly mutated in a variety of human neoplasias. Sequence analysis revealed that MMAC1 harbored sequences similar to those found in several protein phosphatases. Subsequent studies demonstrated that MMAC1 possessed in vitro enzymatic activity similar to that exhibited by dual specificity phosphatases. To characterize the potential cellular functions of MMAC1, we expressed wild-type and several mutant variants of MMAC1 in the human glioma cell line, U373, that lacks endogenous expression. While expression of wild-type MMAC1 in these cells significantly reduced their growth rate and saturation density, expression of enzymatically inactive MMAC1 significantly enhanced growth in soft agar. Our observations indicate that while wild-type MMAC1 exhibits activities compatible with its proposed role as a tumor suppressor, cellular expression of MMAC1 containing mutations in the catalytic domain may yield protein products that enhance transformation characteristics.  (+info)

A processive single-headed motor: kinesin superfamily protein KIF1A. (2/9378)

A single kinesin molecule can move "processively" along a microtubule for more than 1 micrometer before detaching from it. The prevailing explanation for this processive movement is the "walking model," which envisions that each of two motor domains (heads) of the kinesin molecule binds coordinately to the microtubule. This implies that each kinesin molecule must have two heads to "walk" and that a single-headed kinesin could not move processively. Here, a motor-domain construct of KIF1A, a single-headed kinesin superfamily protein, was shown to move processively along the microtubule for more than 1 micrometer. The movement along the microtubules was stochastic and fitted a biased Brownian-movement model.  (+info)

Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. (3/9378)

In the yeast Saccharomyces cerevisiae, the non-Mendelian inherited genetic element [URE3] behaves as a prion. A hypothesis has been put forward which states that [URE3] arises spontaneously from its cellular isoform Ure2p (the product of the URE2 gene), and propagates through interactions of the N-terminal domain of the protein, thus leading to its aggregation and loss of function. In the present study, various N- and C-terminal deletion mutants of Ure2p were constructed and their cross-interactions were tested in vitro and in vivo using affinity binding and a two-hybrid analysis. We show that the self-interaction of the protein is mediated by at least two domains, corresponding to the first third of the protein (the so-called prion-forming domain) and the C-terminal catalytic domain.  (+info)

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. (4/9378)

The catalytic subunit of protein serine/threonine phosphatase 4 (PP4C) has greater than 65% amino acid identity to the catalytic subunit of protein phosphatase 2A (PP2AC). Despite this high homology, PP4 does not appear to associate with known PP2A regulatory subunits. As a first step toward characterization of PP4 holoenzymes and identification of putative PP4 regulatory subunits, PP4 was purified from bovine testis soluble extracts. PP4 existed in two complexes of approximately 270-300 and 400-450 kDa as determined by gel filtration chromatography. The smaller PP4 complex was purified by sequential phenyl-Sepharose, Source 15Q, DEAE2, and Superdex 200 gel filtration chromatographies. The final product contained two major proteins: the PP4 catalytic subunit plus a protein that migrated as a doublet of 120-125 kDa on SDS-polyacrylamide gel electrophoresis. The associated protein, termed PP4R1, and PP4C also bound to microcystin-Sepharose. Mass spectrometry analysis of the purified complex revealed two major peaks, at 35 (PP4C) and 105 kDa (PP4R1). Amino acid sequence information of several peptides derived from the 105 kDa protein was utilized to isolate a human cDNA clone. Analysis of the predicted amino acid sequence revealed 13 nonidentical repeats similar to repeats found in the A subunit of PP2A (PP2AA). The PP4R1 cDNA clone engineered with an N-terminal Myc tag was expressed in COS M6 cells and PP4C co-immunoprecipitated with Myc-tagged PP4R1. These data indicate that one form of PP4 is similar to the core complex of PP2A in that it consists of a catalytic subunit and a "PP2AA-like" structural subunit.  (+info)

PrKX is a novel catalytic subunit of the cAMP-dependent protein kinase regulated by the regulatory subunit type I. (5/9378)

The human X chromosome-encoded protein kinase X (PrKX) belongs to the family of cAMP-dependent protein kinases. The catalytically active recombinant enzyme expressed in COS cells phosphorylates the heptapeptide Kemptide (LRRASLG) with a specific activity of 1.5 micromol/(min.mg). Using surface plasmon resonance, high affinity interactions were demonstrated with the regulatory subunit type I (RIalpha) of cAMP-dependent protein kinase (KD = 10 nM) and the heat-stable protein kinase inhibitor (KD = 15 nM), but not with the type II regulatory subunit (RIIalpha, KD = 2.3 microM) under physiological conditions. Kemptide and autophosphorylation activities of PrKX are strongly inhibited by the RIalpha subunit and by protein kinase inhibitor in vitro, but only weakly by the RIIalpha subunit. The inhibition by the RIalpha subunit is reversed by addition of nanomolar concentrations of cAMP (Ka = 40 nM), thus demonstrating that PrKX is a novel, type I cAMP-dependent protein kinase that is activated at lower cAMP concentrations than the holoenzyme with the Calpha subunit of cAMP-dependent protein kinase. Microinjection data clearly indicate that the type I R subunit but not type II binds to PrKX in vivo, preventing the translocation of PrKX to the nucleus in the absence of cAMP. The RIIalpha subunit is an excellent substrate for PrKX and is phosphorylated in vitro in a cAMP-independent manner. We discuss how PrKX can modulate the cAMP-mediated signal transduction pathway by preferential binding to the RIalpha subunit and by phosphorylating the RIIalpha subunit in the absence of cAMP.  (+info)

Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase. (6/9378)

Site-directed mutagenesis has been employed to study the mechanism of hydride transfer from NADPH to NADPH-cytochrome P450 oxidoreductase. Specifically, Ser457, Asp675, and Cys630 have been selected because of their proximity to the isoalloxazine ring of FAD. Substitution of Asp675 with asparagine or valine decreased cytochrome c reductase activities 17- and 677-fold, respectively, while the C630A substitution decreased enzymatic activity 49-fold. Earlier studies had shown that the S457A mutation decreased cytochrome c reductase activity 90-fold and also lowered the redox potential of the FAD semiquinone (Shen, A., and Kasper, C. B. (1996) Biochemistry 35, 9451-9459). The S457A/D675N and S457A/D675N/C630A mutants produced roughly multiplicative decreases in cytochrome c reductase activity (774- and 22000-fold, respectively) with corresponding decreases in the rates of flavin reduction. For each mutation, increases were observed in the magnitudes of the primary deuterium isotope effects with NADPD, consistent with decreased rates of hydride transfer from NADPH to FAD and an increase in the relative rate limitation of hydride transfer. Asp675 substitutions lowered the redox potential of the FAD semiquinone. In addition, the C630A substitution shifted the pKa of an ionizable group previously identified as necessary for catalysis (Sem, D. S., and Kasper, C. B. (1993) Biochemistry 32, 11539-11547) from 6.9 to 7.8. These results are consistent with a model in which Ser457, Asp675, and Cys630 stabilize the transition state for hydride transfer. Ser457 and Asp675 interact to stabilize both the transition state and the FAD semiquinone, while Cys630 interacts with the nicotinamide ring and the fully reduced FAD, functioning as a proton donor/acceptor to FAD.  (+info)

Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR. (7/9378)

The interferon-inducible, double-stranded RNA-dependent protein kinase PKR has been implicated in anti-viral, anti-tumor, and apoptotic responses. Others have attempted to examine the requirement of PKR in these roles by targeted disruption at the amino terminal-encoding region of the Pkr gene. By using a strategy that aims at disruption of the catalytic domain of PKR, we have generated mice that are genetically ablated for functional PKR. Similar to the other mouse model of Pkr disruption, we have observed no consequences of loss of PKR on tumor suppression. Anti-viral response to influenza and vaccinia also appeared to be normal in mice and in cells lacking PKR. Cytokine signaling in the type I interferon pathway is normal but may be compromised in the erythropoietin pathway in erythroid bone marrow precursors. Contrary to the amino-terminal targeted Pkr mouse, tumor necrosis factor alpha-induced apoptosis and the anti-viral apoptosis response to influenza is not impaired in catalytic domain-targeted Pkr-null cells. The observation of intact eukaryotic initiation factor-2alpha phosphorylation in these Pkr-null cells provides proof of rescue by another eukaryotic initiation factor-2alpha kinase(s).  (+info)

His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes. (8/9378)

Bovine pancreatic ribonuclease A (RNase A) has a conserved His ... Asp catalytic dyad in its active site. Structural analyses had indicated that Asp121 forms a hydrogen bond with His119, which serves as an acid during catalysis of RNA cleavage. The enzyme contains three other histidine residues including His12, which is also in the active site. Here, 1H-NMR spectra of wild-type RNase A and the D121N and D121A variants were analyzed thoroughly as a function of pH. The effect of replacing Asp121 on the microscopic pKa values of the histidine residues is modest: none change by more than 0.2 units. There is no evidence for the formation of a low-barrier hydrogen bond between His119 and either an aspartate or an asparagine residue at position 121. In the presence of the reaction product, uridine 3'-phosphate (3'-UMP), protonation of one active-site histidine residue favors protonation of the other. This finding is consistent with the phosphoryl group of 3'-UMP interacting more strongly with the two active-site histidine residues when both are protonated. Comparison of the titration curves of the unliganded enzyme with that obtained in the presence of different concentrations of 3'-UMP shows that a second molecule of 3'-UMP can bind to the enzyme. Together, the data indicate that the aspartate residue in the His ... Asp catalytic dyad of RNase A has a measurable but modest effect on the ionization of the adjacent histidine residue.  (+info)

Mammalian Cdc25 phosphatase is responsible for the dephosphorylation of Cdc2 and other cyclin-dependent kinases at Thr14 and Tyr15, thus activating the kinase and allowing cell cycle progression. The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. Apart from a CX3R motif, which is present at the active site of all known tyrosine phosphatases, Cdc25 does not share any obvious sequence similarity with any of those enzymes. Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. Using the generalized profile technique, a sensitive method for sequence database searches, we found an extended and highly significant sequence similarity between the Cdc25 catalytic domain and similarly sized regions in other proteins: the non-catalytic domain of two distinct families of MAP-kinase phosphates, the non-catalytic domain of several ubiquitin protein ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
UCSF researchers have invented a novel method to generate covalent macromolecular inhibitors. This strategy allows a peptide inhibitor to bind to its target protein specifically and irreversibly through proximity-enabled bioreactivity.
The Enzyme Collection contains over 550 mAbs that recognize catalytic domains or associated regulatory subunits in enyme complexes
The Enzyme Collection contains over 550 mAbs that recognize catalytic domains or associated regulatory subunits in enyme complexes
The SCOP classification for the Metallo-dependent phosphatases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
ウサギ・ポリクローナル抗体 ab96186 交差種: Ms,Hu 適用: WB,ICC/IF…cAMP Protein Kinase Catalytic subunit抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody…
Enzymes are nanomachines that are exceptionally efficient at catalyzing a chemical reaction. They play a role in all cellular mechanisms. Like all proteins, they are made up of amino acid chains that are folded and assembled in a very precise 3D structure. Some enzymes, like ribonuclease A, are so efficient that they catalyze the transformation of chemical molecules thousands of times per second.. In this study, Donald Gagné, a researcher in Professor Doucets lab holding a PhD in biology from INRS, analyzed the impact of removing a methyl group located near a loop distant from the reaction site of ribonuclease A-a very slight change that presumably would have no effect. The mutation does not perturb the 3D structure of the enzyme. However, it did result in a four-fold reduction in the affinity of ribonuclease A for nucleotides (molecules to which it must bind to carry out its function). How is this possible?. Using crystallography techniques and nuclear magnetic resonance to examine the enzyme ...
BioAssay record AID 1078965 submitted by ChEMBL: Inhibition of human FGFR4 catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 0.06 uM after 90 mins by microfluidic peptide phosphorylation assay.
BioAssay record AID 1078796 submitted by ChEMBL: Inhibition of human FER catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 9 uM after 90 mins by microfluidic peptide phosphorylation assay.
1GNR: X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp.
Read Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase, Cellular and Molecular Life Sciences on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
, MDC Recombinant Protein (Active), GTX48056-PRO, Applications: ELISA, WB, Functional Assay; ELISA, Western Blot (WB), Functional Assay; CrossReactivity:
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
Plasmid pdCas9 (GB1079) from Dr. Diego Orzaezs lab contains the insert Cas9 coding region with mutated (D10A, H840A) and inactivated catalytic domains (human codon optimised) and is published in Plant Methods. 2016 Feb 1;12:10. doi: 10.1186/s13007-016-0101-2. eCollection 2016. This plasmid is available through Addgene.
appendicitis - Meaning in Thai, what is meaning of common in Thai dictionary, audio pronunciation, synonyms and definitions of common in Thai and English.
Diflavin reductases are essential proteins capable of splitting the two-electron flux from reduced pyridine nucleotides to a variety of one electron acceptors. The primary sequence of diflavin reductases shows a conserved domain organization harboring two catalytic domains bound to the FAD and FMN flavins sandwiched by one or several non-catalytic domains. The catalytic domains are analogous to existing globular proteins: the FMN domain is analogous to flavodoxins while the FAD domain resembles ferredoxin reductases. The first structural determination of one member of the diflavin reductases family raised some questions about the architecture of the enzyme during catalysis: both FMN and FAD were in perfect position for interflavin transfers but the steric hindrance of the FAD domain rapidly prompted more complex hypotheses on the possible mechanisms for the electron transfer from FMN to external acceptors. Hypotheses of domain reorganization during catalysis in the context of the different members of
Dynamic processes are implicit in the catalytic function of all enzymes. To obtain insights into the relationship between the dynamics and thermodynamics of protein fluctuations and catalysis, we have measured millisecond time scale motions in the enzyme dihydrofolate reductase using NMR relaxation methods. Studies of a ternary complex formed from the substrate analog folate and oxidized NADP+ cofactor revealed conformational exchange between a ground state, in which the active site loops adopt a closed conformation, and a weakly populated (4.2% at 30 degrees C) excited state with the loops in the occluded conformation. Fluctuations between these states, which involve motions of the nicotinamide ring of the cofactor into and out of the active site, occur on a time scale that is directly relevant to the structural transitions involved in progression through the catalytic cycle ...
Electrostatic interactions between ligands and their receptors are important factors for molecular recognition. Assessing the ligand-receptor electrostatic complementarity provide valuable information for molecular design. In this hands-on workshop we will focus on using Flare™, Cressets structure-based design application to design ligands that are electrostatically complementary to the protein active site. You will learn how to visualize ligand-protein interactions; design new molecules in the context of the active site; easily dock new molecule designs to a protein active site; and assess the electrostatic complementarity between ligands and protein.
Scientists at the Center for Molecular Electrocatalysis conducted a detailed comparison of catalytic performance. They compared catalysts with different ring sizes and different numbers of proton relays. They found that the catalyst 7P2N with a smaller ring and fewer proton relays was faster or had a higher turnover efficiency. CME is an Energy Frontier Research Center funded by DOE Basic Energy Sciences and led by Pacific Northwest National Laboratory
PDE7 inhibitors regulate pro-inflammatory and immune T-cell functions, and are a potentially novel class of drugs especially useful in the treatment of a wide variety of immune and inflammatory disorders. Starting from our lead family of thioxoquinazolines, we designed, synthesized, and characterized a novel series of thioxoquinazoline derivatives. Many of these compounds showed inhibitory potencies at sub-micromolar levels against the catalytic domain of PDE7A1 and at the micromolar level against PDE4D2. Cell-based studies showed that these compounds not only increased intracellular cAMP levels, but also had interesting anti-inflammatory properties within a therapeutic window. The in silico data predict that these compounds are capable of the crossing the blood-brain barrier. The X-ray crystal structure of the PDE7A1 catalytic domain in complex with compound 15 at a resolution of 2.4 A demonstrated that hydrophobic interactions at the active site pocket are a key feature. This structure, ...
Anti-ACE-1 (Angiotension Converting Enzyme, Angiotension I-converting enzyme, Peptidyl-dipeptidase-A); Carboxy Catalytic domain Antibody related publications, related pathways and related gentaur products
Of course much of human biology - growth and development, and cancer metastasis are the big ones - rely on these sensing and adhesion mechanisms, but Geiger and Spatz bring up some others: How certain cells sense blood flow, for instance, might affect the sticky buildup of plaques on artery walls. And they suggest that even before primitive cells began sticking together to form multicellular organisms, they probably formed some version of these complexes to adhere to other things - food sources, for instance.. The second article describes the postdoctoral research and future plans of Dr. Sarel Fleishman, who recently joined the Institute. Fleishman was in the protein design lab of Prof. David Baker at the University of Washington, Seattle, where he designed a protein that is able to block a wide range of flu viruses.. Designed is the operative word here: Fleishman and his lab mates showed that one can predict what is needed to selectively bind to a virus proteins active site, create a ...
Sigma-Aldrich offers abstracts and full-text articles by [Rasha H Alghamdi, Paul OReilly, Chunyu Lu, James Gomes, Thomas A Lagace, Ajoy Basak].
Mutations are changes in the base sequence of DNA, these mutations can produce new alleles of genes, if this changes a different protein or a non-functioning protein (change in the structure leading to a wrong active site) can be produced. ...
A molecule that doesnt have a similar shape to the substrate, but binds elsewhere than the active site. This changes the shape of the enzyme and the active site, meaning that the substrate can no longer fit. Therefore, no reaction occurs. ...
Within biological systems iron is a transition metal that allows access to the benefits of molecular oxygen as an oxidant. However, with these benefits come grave consequences if the reactions are not strictly controlled. The most prominent strategy of control and specialization is the protein environment that surrounds iron. Within iron containing proteins, specifically heme proteins, there are four basic levels of structure that impact the irons function: cofactor structure, protein-supplied ligands, non-ligand active site environment, and protein features that are distant from the active site. This last level remains poorly understood due to a lack of good models to pursue such studies. Catalase-peroxidases are unique heme proteins because they catalyze peroxide decomposition by two separate mechanisms, catalase and peroxidase, using the same active site. However, were it not for three structural features distant from the active site, catalase-peroxidases would be practically superimposable ...
Robb, CS, Mystkowska, AA and Hehemann, JH (2017) Crystal structure of a marine glycoside hydrolase family 99-related protein lacking catalytic machinery. Protein Science, 26(12). 2445-2450. doi:10.1002/pro.3291 ...
Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. We have selected two of these regions to build signature patterns. The first region, which is located in the N-terminal extremity of the catalytic domain, is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. The second region, which is located in the central part of the catalytic domain, contains a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [6]; we have derived two signature patterns for that region: one specific for serine/ threonine kinases and the other for tyrosine kinases. We also developed a profile which is based on the alignment in [1] and covers the entire catalytic domain. Note: If a ...
Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. We have selected two of these regions to build signature patterns. The first region, which is located in the N-terminal extremity of the catalytic domain, is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. The second region, which is located in the central part of the catalytic domain, contains a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [6]; we have derived two signature patterns for that region: one specific for serine/ threonine kinases and the other for tyrosine kinases. We also developed a profile which is based on the alignment in [1] and covers the entire catalytic domain. Note: If a ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Zinc atom in PDB 3frg: Catalytic Domain of Human Phosphodiesterase 4B2B in Complex With A Quinoline Inhibitor
New insights into the behaviour of molecules could have major implications for the design of drugs that block protein interactions. A team of researchers led by Dr Peter Crowley at the National University of Ireland Galway has revealed in intricate detail how a drug-like molecule can explore the surface of a protein.. The pioneering work was published by Nature Chemistry online (Sunday, 29 April) and will appear in the June issue of the journal. It was found that molecules scout around the protein surface, moving from one location to another constantly examining their surroundings.. For the past thirty years, drug design has been dominated by the search for small molecules that fit perfectly into a proteins active site and modify its activity. Recently, the focus of attention has shifted to molecules that recognise and bind to the protein surface. Such molecules can camouflage the protein and prevent it binding to other proteins. Knowledge of these interactions is essential to the development ...
i) studies of copper-dioxygen chemistry in order to elucidate characteristics of peroxo-dicopper(II) and bis-µ-oxo dicopper(III) complexes, the nature of the equilibrium interconverting them, searching for possible differential reactivity, and examining and probing for new highly reactive higher-valent copper-oxo species.. (ii) developing new copper ion peptide chemistry, using amino acids and peptide sequences which are relevant to copper protein active sites; specific structural motifs will be examined. The research is also aimed to study peptides which bind copper and which have been implicated to be toxic (and effect biological oxidative damage) in Alzheimers disease states.. (iii) reactions of copper ion complexes with elemental sulfur, to generate new copper-sulfide species. A reduced tetracopper(I)-sulfide complex facilitates reduction of nitrous oxide in Nature. Newly synthesized dicopper(II)-disulfide complexes have been characterized and (e.g., see diagram) and are being used as ...
These enzymes are very specific, Dordick said, targeting one or only a few bacteria. In this paper, the researchers set out to see if they could improve the combinations nature has created.. The idea was: Could we use a Lego-like approach here? Could we take a binding domain from one enzyme and can we mix it with a binding domain or catalytic domain of another one? Dordick said.. More specifically, the team took the protein streptavidin, which acts as an effective template to which the researchers could attach a binding domain from one organism and a catalytic domain from another. The modularity approach allows them to make new combinations quickly in order to determine which work best.. They found that in targeting Staphylococcus aureus - commonly known as staph - their combinations were very effective, at times even better than what occurs in nature.. We genetically expressed the binding domains or the catalytic domains from several different organisms, Dordick said. We identified some ...
Active Recombinant rhesus monkey IL-13 protein (Active) is an Escherichia coli Full length protein 19 to 132 aa range, | 98% purity and validated in FuncS, SDS-PAGE, HPLC. ab216214 is fully biologica…
, LIX Recombinant Protein (Active), GTX48052-PRO, Applications: ELISA, WB, Functional Assay; ELISA, Western Blot (WB), Functional Assay; CrossReactivity:
Active Recombinant human CNDP1/CN1 protein (Active) is a Baculovirus infected insect Full length protein 27 to 507 aa range, | 95% purity, | 1.000 Eu/µg endotoxin level and validated in SDS-PAGE. Spe…
Purpose Metabolism, and especially glucose uptake, is normally an integral quantitative cell characteristic thats associated with cancer tumor initiation and development closely. advantages within the various other available blood sugar tracers, such as for example 2-DG or the radiolabel isotope FDG, including INCB8761 its low comparative cost, convenience of high temporal and spatial quality (on the single-cell level), insufficient ionizing radiation, as well as the nondestructive nature enabling immediate monitoring of blood sugar transport in live cells. Furthermore, we developed another independent method of directly measure the distribution of blood sugar uptake on the single-cell level that utilizes the energy of high-content computerized microscopy (HCAM), cell-cytometric picture evaluation (via in DMSO. Likewise, split plates had been treated and ready with Erlotinib at the same concentrations. Cells had been incubated with medications for another INCB8761 24 h Cish3 under regular ...
AbeBooks.com: Enzymic Catalysis (Modern Perspectives in Biology): Spine creases, wear to binding and pages from reading. May contain limited notes, underlining or highlighting that does affect the text. Possible ex library copy, thatâ ll have the markings and stickers associated from the library. Accessories such as CD, codes, toys, may not be included.
This Special Issue contains twelve reviews as well as an interview that feature a rapidly developing area of biology: catalytically inactive enzyme homologs, also known as pseudoenzymes. These pseudoenzymes, are often referred to as dead enzymes, and are found within most enzyme families. Pseudoenzymes have lost their enzymatic capacity, often via the evolutionary loss of key catalytic residues, however, pseudoenzymes are far from being functionally dead, as evidenced within this Special Issue. As a matter of fact, pseudoenzymes fulfil a range of integral biochemical roles, frequently appearing more versatile as biochemical regulators than their catalytic cousins. As well as focusing on the breadth and depth of dead enzyme biology, this Special Issue emphasizes the power of pseudoenzymes as key biochemical regulators in health and disease and potentially as more tractable drug targets than some enzymes themselves. We hope you find these reviews enlivening and we thank the authors for these ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Business Gurus:. …In this article, Jim Collins introduces the catalytic mechanism, a simple yet powerful managerial tool that helps translate lofty aspirations into concrete reality. Whats the difference between catalytic mechanisms and most traditional managerial controls? Catalytic mechanisms share five characteristics. First, they produce desired results in unpredictable ways. Second, they distribute power for the benefit of the overall system, often to the discomfort of those who traditionally hold power. Third, catalytic mechanisms have teeth. Fourth, they eject viruses--those people who dont share the companys core values. Finally, they produce an ongoing effect.. [Editorial Review, Book Description of Turning Goals into Results: The Power of Catalytic Mechanisms by Jim Collins posted at www.amazon.com ]. Now that we are really beginning to understand what makes organizations great in the business world, we might actually provide some DNA to the whole social system. ...
Enzymes are three-dimensional machines that have an active site, which recognizes specifically shaped substrates. If a chemical inhibits the enzyme by binding at the active site, that is a giveaway sign that the chemical is in the category of competitive inhibitors, as opposed to non-competitive inhibitors. However, ...
Enzymes are biological catalysts. See enzymes in digestion. How substrates fit into an enzymes active site and the effects of temperature and pH on enzyme activity.
3) An approach of the ionic species to the catalytic nucleophile leads to the formation of a covalent intermediate of inverted alpha-configuration in a so-called chair conformation ...
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Kinases control virtually all aspects of biology. Forty-eight human proteins have a kinase-like domain that lacks at least one of the conserved catalytic residues; these proteins are therefore predicted to be inactive and have been termed pseudokinases. Here, we describe exciting work suggesting tha …
Abstract: Ubiquitin specific proteases (USPs) reverse ubiquitination and regulate virtually all cellular processes. Defined non-catalytic domains in USP4 and USP15 are known to interact with E3 ligases and substrate recruitment factors. No such interactions have been reported for these domains in the paralog USP11, a key regulator of DNA double-strand break repair by homologous recombination (HR). We hypothesized that USP11 domains adjacent to its protease domain harbour unique peptide-binding sites. Here, using a next-generation phage display (NGPD) strategy, combining phage display library screening with next generation sequencing, we discovered unique USP11 interacting peptide motifs. Isothermal titration calorimetry disclosed that the highest affinity peptides (KD of ~10 μM) exhibit exclusive selectivity for USP11 over USP4 and USP15 in vitro. Furthermore, a crystal structure of a USP11-peptide complex revealed a previously unknown binding site in USP11s non-catalytic ubiquitin-like (UBL) ...
Abstract: Ubiquitin specific proteases (USPs) reverse ubiquitination and regulate virtually all cellular processes. Defined non-catalytic domains in USP4 and USP15 are known to interact with E3 ligases and substrate recruitment factors. No such interactions have been reported for these domains in the paralog USP11, a key regulator of DNA double-strand break repair by homologous recombination (HR). We hypothesized that USP11 domains adjacent to its protease domain harbour unique peptide-binding sites. Here, using a next-generation phage display (NGPD) strategy, combining phage display library screening with next generation sequencing, we discovered unique USP11 interacting peptide motifs. Isothermal titration calorimetry disclosed that the highest affinity peptides (KD of ~10 μM) exhibit exclusive selectivity for USP11 over USP4 and USP15 in vitro. Furthermore, a crystal structure of a USP11-peptide complex revealed a previously unknown binding site in USP11s non-catalytic ubiquitin-like (UBL) ...
of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.[3] Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[1]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.[4] The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivans pyridine ring and the interactions between Gly27 and Crixivans aromatic rings.[5] ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Zinc atom in PDB 1tbf: Catalytic Domain of Human Phosphodiesterase 5A in Complex With Sildenafil
For additional Rizzo Lab tutorials see [[DOCK Tutorials]]. This tutorial is based on the [[2010 DOCK tutorial with Streptavidin]] with minor modifications. ==About DOCK== DOCK was developed by Irwin D. Tack Kuntz, Jr., PhD and colleagues at UCSF. Please see the webpage at [http://dock.compbio.ucsf.edu/ UCSF DOCK]. DOCK is a molecular docking program used in drug discovery. This program, given a protein active site and a small molecule, tries to predict the correct binding mode of the small molecule in the active site, and the associated binding energy. Small molecules with highly favorable binding energies could be new drug leads. This makes DOCK a valuable drug discovery tool. DOCK is typically used to screen massive libraries of millions of compounds against a protein to isolate potential drug leads. These leads are then further studied, and could eventually result in a new, marketable drug. DOCK is works well as a screening procedure for generating leads, but not nearly as well for ...
For additional Rizzo Lab tutorials see [[DOCK Tutorials]]. This tutorial is based on the [[2010 DOCK tutorial with Streptavidin]] with minor modifications. ==About DOCK== DOCK was developed by Irwin D. Tack Kuntz, Jr., PhD and colleagues at UCSF. Please see the webpage at [http://dock.compbio.ucsf.edu/ UCSF DOCK]. DOCK is a molecular docking program used in drug discovery. This program, given a protein active site and a small molecule, tries to predict the correct binding mode of the small molecule in the active site, and the associated binding energy. Small molecules with highly favorable binding energies could be new drug leads. This makes DOCK a valuable drug discovery tool. DOCK is typically used to screen massive libraries of millions of compounds against a protein to isolate potential drug leads. These leads are then further studied, and could eventually result in a new, marketable drug. DOCK is works well as a screening procedure for generating leads, but not nearly as well for ...
PIK3C2B (phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
Protein features are: Chitin binding domain; Chitinase II; Glycoside hydrolase, chitinase active site; Glycoside hydrolase, family 18, catalytic domain; Glycoside hydrolase, subgroup, catalytic core; Glycoside hydrolase, superfamily ...
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Purpose Metabolism, and especially glucose uptake, is normally an integral quantitative cell characteristic thats associated with cancer tumor initiation and development closely. advantages within the various other available blood sugar tracers, such as for example 2-DG or the radiolabel isotope FDG, including INCB8761 its low comparative cost, convenience of high temporal and spatial quality (on the single-cell level), insufficient ionizing radiation, as well as the nondestructive nature enabling immediate monitoring of blood sugar transport in live cells. Furthermore, we developed another independent method of directly measure the distribution of blood sugar uptake on the single-cell level that utilizes the energy of high-content computerized microscopy (HCAM), cell-cytometric picture evaluation (via in DMSO. Likewise, split plates had been treated and ready with Erlotinib at the same concentrations. Cells had been incubated with medications for another INCB8761 24 h Cish3 under regular ...
Exceptions to a long-held rule against chemically bonding to biological targets are powering new cancer medicines, finds Andy Extance
Modules of approx. 70 residues. The chitin-binding function has been demonstrated in several cases. These modules are found attached to a number of chitinase catalytic domains, but also in non-catalytic proteins either in isolation or as multiple repeats; chitin binding (EC IIa.chitin ...
This is a list of changes made recently to pages linked from a specified page (or to members of a specified category). Pages on your watchlist are bold. ...
Catalysis Today focuses on the rapid publication of original invited papers devoted to currently important topics in catalysis and related subjects....
鳳嬌是行為、材質與人的催化室。 時間、空間、纖維、自然萬物、你我的天賦、經驗、專業、概念和行動都可以在此化為靈感、創造、潮流和洞見。催化進行中,未來尚未來,鳳嬌現在還不急著定義自己。. ...
鳳嬌是行為、材質與人的催化室。 時間、空間、纖維、自然萬物、你我的天賦、經驗、專業、概念和行動都可以在此化為靈感、創造、潮流和洞見。催化進行中,未來尚未來,鳳嬌現在還不急著定義自己。. ...
This enzyme has 8 helical domains anchoring it in the Golgi membrane of the ER; the catalytic domain is in the cytosol. It is ...
The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and ... 2000). "The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated ... V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome. GRCh38: Ensembl release 89: ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c' ', and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c double prime, and ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This encoded protein is one of three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This gene encodes the V1 domain D subunit protein. GRCh38: Ensembl release 89: ENSG00000100554 - Ensembl, May 2017 GRCm38: ...
Busch C, Schömig K, Hofmann F, Aktories K (November 2000). "Characterization of the Catalytic Domain of Clostridium novyi Alpha ...
Its catalytic domain is homologous to that of other polymerases. It is presumed that the horizontal transfer of bacterial CCA- ... nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein". The ... However, the wide distribution of this modification and the fact that it is present in organisms from all three domains of life ... Yehudai-Resheff S, Portnoy V, Yogev S, Adir N, Schuster G (September 2003). "Domain analysis of the chloroplast polynucleotide ...
"Modulation of Catalytic Activity in Multi-Domain Protein Tyrosine Phosphatases". PLOS ONE. 6 (9): e24766. Bibcode:2011PLoSO... ... She was the lead developer of 3DSwap, a database of 3D domain-swapped proteins. Besides, along with James Spudich of the ...
... activity can be identified by its catalytic protein domain (hTERT). This[clarify] is the rate-limiting step in ... The protein consists of four conserved domains (RNA-Binding Domain (TRBD), fingers, palm and thumb), organized into a "right ... "Minimum length requirement of the alignment domain of human telomerase RNA to sustain catalytic activity in vitro". Nucleic ... On the other hand, one study showed that activating telomerase in cancer-resistant mice by overexpressing its catalytic subunit ...
Hanks SK, Hunter T (May 1995). "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain ... These domains are not related to the carboxy-terminal domain of double-time, suggesting a split in the evolution of the ... Each of these mutations maps to the kinase domain of DBT gene. The short- and long-period alleles of DBT enhance or attenuate, ... Wnt binding to LRP causes a rapid increase in phosphorylation of the cytoplasmic domain of LRP by CK1gamma. Phosphorylation of ...
In the central part of the catalytic domain, there is a conserved aspartic acid, which is important for the catalytic activity ... In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine ... Hanks SK, Quinn AM (1991). "Protein kinase catalytic domain sequence database: identification of conserved features of primary ... Hanks SK, Hunter T (May 1995). "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain ...
MYLK's contain a catalytic core domain with an ATP binding domain. On either sides of the catalytic core sit calcium ion/ ... Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain ... While there are numerous differing domains depending on the cell type, there are several characteristic domains common amongst ... On the other side of the kinase at the N-Terminus end, sits the actin-binding domain, which allows MYLK to form interactions ...
Moremen KW, Touster O, Robbins PW (Sep 1991). "Novel purification of the catalytic domain of Golgi alpha-mannosidase II. ...
Evidence for a Nucleotide Pyrophosphatase Catalytic Domain in MutT-like Enzymes. J. Biol. Chem. 1995, 270 (4), 1529-1534. https ...
Domain B makes up a twisted antiparallel β sheet. Some of the loops in domain B help shape the groove near the catalytic site. ... Domain A contains the (β/α)8 barrel and the catalytic site. In the catalytic site, three residues in particular play important ... For example, both enzymes have three domains in their catalytic core and a (β/α)8 barrel. Glucansucrase has 5 major domains: A ... The folding characteristics of α-amylase and glucansucrase are still very similar, but their domains are permuted. Domains A, B ...
All retain a conventional catalytic domain, but lack a recognizable specificity domain. 5′ tRNA processing activity of the RNA ... The primary role of the C5 protein is to enhance the substrate binding affinity and the catalytic rate of the M1 RNA enzyme ... Guerrier-Takada C, Gardiner K, Marsh T, Pace N, Altman S (December 1983). "The RNA moiety of ribonuclease P is the catalytic ... Isolated eukaryotic and archaeal RNase P RNA has not been shown to retain its catalytic function, but is still essential for ...
DNA binding domain Amine oxidase domain: catalytic active site of LSD proteins; larger than related proteins to help fit size ... N/C terminal domains): Binding domain of key cofactors such as alpha-keto glutarate; connected by a beta-hairpin/mixed domain ... West AH, Martinez-Hackert E, Stock AM (Jul 1995). "Crystal structure of the catalytic domain of the chemotaxis receptor ... Domains include: SWIRM1 (Swi3, Rsc, and Moira domain): Proposed anchor site for histone molecules; found in several chromatin ...
Huang WC, Ellis J, Moody PC, Raven EL, Roberts GC (September 2013). "Redox-linked domain movements in the catalytic cycle of ... It is assumed that the part of GcoB interacting with GcoA is at the intersection between the FAD binding domain and ferredoxin ... The component proteins are a cytochrome P450 enzyme (encoded by the gcoA gene from the family CYP255A) and a three-domain ... domain. To achieve this GcoB would have to go through some structural change, which would represent a new class of P450 systems ...
These domains aid in substrate recognition and catalytic activity. Four diverse examples of TIM barrels containing additional ... Successful TIM barrel designs include both domain fusions of existing proteins and de novo designs. Domain fusions experiments ... 4 half-barrel domains amongst preexisting TIM barrels. In accordance with this idea, a high catalytic activity on the HisAF ... be so long that they contain other protein domains. Recently, it has been demonstrated that catalytic loops can be exchanged ...
... has catalytic head domains regulated by hydrophobic residues. When Cry6Aa is first ingested, it remains a pro-toxin ... Most Cry proteins have 3 main domains with functional homology across proteins, domain I contains an alpha helix bundle, domain ... The head domain folds over the helices and contains a beta tongue group, which may trigger pore formation. There is a strong ... However, Cry6Aa, a nine turn protein, consists of bipartite head and tail domains composed mainly of alpha helices. Secondary ...
"Somatic mutation of EGFR catalytic domain and treatment with gefitinib in colorectal cancer". Ann. Oncol. 16 (11): 1848-9. doi: ... Kim YG, Cha J, Chandrasegaran S (February 1996). "Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain". ... January 2011). "TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain". Nucleic Acids ... April 2010). "Generation of redesigned homing endonucleases comprising DNA-binding domains derived from two different scaffolds ...
September 2003). "Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules". Nature. 425 (6953 ...
The CDK6 protein contains a catalytic core composed of a serine/threonine domain. This protein also contains an ATP-binding ... like the protein p21 and p27 act blocking and inhibiting the assembled C-CDKs binding complex enzymes in their catalytic domain ... This kinase is a catalytic subunit of the protein kinase complex, important for the G1 phase progression and G1/S transition of ... Grossel MJ, Baker GL, Hinds PW (Oct 1999). "cdk6 can shorten G(1) phase dependent upon the N-terminal INK4 interaction domain ...
"Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules". Nature. 425 (6953): 98-102. doi: ...
Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM (2006). "Structure of the catalytic domain of the hepatitis C virus NS2-3 ... Although NS3 domain's active role is not known yet, scientist propose that NS3 may interact with the active site of NS2 which ... NS2 Pro (non-structural protease) monomer is made up of two sub-domains which is connected by a linker. Each monomer contains ... The NS2-3 protease requires both NS2 and NS3 domain for proteolytic cleavage. Addition of Zinc is also required as NS2-3 ...
"Somatic mutation of EGFR catalytic domain and treatment with gefitinib in colorectal cancer". Ann. Oncol. 16 (11): 1848-9. doi: ...
... has a large conserved catalytic domain specific to the protein kinase superfamily. Nineteen ATP-binding sites found in ... SH3 Domain Binding Kinase Family Member 3 is an enzyme that in humans is encoded by the SBK3 gene (also known as SGK110). SBK3 ... The tyrosine motif exists in SBK3 (residues 44-233) and is found to overlap the conserved protein kinase superfamily domain ( ... A cross-program analysis revealed a predicted transmembrane domain (TMD) approximately spanning residues 224-240. A SUMO- ...
Specifically, USP domains are characterized for having interspered points with insertions in the catalytic domain. This ... The number of aminoacids in USPs catalytic domain can vary from 295 and 850 residues. This variations suggest that either ... Based on its conserved catalytic domains and its mechanism of catalysis, deubiquitinating enzymes are classified in the group ... All USP domains, including USP27X, can be divided into six conserved boxes that are mapped onto the USP domain core structure. ...
"Robust and tunable circadian rhythms from differentially sensitive catalytic domains". Proceedings of the National Academy of ... This leads to tight stacking of the CII domain to the CI domain. KaiB then binds to the exposed B loop on the CII domain of ... The CI and CII domains are linked by the N-terminal region of the CII domain. The last 20 residues from the C-terminal of the ... KaiC has two P loops or Walker's motif As (ATP-/GTP-binding motifs) in the CI and CII domains; the CI domain also contains two ...
PDZ domain binding. • cadherin binding. • peptidase activity. • beta-catenin binding. • protein binding. • calcium channel ... positive regulation of catalytic activity. • mitochondrial transport. • post-embryonic development. • positive regulation of ... Presenilin possesses a 9 transmembrane domain topology, with an extracellular C-terminus and a cytosolic N-terminus.[7][8] ... membrane protein intracellular domain proteolysis. • positive regulation of protein import into nucleus. • ephrin receptor ...
VPg domain) contacting the upper stem and the 3D domains (VPg domain) contacting the lower stem. Step 2: The 3C dimer opens the ... and mutations within the VPg sequence can severely diminish RdRp catalytic activity. While the tyrosine hydroxyl of VPg can ... Step 1: Two 3CD (VPg complex) molecules bind to CRE with the 3C domains ( ... "Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins". J. Virol. 87 (10): ...
Catalytic bead sensor. *Chemical field-effect transistor. *Electrochemical gas sensor. *Electrolyte-insulator-semiconductor ...
... in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain". Br. J. Haematol. 90 (4), 910-5. o. DOI: ...
This article incorporates text from the United States National Library of Medicine, which is in the public domain. ... catalytic activity. • transferase activity, transferring acyl groups. • 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding ...
"for their discovery of catalytic properties of RNA"[۳۳] ۱۹۹۲ رادولف مارکوس[۱] United States "for his contributions to the ... "for having extended the domain of microeconomic analysis to a wide range of human behaviour and interaction, including ... "for their discovery of the course of the catalytic conversion of گلیکوژن"[۴۸] ...
Moreover, superoxide dismutase has the largest kcat/KM (an approximation of catalytic efficiency) of any known enzyme (~7 x 109 ... Iron/manganese superoxide dismutases, alpha-hairpin domain. Structure of domain1 (color), human mitochondrial Mn superoxide ... Iron/manganese superoxide dismutases, C-terminal domain. Structure of domain2 (color), human mitochondrial Mn superoxide ...
Through the process of viral infection into hosts the three domains of life evolved.[83][84] Another interesting proposal is ... After only a few weeks, a DNAzyme with significant catalytic activity had evolved.[33] In general, DNA is much more chemically ... Patrick Forterre has been working on a novel hypothesis, called "three viruses, three domains":[83] that viruses were ... The RNA world hypothesis is supported by the observations that ribosomes are ribozymes: the catalytic site is composed of RNA, ...
... domains. The UBL domains are recognized by the 19S proteasome caps and the UBA domains bind ubiquitin via three-helix bundles. ... Sakata E, Stengel F, Fukunaga K, Zhou M, Saeki Y, Förster F, Baumeister W, Tanaka K, Robinson CV (June 2011). "The catalytic ... In mammals, the β1, β2, and β5 subunits are catalytic; although they share a common mechanism, they have three distinct ... Each catalytic β subunit also possesses a conserved lysine residue required for proteolysis.[22] ...
"Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains" ... The HIFalpha prolyl hydroxylases, termed PHDs/EGLNs (prolyl hydroxylase domain proteins/EGL nine homologues), bind to a ...
Catalytic bead sensor. *Chemical field-effect transistor. *Electrochemical gas sensor. *Electrolyte-insulator-semiconductor ...
It is a catalytic subunit of the protein kinase complex that is important for cell cycle G1 phase progression. The activity of ... 1996). "Germline mutations in the p16INK4a binding domain of CDK4 in familial melanoma". Nat. Genet. 12 (1): 97-9. doi:10.1038/ ...
... a C-terminal VCA domain and central B and GBD (GTP binding domain) domains. WASp, is expressed exclusively in hematopoietic ... regulation of catalytic activity. • Rho protein signal transduction. • regulation of actin polymerization or depolymerization. ... the central domain (C) was once thought to bind cofilin but is now believed to enhance the interactions between the V domains ... domain where they interact with actin nucleating complex (ARP2/3) and they differ in their terminal domains. WASp and N-WASP ...
... a catalytic core domain (RNaseH fold) a C-terminal DNA-binding domain (SH3 fold) Crystal and NMR structures of the individual ... All retroviral IN proteins contain three canonical domains, connected by flexible linkers: an N-terminal HH-CC zinc-binding ... Biochemical data and structural data suggest that retroviral IN functions as a tetramer (dimer-of-dimers). All three domains ... domains and 2-domain constructs of integrases from HIV-1, HIV-2, SIV, and Rous Sarcoma Virus (RSV) have been reported, with the ...
ERG-associated protein with SET domain (ESET)), which targets and trimethylates H3-K9 residues.[82] It's proposed that this ... "Additive neuroprotective effects of a histone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of ... "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors". primary. The Journal of Cell Biology. 191 (2): ... via interference of transcription factor binding and recruitment of transcriptional repressors with methyl binding domains. ...
catalytic activity mol⋅s−1. Notes. 1. The table is ordered so that a derived unit is listed after the units upon which its ... but it was outside its domain to publish recommendations for other quantities. Beginning in about 1900, physicists who had been ...
The human protein structure consists of a globular domain with three α-helices and a two-strand antiparallel β-sheet, an NH2- ... negative regulation of catalytic activity. • positive regulation of neuron apoptotic process. • regulation of peptidyl-tyrosine ... binding domain via nitrogen atoms in the histidine imidazole side-chains and deprotonated amide nitrogens from the 2nd and 3rd ...
There are currently no therapeutic approaches targeting CASS4, and in the absence of a catalytic domain and no extracellular ... Figure 1. Interaction network and domain structure scheme of Cass4. SH3 domain (SH3) preceded by a short region with no defined ... domain.[8] For the better studied members of the CAS family (BCAR1 and NEDD9), all of these domains have been defined as ... It also lacks a YDYVHL sequence at the N-terminal end of the FAT-like carboxy-terminal domain, even though this motif is ...
GO:0048554 positive regulation of catalytic activity. • positive regulation of glycogen biosynthetic process. • positive ... "Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF ...
Hanks SK, Quinn AM (1991). "Protein kinase catalytic domain sequence database: identification of conserved features of primary ... "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification". FASEB J ... "Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase". Science 253 (5018): 407 ...
... an aaRS consists of a catalytic domain (where both the above reactions take place) and an anticodon binding domain (which ... Noncatalytic domains[edit]. The novel domain additions to aaRS genes are accretive and progressive up the Tree of Life.[18][19] ... The catalytic domains of all the aaRSs of a given class are found to be homologous to one another, whereas class I and class II ... As genetic efficiency evolved in higher organisms, 13 new domains with no obvious association with the catalytic activity of ...
catalytic step 2 spliceosome. • U4/U6 x U5 tri-snRNP complex. • spliceosomal complex. • U4 snRNP. • small nuclear ... 1d3b: CRYSTAL STRUCTURE OF THE D3B SUBCOMPLEX OF THE HUMAN CORE SNRNP DOMAIN AT 2.0A RESOLUTION ...
Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins ( ... Beebe, K.D., Shin, J.N., Peng, J., Chaudhury, C., Khera, J. and Pei, D.H. (2000). "Substrate recognition through a PDZ domain ...
... in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain". British Journal of Haematology. 90 (4): ... See also: Factor IX § Domain architecture. The first crystal structure of human factor Xa was deposited in May 1993. To date, ... The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site. Factor Xa ...
The catalytic domain of PRMTs consists of a SAM binding domain and substrate binding domain (about 310 amino acids in total).[5 ... A loop serving as the binding site for SAM links the N-terminal and the C-terminal domains of the Dot1 catalytic domain. The C- ... Min J, Feng Q, Li Z, Zhang Y, Xu RM (March 2003). "Structure of the catalytic domain of human DOT1L, a non-SET domain ... and the post-SET domains. The pre-SET and post-SET domains flank the SET domain on either side. The pre-SET region contains ...
... domains. Main article: Protein domain. Many proteins are composed of several protein domains, i.e. segments of a ... Gutteridge A, Thornton JM (November 2005). "Understanding nature's catalytic toolkit". Trends in Biochemical Sciences. 30 (11 ... Domains usually also have specific functions, such as enzymatic activities (e.g. kinase) or they serve as binding modules (e.g ... Short amino acid sequences within proteins often act as recognition sites for other proteins.[26] For instance, SH3 domains ...
1vzj: STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED ... Identification of residues involved in catalytic activity and in polypeptide folding.. J. Biol. Chem. 1992, 267 (25): 17640-8. ... Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and ...
Catalytic bead sensor. *Chemical field-effect transistor. *Electrochemical gas sensor. *Electrolyte-insulator-semiconductor ...
catalytic cracked gasoline, or catalytic cracked naphtha, produced with a catalytic cracker, has a moderate octane rating, high ... This article incorporates text from this source, which is in the public domain. ... In 1937, Eugene Houdry developed the Houdry process of catalytic cracking, which produced a high-octane base stock of gasoline ... reformate, produced in a catalytic reformer, has a high octane rating with high aromatic content and relatively low olefin ...
Note 3: An enzyme loses its catalytic activity when it is denaturized.[2] ... implications for oligomer formation by 3D domain swapping", J. Am. Chem. Soc., 132 (5): 1621-30, doi:10.1021/ja9081638, PMID ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Domain relationships *Phosphatidylinositol 3-/4-kinase, catalytic domain (IPR000403) *PI3Kalpha, catalytic domain (IPR037704) ... Protein kinase-like domain superfamily (IPR011009). *Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily (IPR036940) ... a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Domain relationships *Peptidase family A1 domain (IPR033121) *Aspergillopepsin-like catalytic domain (IPR034163) ... Aspergillopepsin-like catalytic domain (IPR034163). Short name: Aspergillopepsin-like_cat_dom Overlapping homologous ... The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the ...
An important difference between the two is that the Cdc25B domain binds oxyanions in the catalytic site while that of Cdc25A ... A series of minimal domain Cdc25B constructs maintaining catalytic activity have been expressed. The structure of a minimum ... A series of minimal domain Cdc25B constructs maintaining catalytic activity have been expressed. The structu ... ... Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle.. Reynolds, R.A., Yem ...
The catalytic domain (CD) of the E2o component catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl ... A third catalytic residue (Asp379) assumes a conformation similar to the corresponding residue in E2pCD (Asn614), but different ... E2oCD has been solved to 3.0 A resolution using molecular replacement phases derived from the structure of the catalytic domain ...
... the catalytic domain remains either undetermined or ambiguous. Characterization of the catalytic domain in these superfamilies ... The catalytic domain of all eukaryotic cut-and-paste transposase superfamilies Message Subject (Your Name) has sent you a ... The catalytic domain of all eukaryotic cut-and-paste transposase superfamilies. Yao-Wu Yuan and Susan R. Wessler ... A catalytic domain signified by an acidic amino acid triad, known as the "DDE/D" motif, has been unambiguously identified in ...
Catalytic domain used in Immunocytochemistry/ Immunofluorescence. Abcam provides excellent in-house scientific support ...
GC-A contains an ANF-binding domain in the extracellular region and a kinase-like domain and catalytic domain in the ... catalytic domain).4 Since the catalytic domain of guanylate cyclase (GC-c) can be functionally expressed as a soluble protein ... The catalytic domain plus a portion of the kinase-like domain of GC-A (293 amino acids) have been expressed in Escherichia coli ... Recently, we have further shown that the catalytic domain plus three amino acids from the kinase-like domain of GC-A (242 amino ...
Chimeric Proteins Suggest That the Catalytic and/or C-Terminal Domains Give CesA1 and CesA3 Access to Their Specific Sites in ... Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains. Isaac ... Lack of activation of the two-hybrid system by the Zn domain fused to the GAL4 activating domain (Fig. 2A, 4 and 5) further ... As for the yeast two-hybrid system, this domain of CesA1 can interact with itself (Fig. 2B, lane 5) or with the similar domain ...
Following domains in our database have detailed information on amino acids needed for their catalytic activity. When any of ... these domains appear in the sequences analyzed, the domain annotation pages will show a detailed report on the catalytic ...
... which binds the PP1 catalytic domain, and its SH3 domain, which engages the PP1 C-terminal tail. The ASPP2 SH3 domain can ... ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail.. Bertran MT1, Mouilleron ... c Close-up view of ASPP2 Ankyrin1 domain interaction with PP1. d The PP1α PPII motif binds to ASSP2 SH3 domain. The three core ... c The SH3 domain of ASPP is required for binding to PP1α96A and PP1β9C. The W987K mutation in the ASPP SH3 domain (ASPPWK) ...
Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ...
Computer model showing the structure of the catalytic domain of eukaryotic guanylate cyclase (green, blue). PO4 residues shown ... Caption: Catalytic domain of eukaryotic guanylate cyclase. Computer model showing the structure of the catalytic domain of ... Keywords: art, artwork, biochemical, biochemistry, biological, biology, black background, catalytic, compound, cyclase, ...
434c) Rectangular Geometry of Catalytic Pore Domains for Electrochemical Systems: Role of the Deviations From "Ideality". ... The study of catalytic pore in electrochemical systems is vital in determine the effectiveness region and acceptable pore size ... This study will, for example, exemplify the role of the use of idealized geometrical domains (and their accuracy) in the ...
... little study has been directed away from the prototypical functional elements of the kinase domain. We have performed a s … ... The role of conserved water molecules in the catalytic domain of protein kinases Proteins. 2009 Aug 15;76(3):527-35. doi: ... little study has been directed away from the prototypical functional elements of the kinase domain. We have performed a ... simulations demonstrated that these waters confer a great deal of stability to their local environment and to a key catalytic ...
... catalytic domain superfamily including the families contained in it. Additional information provided includes InterPro ... annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations ... Metalloproteases ("zincins"), catalytic domain superfamily. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [. 0] (11) ... There are 56 hidden Markov models representing the Metalloproteases ("zincins"), catalytic domain superfamily. Information on ...
... that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts ... Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.. [Erandi Lira- ... cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain ... dictated by conformational heterogeneity and relies on a flexible linker located between the catalytic and the lectin domains. ...
The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ...
... domain combinations, taxonomic visualisation and hidden Markov model information. ... The SCOP classification for the Adenylyl and guanylyl cyclase catalytic domain family. Additional information, provided for ... Adenylyl and guanylyl cyclase catalytic domain family. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [. 0] (11) ... Browse and view proteins in genomes which have different domain combinations including a Nucleotide cyclase domain. ...
They are related by virtue of their kinase domains (also known as catalytic domains), which consist of approximately 250-300 ... The kinase domains that define this group of enzymes contain 12 conserv … ... They are related by virtue of their kinase domains (also known as catalytic domains), which consist of approximately 250-300 ... The kinase domains that define this group of enzymes contain 12 conserved subdomains that fold into a common catalytic core ...
Since this product is a truncated protein and does not contain intracellular catalytic activity domain, it is not suitable for ... PDGFRA Recombinant Human Protein (without Catalytic Activity Domain), His Tag, Invitrogen™ Sino Biological™ 50ug ... PDGFRA Recombinant Human Protein (without Catalytic Activity Domain), His Tag, Invitrogen™ Sino Biological™ ... This recombinant protein was expressed from a DNA sequence encoding the extracellular domain (Met 1-Glu 524) of human PDGFRA ( ...
Inhibition of human HGK catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence- ...
Pseudokinase domains are similar to kinase domains, but they lack catalytic activity. Although many domains originally ... The pseudokinase domains of guanylyl cyclase-A and -B allosterically increase the affinity of their catalytic domains for ... The pseudokinase domains of guanylyl cyclase-A and -B allosterically increase the affinity of their catalytic domains for ... The pseudokinase domains of guanylyl cyclase-A and -B allosterically increase the affinity of their catalytic domains for ...
It is established that the catalytic domain of PCSK9 (aa153-421) and the EGF-A domain of LDL-R (aa314-355) are involved in the ... LDL-R promoting activity of peptides derived from human PCSK9 catalytic domain (153-421): design, synthesis and biochemical ... The major goal of this study is to identify peptide/s from the catalytic domain of hPCSK9 that can block the binding of hPCSK9 ... It is proposed that LDL-R promoting activity of this and other selected PCSK9 catalytic peptides such as P36, P37, P46 and P47 ...
... catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR-iPKS) for the first time and ... A cis-acting enoyl reductase (ER) catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR ... Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide ... Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide ...
The catalytic domain was overexpressed in Escherichia coli, and using a two-step procedure, it was possible to isolate ... 2014) The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers. Plant Cell 26: 2996- ... To gain deeper insight into the structure and role of the catalytic domain of CESA in rosette formation, we carried out a ... Comparison of the size of the catalytic domain trimer with dimensions of rosette CSCs obtained from TEM studies strongly ...
Inhibition of human CK1D catalytic domain expressed in Escherichia coli cell assessed as substrate phosphorylation using ...
Both catalytic domains in SPs 6, 80, 86, 126, and 176 (N and C) were included in this analysis. Construction of a phylogenetic ... Phylogenetic analysis of the catalytic domains of 193 Drosophila SPs and SPHs. ... Phylogenetic analysis of the catalytic domains of 193 Drosophila SPs and SPHs. ... sequence alignment and phylogenetic analysis of the catalytic or protease-like domains of 193 Drosophila SPs and SPHs were ...
Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger. / Stoffer, B; ... title = "Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger", ... T1 - Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger ... Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger. ...
The catalytic subunit of ISW2 consists of the ATPase domain and three domains at the C-terminus called HAND, SANT and SLIDE ( ... HSS) domains. The individual roles of each HSS domains and how they coordinate with the ATPase domain during remodeling are not ... In summary, the understandings of Isw2 ATPase domain and C-terminus domains support the assumption that there is no redundancy ... The biochemical characteristics of ATPase domain mutations and structure comparison with solved ISWI ATPase domain indicate the ...
  • Specificity is determined by nearest-neighbour hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. (ebi.ac.uk)
  • The Cdc25B constructs, with various truncations of the C-terminal residues, are shown to have potent catalytic activity. (rcsb.org)
  • Furthermore, we identified additional highly conserved amino acid residues or motifs within the DDE/D domain that together form a "signature string" that is specific to each superfamily. (pnas.org)
  • When any of these domains appear in the sequences analyzed, the domain annotation pages will show a detailed report on the catalytic residues. (embl-heidelberg.de)
  • Using the A. thaliana dek1-3 complementation assay, we show that four conserved amino acid residues of two Ca²⁺-binding sites in the CysPc domain of classical calpains are conserved in land plants and functionally essential in A. thaliana DEK1. (nih.gov)
  • Molecular modeling indicated that all the residues of the ATP-binding site of the prototypical kinase PKA, except the catalytic aspartate, are conserved in the PKDs of GC-A and GC-B. Kinase-inactivating alanine substitutions for the invariant lysine in subdomain II or the aspartate in the DYG-loop of GC-A and GC-B failed to decrease enzyme phosphate content, consistent with the PKDs lacking kinase activity. (sciencemag.org)
  • A mutagenesis approach was taken to address the functions of specific conserved tyrosine residues within these catalytic and juxtamembrane domains. (asm.org)
  • Tandem mass spectrometry experiments confirmed autophosphorylation of the two juxtamembrane tyrosine residues and also identified a tyrosine within the kinase domain activation segment as a phosphorylation site. (asm.org)
  • Together, our data suggest that the catalytic and therefore biological activities of Eph receptors are controlled by a two-component inhibitory mechanism, which is released by phosphorylation of the juxtamembrane and activation segment tyrosine residues. (asm.org)
  • We deleted SANT domain (ΔSANT) and also created mutations in three basic amino acid residues (mSANT) on the surface of SANT domain predicted to be interacting with nucleosomal DNA. (siu.edu)
  • Residues in the Isw2 ATPase domain acidic patch as identified in previous studies have been selected and mutated to examine the effects. (siu.edu)
  • To identify potential catalytic residues, we generated site-directed mutations in recombinant BjCHI3. (deepdyve.com)
  • We report here 500 pico seconds (ps) molecular dynamics (MD) simulation results on two molecules of 4-acetylamino-5-hydroxy naphthalene 2-7disulfonic acid (Y-3) in the catalytic domain (residues 54-199) of avian sarcoma virus integrase (ASV-IN) dimer. (jbsdonline.com)
  • On the basis of amino acid sequence alignments and structural data of related enzymes, we have performed a mutational analysis of 14 amino acid residues in the catalytic domain of the murine Dnmt3a DNA-(cytosine C5)-methyltransferase. (cf.ac.uk)
  • The target residues are located within the ten conserved amino acid sequence motifs characteristic for cytosine-C5 methyltransferases and in the putative DNA recognition domain of the enzyme (TRD). (cf.ac.uk)
  • In addition, we performed a detailed structural and functional study of this domain in which we identified key residues required for its activity. (ox.ac.uk)
  • Search strategies based on conserved and functionally assigned amino acid (AA) residues in the catalytic center of known NCs [ 7 ] have now opened the way to a systematic search of NCs in higher plants and has led to the discovery of a number of Arabidopsis thaliana candidate molecules with catalytic activity in vitro and in vivo . (biomedcentral.com)
  • The importance of the C-terminal domain and its residues 218 and 258 that are different between the two PGTs was assessed via structure-guided domain swapping or single and dual amino acid substitutions. (kpubs.org)
  • The results strongly support essential role of the C-terminal domain and the two residues for catalysis as well as sugar donor specificity, bringing insight into the structural features of the PGTs. (kpubs.org)
  • As it was speculated that the amino acid residues different between them in the C-terminal domain would be responsible for the sugar donor specificity, we prepared here 2 chimeric enzymes via domain swapping of the C-terminal and 6 single and dual amino acid substitution mutants via site-directed mutagenesis and determined the activity towards various UDP-sugars. (kpubs.org)
  • We substituted alanine for each of these residues and determined that an interaction with multiple residues of the N-terminal domain is responsible for the mutator phenotype. (bris.ac.uk)
  • The structural model of the catalytic D4 domain of HVAP-1 reveals that all components necessary for enzymatic monoamine oxidase activity are indeed present within the HVAP-1 and pinpoints residues that may be key to substrate entry through a channel to the active site and residues likely to be involved in substrate specificity as well as structural features critical to dimer formation. (abo.fi)
  • Except for a few members of the CslD family, the closest ancestors to the CesA genes and some of which may function in cellulose synthesis in tip-growing cells, these domains are notably lacking in the other members of the CesA superfamily ( 3 , 19 ). (pnas.org)
  • Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-YIG superfamily member, using NMR restraints and Monte Carlo dynamics. (dbcls.jp)
  • Phylogenetic analysis of the catalytic domains of 193 Drosophila SPs and SPHs. (okstate.edu)
  • To obtain an overview of this SP-related protein family, sequence alignment and phylogenetic analysis of the catalytic or protease-like domains of 193 Drosophila SPs and SPHs were performed as described in Materials and Methods. (okstate.edu)
  • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. (readabstracts.com)
  • A series of minimal domain Cdc25B constructs maintaining catalytic activity have been expressed. (rcsb.org)
  • Each of the lobes provides a catalytic Asp residue, positioned within the hallmark motif Asp-Thr/Ser-Gly, to the active site. (ebi.ac.uk)
  • The catalytic cysteine residue, Cys473, can be oxidized to form a disulfide linkage to Cys426. (rcsb.org)
  • A third catalytic residue (Asp379) assumes a conformation similar to the corresponding residue in E2pCD (Asn614), but different from its counterpart in CAT (Asp199). (rcsb.org)
  • Molecular dynamics simulations demonstrated that these waters confer a great deal of stability to their local environment and to a key catalytic residue. (nih.gov)
  • Subtilisin Carlsberg, in addition, produces a type of domain which is hydrolysed before Ser-444, an O-glycosylated residue. (biochemj.org)
  • Mutation in the predicted catalytic base residue, D834E of NBD1, altered NBD1 ATPase activity disrupting potentiation of catalytic behavior in the NBD1/NBD2 interactome. (elsevier.com)
  • Families of aspartic peptidases, and those of unknown catalytic mechanism. (ebi.ac.uk)
  • These structural and biochemical analyses, combined with molecular modeling, provide mechanistic insights into the catalytic mechanism and nucleosomal specificity of Dot1 proteins. (mendeley.com)
  • Here we present the first crystal structures of complexes of GalNAc-T2 with glycopeptides that together with enhanced sampling molecular dynamics simulations demonstrate a cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain. (sigmaaldrich.com)
  • Thus, the pseudokinase domains of GC-A and GC-B promote the catalytic activity of these receptors through an allosteric mechanism that is conserved with catalytically active kinases. (sciencemag.org)
  • In this study we focused on the SANT domain and found other mechanism of regulation that are independent of the H4 tail. (siu.edu)
  • The absence of SANT domain affected ISW2 activity neither through ATP hydrolysis nor DNA translocation, but in the mechanism of remodeling process. (siu.edu)
  • Structures of the Human Poly (Adp-Ribose) Glycohydrolase Catalytic Domain Confirm Catalytic Mechanism and Explain Inhibition by Adp-Hpd Derivatives. (nih.gov)
  • Currently, only one crystal structure of the enzyme is available, and the most widely accepted reaction mechanism is a hypothetical one, mostly derived from the functions of enzymes related to reverse gyrase domains. (unibas.ch)
  • Together with the finding of new conformational states via smFRET, and "targeted" supercoiling assays with the full-length enzyme, we end up proposing a detailed catalytic mechanism, similar to the one derived from the reverse gyrase structure, only this time based on and supported by a combination of kinetic, thermodynamic, and structural data. (unibas.ch)
  • Recombinant catalytic domains of rice ( Oryza sativa ) CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. (plantcell.org)
  • To explore the properties of multi-domain BjCHI1, we have expressed recombinant BjCHI1 and two derivatives, which lack one (BjCHI2) or both (BjCHI3) chitin-binding domains, as secreted proteins in Pichia pastoris. (deepdyve.com)
  • Secondly, recombinant peptides containing the GC domain need to be tested in in vitro GC assays such as the enzyme-linked immune-sorbent assay (ELISA) and/or in mass spectrometry based cGMP assays. (biomedcentral.com)
  • We have engineered and produced recombinant proteins of the matriptase protease domain, and have determined the crystal structures of the protease:SFTI-1 complex at 2.0 Å as well as the protease:benzamidine complex at 1.2 Å. (biomedcentral.com)
  • Here, nanoscale protein topography mapped assembly of monodisperse purified recombinant SUR2A NBD1/NBD2 domains, precharacterized by dynamic light scattering. (elsevier.com)
  • Abstract Guanylate cyclase-A, the receptor for atrial natriuretic factor, contains a protein kinase-like domain and a catalytic domain in the intracellular region. (ahajournals.org)
  • GC-A contains an ANF-binding domain in the extracellular region and a kinase-like domain and catalytic domain in the intracellular region. (ahajournals.org)
  • Since this product is a truncated protein and does not contain intracellular catalytic activity domain, it is not suitable for use in enzyme activity studies. (fishersci.ca)
  • Natriuretic peptides regulate multiple physiologic systems by activating transmembrane receptors containing intracellular guanylyl cyclase domains, such as GC-A and GC-B, also known as Npr1 and Npr2, respectively. (sciencemag.org)
  • Both enzymes contain an intracellular, phosphorylated pseudokinase domain (PKD) critical for activation of the C-terminal cGMP-synthesizing guanylyl cyclase domain. (sciencemag.org)
  • PSKR belongs to a family of NCs that contains the GC catalytic center embedded within the intracellular kinase domain of leucine rich repeat receptor-like molecules and in in vitro experiments we have demonstrated that both the kinase and the GC domain have catalytic activity. (biomedcentral.com)
  • Most RPTPs have two homologous intracellular domains but only the membrane proximal one is catalytically active. (biochim.ro)
  • Point mutations in the purine-binding site of the catalytic domain abolished GC activity but not allosteric activation. (sciencemag.org)
  • Mutations designed to rigidify the conserved regulatory or catalytic spines within the PKDs increased guanylyl cyclase activity, increased sensitivity to natriuretic peptide, or reduced the Michaelis constant in the absence of ATP, consistent with ATP binding stabilizing the PKD in a conformation analogous to that of catalytically active kinases. (sciencemag.org)
  • The biochemical characteristics of ATPase domain mutations and structure comparison with solved ISWI ATPase domain indicate the acidic patch is unlikely to interact with DNA as predicted previously. (siu.edu)
  • Furthermore, a G990E replacement in the catalytic domain conferred Set1 hyperactivity and restored trimethylation to a Set1 derivative bearing mutations in the RRM domain. (embopress.org)
  • Mutations in the catalytic domain of factor IX that are relate. (mysciencework.com)
  • Mutations in the catalytic domain of factor IX that are related to the subclass hemophilia Bm. (mysciencework.com)
  • Structural stability of human protein tyrosine phosphatase ρ catalytic domain: effect of point mutations. (ox.ac.uk)
  • One approach in this direction is to study the effect of the mutations and investigate if critical properties of the protein are affected, as done here with three mutations reported to occur in the catalytic SET domain of MLL3. (biomedcentral.com)
  • Our data indicate that somatic mutations in the SET domain of MLL3 alter its catalytic properties indicating that the mutations might contribute to carcinogenesis in a distinct mutation-specific manner. (biomedcentral.com)
  • Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII. (unife.it)
  • Four missense mutations located in the catalytic domain of factor VII were found. (unife.it)
  • Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. (ebi.ac.uk)
  • The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. (ebi.ac.uk)
  • Homology modeling must include substrate docking that can provide support for the structural feasibility of the GC catalytic centers in those candidates. (biomedcentral.com)
  • Matrix metalloproteinases share high protein sequence homology and have defined domain structures. (elsevier.com)
  • Somatic ACE1 contains two homologous catalytic domains: the N- and C-domain, which have different substrate specificities. (biomedcentral.com)
  • View conserved domains detected in this protein sequence using CD-search. (nih.gov)
  • The major obstacle is that the catalytic domain of GC-A does not contain G-x-G-x-x-G, the diagnostic consensus sequence of the nucleotide binding site that interacts with the phosphate chain of the nucleotide. (ahajournals.org)
  • R130A displayed a strong reduction in catalytic activity and a complete change in flanking sequence preferences, indicating that Arg130 has an important role in the DNA interaction of Dnmt3a. (cf.ac.uk)
  • Comparison of the structure of the guanylate cyclase domain with the known structures of adenylate cyclases confirms the close similarity in architecture between these two enzymes, as expected from their sequence similarity. (biomedcentral.com)
  • Both classes of guanylate cyclase share a catalytic module that is closely related in sequence to that of mammalian adenylate cyclases. (biomedcentral.com)
  • It is expected that sequence of the ancestor PTP catalytic domain and its characteristics will consistently contribute to our understanding of the evolution of PTPs and the physiological function of the ancestor PTP. (biochim.ro)
  • We explored the effect of amino acid substitutions in a region of the highly conserved sequence motif B in the fingers domain on replication fidelity. (bris.ac.uk)
  • We also show that a flexible, positively charged region at the C terminus of the catalytic domain is critical for nucleosome binding and enzymatic activity. (mendeley.com)
  • Since mutation of Leu 817 to Arg abolishes the catalytic activity, Leu 817 is likely located near the active site of guanylate cyclase-A. These results demonstrate that the carboxyl fragment of guanylate cyclase-A is an ideal system for studying the active site of guanylate cyclase-A. (ahajournals.org)
  • Following domains in our database have detailed information on amino acids needed for their catalytic activity. (embl-heidelberg.de)
  • Our model indicates that the activity profile of GalNAc-T2 is dictated by conformational heterogeneity and relies on a flexible linker located between the catalytic and the lectin domains. (sigmaaldrich.com)
  • LDL-R promoting activity of peptides derived from human PCSK9 catalytic domain (153-421): design, synthesis and biochemical evaluation. (sigmaaldrich.com)
  • It is proposed that LDL-R promoting activity of this and other selected PCSK9 catalytic peptides such as P36, P37, P46 and P47 are most likely mediated via intervention of PCSK9:LDL-R complex formation. (sigmaaldrich.com)
  • Coexpression of inactive mutants produced half the activity expected for symmetric catalytic dimers. (sciencemag.org)
  • Pseudokinase domains are similar to kinase domains, but they lack catalytic activity. (sciencemag.org)
  • Although many domains originally classified as pseudokinases were subsequently shown to have limited or context-dependent kinase activity, some act as scaffolds or allosteric regulators. (sciencemag.org)
  • Ligand stimulation of wild-type EphB2 in neuronal NG108-15 cells resulted in an upregulation of catalytic activity and an increase in cellular tyrosine phosphorylation, accompanied by a retraction of neuritic processes. (asm.org)
  • We studied hTERT proteins containing N-terminal deletions or substitutions to identify and characterize hTERT domains mediating telomerase catalytic activity, hTR binding, and hTERT multimerization. (asm.org)
  • We provide evidence that SANT domain regulated ISW2 activity without affecting ATPase and DNA translocation activity and was dependent on conformation changes of histone octamers instead of histone H4 tail. (siu.edu)
  • By fusing GPB to the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) catalytic domain of the PlyC lysin, we constructed a novel chimeric lysin, ClyJ, with improved activity to the pneumococcal Cpl-1 lysin. (asm.org)
  • Esterification of free fatty acids in natural oils and fats was used to probe the catalytic activity of the synthesized acid-modified mesoporous catalysts. (iastate.edu)
  • Set1 also bears several conserved domains with uncharacterized contributions to activity. (embopress.org)
  • The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. (escholarship.org)
  • The kinase activity is regulated in the platform of chemotaxis signaling complexes formed by CheW, chemoreceptors, and the regulatory domain of CheA. (escholarship.org)
  • N167A (motif VI) and R202A (motif VIII) have normal AdoMet and DNA binding but reduced catalytic activity. (cf.ac.uk)
  • Insertion of endocellulase catalytic domains into thermostable consensus ankyrin scaffolds: effects on stability and cellulolytic activity. (dbcls.jp)
  • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects. (dbcls.jp)
  • Hydrogen production tests confirmed the improved catalytic activity of CdSe/CdS dimers, which was enhanced 3-4 times upon etching treatment. (edu.lb)
  • We report novel findings in post mortem AD brain tissue, using novel immunocapture-based enzyme activity assays, that the activity of the two catalytic domains of ACE1 are significantly altered in opposing directions in AD. (biomedcentral.com)
  • ACE1 C-domain and N-domain activity was measured by immunocapture-based FRET assays. (biomedcentral.com)
  • ACE1 C-domain activity was significantly elevated in AD by 25.85% (median = 30,407 rfu in AD compared to median = 24,161 rfu in controls) ( p = 0.018) (Fig. 1 a). (biomedcentral.com)
  • Binding of Mn 2+ to the active site is essential for the catalytic activity of RepB. (frontiersin.org)
  • This transition, which is also shown to result in loss of DNA binding capacity and catalytic activity of RepB, is confined to its N-terminal domain. (frontiersin.org)
  • The level of catalytic activity of the protein, especially in the case of full-length RepB, cannot be explained based only on the high-affinity binding of Mn 2+ at the active site and suggests the existence of additional, lower-affinity metal binding site(s), missing in the separate catalytic domain, that must also be saturated for maximal activity. (frontiersin.org)
  • These results show that, starting with an activity for adenylate synthesis, barriers are relatively low for building catalytic units for aminoacylation of RNA helices. (scripps.edu)
  • We reconciled these differences by demonstrating that the presence of the putative N-terminal Zn-finger in the helicase-like domain construct is the cause for the decreased activity. (unibas.ch)
  • Finally, our pre steady-state kinetic studies allowed us to fully describe the unstimulated ATPase activity of the isolated helicase-like domain. (unibas.ch)
  • Catalytic activity and selectivity were altered in all the mutants (2 chimeric and 6 substitution) to accept both UDP-glucose and UDP-xylose. (kpubs.org)
  • Two of them led to massive changes of the enzymatic properties in vitro and in cells - N4848S abolished the catalytic activity and Y4884C changed the product pattern of the enzyme leading to increased generation of H3K4me2 and me3, while the MLL3 wild-type only deposits H3K4 monomethylation. (biomedcentral.com)
  • Thus, NBD1/NBD2 assembly, resolved by a panel of proteomic approaches, provides a molecular substrate that determines the optimal catalytic activity in SUR2A, establishing a paradigm for the structure-function relationship within the K ATP channel complex. (elsevier.com)
  • We also provide evidence that the herbicide CGA 325′615 (Syngenta, Basel), which inhibits synthesis of crystalline cellulose and leads to a disruption of rosette architecture, may affect the oxidative state of the zinc-finger domain that is necessary for rosette stability. (pnas.org)
  • Organic-inorganic hybrid mesoporous silicas were synthesized via nonionic supramolecular assembly using the co-condensation synthesis technique with the intention of understanding the catalytic domain as well as developing strategies to control the catalytic functionalities at the molecular level. (iastate.edu)
  • The class-defining domain of a tRNA synthetase is closely related to the primordial enzyme that catalyzed synthesis of aminoacyl adenylate. (scripps.edu)
  • Synthesis of the ancestral PTP catalytic domain and its characterization both in vitro and in vivo. (biochim.ro)
  • 3 4 However, although the catalytic domain of GC-A has been assigned to a 239-amino acid region, 4 the exact location of the active site (or the catalytic cavity) is still unknown. (ahajournals.org)
  • Incorporation of hydrophobic groups into the organic-inorganic acid catalyst enhanced the catalytic conversion of the fatty acids, although the catalytic performance of the resulting catalyst strongly depended on the incorporation technique as well as the size of the hydrophobic organic groups. (iastate.edu)
  • One notable characteristic of all of the CesA proteins is the presence of two zinc-finger domains located within the cytoplasmic N-terminal region of the proteins. (pnas.org)
  • This discovery was significant, as many SET domain proteins had been identified as transcriptional regulators, but their mode of action was not understood. (embopress.org)
  • Mutant proteins were purified and tested for their catalytic properties and their abilities to bind DNA and AdoMet. (cf.ac.uk)
  • OXR1 contains the Tre2/Bub2/Cdc16 (TBC), lysin motif (LysM), domain catalytic (TLDc) domain, a motif present in a family of proteins including TBC1 domain family member 24 (TBC1D24), a protein mutated in a range of disorders characterized by seizures, hearing loss, and neurodegeneration. (ox.ac.uk)
  • To understand the role of this domain in the stress response, we carried out systematic analysis of all mammalian TLDc domain-containing proteins, investigating their expression and neuroprotective properties in parallel. (ox.ac.uk)
  • Our data demonstrate that the integrity of the TLDc domain is essential for conferring neuroprotection, an important step in understanding the functional significance of all TLDc domain-containing proteins in the cellular stress response and disease. (ox.ac.uk)
  • The T domain of diphtheria toxin is known to participate in the pH- dependent translocation of the catalytic C domain of the toxin across the endosomal membrane, but how it does so, and whether cellular proteins are also required for this process, remain unknown. (elsevier.com)
  • Here, we report results showing that the T domain alone is capable of translocating the entire C domain across model, planar phospholipid bilayers in the absence of other proteins. (elsevier.com)
  • Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional characterization of these newly identified family members. (sciencemag.org)
  • Cloning, expression, purification, and characterization of the catalytic domain of sika deer MMP-13. (dbcls.jp)
  • Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1. (dbcls.jp)
  • Characterization of the catalytic domains of Trichoderma reesei endoglucanase I, II, and III, expressed in Escherichia coli. (dbcls.jp)
  • In Cdc25B, both sulfate and tungstate anions are shown to bind in the catalytic site containing the signature motif (HCxxxxxR) in a conformation similar to that of other protein tyrosine phosphatases and dual specificity phosphatases, with the exception of the Cdc25A. (rcsb.org)
  • We identified two RNA interaction domains, RID1 and RID2, the latter containing a vertebrate-specific RNA binding motif. (asm.org)
  • The JmjC domain is a double-stranded β-helical (DSBH) fold also called the jelly-roll fold or double Greek motif. (nih.gov)
  • The Evolutionarily Conserved Tre2/Bub2/Cdc16 (TBC), Lysin Motif (LysM), Domain Catalytic (TLDc) Domain Is Neuroprotective against Oxidative Stress. (ox.ac.uk)
  • The arrangement of the catalytic domain within the CesA monomer and dimer provides a foundation for constructing structural models of the synthase complex and defining the relationship between the rosette structure and the cellulose microfibrils they synthesize. (plantcell.org)
  • Using modern nuclear magnetic resonance (NMR) techniques, we find that by interacting with the catalytic domain, the interdomain linker initiates long-range structural and dynamic changes directed toward the catalytic center of the autophosphorylation reaction. (escholarship.org)
  • Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase. (dbcls.jp)
  • This structural morphology is highly desirable for catalytic applications as it enables both reductive and oxidative reactions to occur simultaneously on dissimilar nanoparticle surfaces. (edu.lb)
  • The effects of SANT domain on ISW2 remodeling were analyzed by site-directed mapping at specific histone octamer positions to track nucleosomal DNA movement near the nucleosome entry/exit and DNA translocation sites. (siu.edu)
  • The central cytoplasmic domain also contains a region that is relatively conserved between orthologs, called the class-specific region ( Vergara and Carpita, 2001 ). (plantphysiol.org)
  • We have investigated protein-protein interaction between distinct domains of the human CD45 cytoplasmic region using a yeast two-hybrid system. (elsevier.com)
  • Processing of metacaspase into a cytoplasmic catalytic domain mediating cell death in Leishmania major. (unil.ch)
  • Direct allosteric regulation between the GAF domain and catalytic domain of photoreceptor phosphodiesterase PDE6. (unh.edu)
  • Computer model showing the structure of the catalytic domain of eukaryotic guanylate cyclase (green, blue). (sciencephoto.com)
  • The natriuretic peptide receptors GC-A and GC-B contain both pseudokinase and guanylyl cyclase domains. (sciencemag.org)
  • found that the pseudokinase domains of GC-A and GC-B were allosteric regulators of the guanylyl cyclase domains. (sciencemag.org)
  • Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (p110alpha, beta, gamma or delta) and one of several regulatory subunits (p85alpha, beta or gamma). (ebi.ac.uk)
  • Here, we isolated dominant hyperactive SET1 D alleles, which revealed a complex interplay among Set1 regulatory domains. (embopress.org)
  • The PDE6 catalytic subunit contains a catalytic domain and regulatory GAF domains. (unh.edu)
  • The catalytic subunit responsible for glucan chain elongation is believed to be a plasma membrane glycosyltransferase named CesA (cellulose synthase). (pnas.org)
  • To investigate the active site (the catalytic cavity) of guanylate cyclase-A, we amplified the catalytic domain plus three amino acids from the kinase-like domain of guanylate cyclase-A (GC-c) with polymerase chain reaction (PCR) and expressed it in Escherichia coli . (ahajournals.org)
  • The cDNA corresponding to the catalytic domain of guanylate cyclase-A (bp 2673 to 3401) was amplified with PCR from a rat brain library (Clonetech). (ahajournals.org)
  • The guanylate cyclase catalytic module, for which no structure has been determined at present, is a class III nucleotide cyclase domain that is also found in mammalian membrane-bound guanylate and adenylate cyclases. (biomedcentral.com)
  • We have determined the crystal structure of the catalytic domain of a soluble guanylate cyclase from the green algae Chlamydomonas reinhardtii at 2.55 Å resolution, and show that it is a dimeric molecule. (biomedcentral.com)
  • The three-dimensional structure of a guanylate cyclase catalytic domain has not been reported. (biomedcentral.com)
  • Our results suggest that functional hTERT complementation requires intact RID2 and RT domains on the same hTERT molecule and is dependent on hTR and the N terminus. (asm.org)
  • The catalytic subunit of ISW2 consists of the ATPase domain and three domains at the C-terminus called HAND, SANT and SLIDE (HSS) domains. (siu.edu)
  • In summary, the understandings of Isw2 ATPase domain and C-terminus domains support the assumption that there is no redundancy of their roles in nucleosome remodeling. (siu.edu)
  • Mapping of the catalytic and epitopic sites of human CD38/NAD+ glycohydrolase to a functional domain in the carboxyl terminus. (semanticscholar.org)
  • Human SENP1 (catalytic domain aa 387-644) (Accession Nr. Q9P0U3 ) fused at the N-terminus to a His-tag. (adipogen.com)
  • alpha amylase, catalytic domain protein [Capnocytophaga sp. (nih.gov)
  • Using 51 synthetic linear peptides (P1-P51) of 15aa long with 10 amino acids overlapping sequences spanning the entire catalytic segment of hPCSK9 (aa153-421), we identified two domains of hPCSK9 namely (aa323-358) and (aa365-384) that exhibited strong binding affinity towards synthetic EGF-A peptide. (sigmaaldrich.com)
  • The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain. (plantcell.org)
  • Access to this repository is by a web server that compares user defined unknown sequences to these pre-defined profiles and outputs a list of predicted catalytic domains. (biomedcentral.com)
  • The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear. (sigmaaldrich.com)
  • Several stromelysin catalytic domain inhibitors inhibited the GCD with similar specificity. (elsevier.com)
  • The catalytic efficiency and substrate specificity under in vitro and in vivo conditions for all constructs will be evaluated and compared. (biochim.ro)
  • In addition, new insights into the role played by the molecular determinants of PTPs' catalytic efficiency and substrate specificity will be generated. (biochim.ro)
  • The GCD cleaved the fluorogenic peptides Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH 2 and Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH 2 with catalytic efficiency close to full length human gelatinase A. The reconstructed GCD cleaves not only thiopeptolide and peptide substrates but also protein substrates such as gelatin. (elsevier.com)
  • ATP bound to and stabilized the pseudokinase domain similarly to its stabilization of the active conformation of the prototypical kinase PKA. (sciencemag.org)
  • The catalytic domain (CD) of the E2o component catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A. The crystal structure of the Escherichia coli E2oCD has been solved to 3.0 A resolution using molecular replacement phases derived from the structure of the catalytic domain from the Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2pCD). (rcsb.org)
  • The catalytic domain plus a portion of the kinase-like domain of GC-A (293 amino acids) have been expressed in Escherichia coli . (ahajournals.org)
  • The catalytic domain was overexpressed in Escherichia coli , and using a two-step procedure, it was possible to isolate monomeric and trimeric forms of AtCESA1CatD. (plantphysiol.org)
  • Despite the number of crystal structures available, little study has been directed away from the prototypical functional elements of the kinase domain. (nih.gov)
  • Although Zn 2+ binding occurs only when the protein is in the reduced form, biochemical analyses show that under oxidative conditions, the GhCesA1 zinc-finger domain and also the full-length protein dimerize via intermolecular disulfide bonds, indicating CesA dimerization can be regulated by redox state. (pnas.org)
  • Several conserved domains of the CesA protein orthologs have been characterized (illustrated schematically in Fig. 1B ). (plantphysiol.org)
  • This configuration is in stark contrast to the domain organization obtained in predicted structures of plant CesA. (plantcell.org)
  • The structure of a minimum domain construct binding sulfate was determined at 1.9 A resolution and a temperature of 100 K. Other forms of the same co?nstruct were determined at lower resolution and room temperature. (rcsb.org)
  • The overall folding and structure of the domain is similar to that found for Cdc25A. (rcsb.org)
  • Structure of the catalytic domain. (mendeley.com)
  • We have solved a 2.5 Å resolution structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM). (mendeley.com)
  • The structure reveals a unique organization of a mainly α-helical N-terminal domain and a central open α/β structure, an active site consisting of a SAM binding pocket, and a potential lysine binding channel. (mendeley.com)
  • We show that this domain in GhCesA1 can bind two atoms of Zn 2+ , as predicted by its structure. (pnas.org)
  • In contrast to structure modeling predictions, solution x-ray scattering studies demonstrate that the monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. (plantcell.org)
  • This thesis reported the structure of an enzymatically active fragment of the dengue virus NTPase/ helicase C-terminal catalytic domain. (ntu.edu.sg)
  • The structure is composed of three domains, bears an asymmetric distribution of charges and comprises a tunnel large enough to accommodate single strand RNA. (ntu.edu.sg)
  • The TLDc domain is highly conserved across species, although the structure-function relationship is unknown. (ox.ac.uk)
  • A crystal structure of the catalytic domain of glucoamylase from A. niger with Tris and glycerol bound in the active site has been solved by molecular replacement and refined to 1.9 Å resolution. (iucr.org)
  • In this work, we have studied the effects of metal binding on the structure and thermostability of full-length hexameric RepB and each of its separate domains by using different biophysical approaches. (frontiersin.org)
  • The crystal structure of the family IIIa cellulose-binding domain (CBD) from the cellulosomal scaffoldin subunit of C. cellulolyticum was determined. (iucr.org)
  • They also revealed high flexibility of the linker joining the RecA domains with relative orientations far from random, and local differences in secondary structure motifs that discard the assumption of all reverse gyrases having a "monolithic" build-up. (unibas.ch)
  • These results are consistent with the notion that gelatinases have the same structure for the catalytic domain as other matrix metalloproteinases like stromelysins and collagenases. (elsevier.com)
  • The x-ray structure of the T domain from Xenopus laevis is reported, in complex with the 24-nucleotide palindromic DNA duplex. (readabstracts.com)
  • Thus, natriuretic peptide binding was required for communication of the allosteric activation signal to the catalytic site. (sciencemag.org)
  • 2′-Deoxy-ATP and 2′-deoxy-GTP were poor allosteric activators, but 2′-deoxy-GTP was an effective substrate, consistent with distinct binding requirements for the allosteric and catalytic sites. (sciencemag.org)
  • We conclude that membrane GC domains are asymmetric homodimers with distinct and reciprocally regulated catalytic and allosteric sites that bind to GTP and ATP, respectively. (sciencemag.org)
  • Unlike most GAF domain-containing cyclic nucleotide phosphodiesterases, little is known about direct allosteric communication of PDE6. (unh.edu)
  • In this study, we demonstrate for the first time direct, inter-domain allosteric communication between the GAF and catalytic domains in PDE6. (unh.edu)
  • Binding of the N-terminal half of Pgamma to the GAF domains suffices to induce this allosteric effect. (unh.edu)
  • Allosteric communication between GAF and catalytic domains is reciprocal, in that drug binding to the catalytic domain slowed cGMP dissociation from the GAF domain. (unh.edu)
  • We conclude that although Pgamma-mediated regulation plays the dominant role in visual excitation, the direct, inter-domain allosteric regulation described in this study may play a feedback role in light adaptational processes during phototransduction. (unh.edu)
  • Our combined data support a model in which the Ala-to-Gln substitution in the fingers domain of Pol δ results in an interaction with the N-terminal domain that affects the base selectivity of the enzyme. (bris.ac.uk)
  • The overall fold of the catalytic JmjC domain in iron- and 2-oxoglutarate-dependent histone demethylases and nucleotide hydroxylases(A) Jmj prototype member JmjD2A (PDB ID: 2OQ7) in complex with Ni2+ (which replaces the endogenous Fe2+) and the 2-oxoglutarate competitive inhibitor N-oxalyl glycine (NOG). (nih.gov)
  • The catalytic domain is a class III nucleotide cyclase domain [ 5 ], which is distributed widely from bacteria to humans. (biomedcentral.com)
  • We showed that properties intrinsic to the helicase-like domain, like DNA-stimulated ATP hydrolysis, nucleotide-dependent affinity switch for DNA, and thermodynamic coupling between DNA binding and ATP binding and hydrolysis, are strongly reduced in the context of reverse gyrase. (unibas.ch)
  • Additionally, we also elucidated the nucleotide cycle and conformational transitions for this helicase-like domain mutant, which gave the first indications of why no positive supercoiling can be performed by the full-length reverse gyrase lacking the latch, and only DNA relaxation is allowed. (unibas.ch)
  • Nucleotide binding domains (NBDs) secure ATP-binding cassette (ABC) transporter function. (elsevier.com)
  • It is necessary to have at least a dimer for creation of the catalytic cavity. (jbsdonline.com)
  • We propose in this project to reconstruct and characterize the catalytic domain of an ancestor of RPTPs. (biochim.ro)
  • This entry represents the peptidase domain found in a group of aspartic endopeptidases of fungal origin, including aspergillopepsin (MEROPS ientifier A01.016) [ PMID: 11418762 ], rhizopuspepsin (A01.012), endothiapepsin (A01.017) and penicillopepsin (A01.011) [ PMID: 339694 ]. (ebi.ac.uk)
  • Recently, we have further shown that the catalytic domain plus three amino acids from the kinase-like domain of GC-A (242 amino acids) are sufficient for performing the catalytic function (unpublished data, 1994). (ahajournals.org)
  • The MLL3 (KMT2C) protein is 4,911 amino acids long, and it contains 8 plant homeodomain (PHD) and a suppressor of variegation, enhancer of zeste, trithorax (SET) domain which contains the catalytic center. (biomedcentral.com)
  • Functional human telomerase complexes are minimally composed of the human telomerase RNA (hTR) and a catalytic subunit (human telomerase reverse transcriptase [hTERT]) containing reverse transcriptase (RT)-like motifs. (asm.org)
  • We recently demonstrated that amino acid 119, in the α2 helix of the central domain of the human immunodeficiency virus type 1 integrase, affected the choice of nonviral target DNA sites. (asm.org)
  • Studies using chimeric integrases involving human immunodeficiency virus type 1 (HIV-1), feline immunodeficiency virus, and visna virus indicate that the central domain of integrase plays a major role in selecting the target sites for insertion of viral DNA ends. (asm.org)
  • C) Catalytic core of human methyladenosine demethylase FTO (PDB ID: 3LFM [14]) demonstrating the double-stranded β-helical fold and including the active site metal (blue sphere). (nih.gov)
  • SENP1 (catalytic domain) (human) (rec. (adipogen.com)
  • A synthetic gene was made to express the catalytic domain of human gelatinase A (GCD), in which two polypeptide fragments of the catalytic domain were joined with deletion of the insert. (elsevier.com)
  • A cis -acting enoyl reductase (ER) catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR-iPKS) for the first time and studied in vitro . (rsc.org)
  • The catalytic domain of glucoamylases G1 and G2 from Aspergillus niger is produced in vitro in high yield by limited proteolysis using either subtilisin Novo or subtilisin Carlsberg. (biochemj.org)
  • GC search motifs constructed from the alignment of known GCs catalytic centers form vertebrates and lower eukaryotes have led to the identification of a number of plant GCs that have been characterized in vitro and in vivo . (biomedcentral.com)
  • An important difference between the two is that the Cdc25B domain binds oxyanions in the catalytic site while that of Cdc25A appears unable to bind oxyanions. (rcsb.org)
  • A concave face formed by domains 2 and 3 is proposed to bind a nucleic acid duplex substrate. (ntu.edu.sg)
  • If it turns out that plants do harbor a large number of functional GC domains as part of multi-domain enzymes, then major new insights will be gained into the complex signal transduction pathways that link cGMP to fundamental processes such as ion transport and homeostasis, biotic and abiotic stress responses as well as cGMP-dependent responses to hormones. (biomedcentral.com)
  • Psidin physically binds the catalytic NatB subunit CG14222 (dNAA20) and functionally interacts with it in vivo . (jneurosci.org)
  • 40) of multi-domain molecules with potentially functional GC catalytic centers in plants that remain to be discovered and characterized. (biomedcentral.com)
  • The thermostability is essentially the same for the single-chain catalytic domain and the original glucoamylases G1 and G2, whereas the catalytic domain cut between Ser-443 and Ser-444 is less thermostable. (biochemj.org)
  • The transposases from several superfamilies possess a protein domain containing an acidic amino acid triad (DDE or DDD) that catalyzes the "cut and paste" transposition reaction. (pnas.org)
  • Purification by affinity chromatography on an acarbose-Sepharose column followed by ion-exchange chromatography on HiLoad Q-Sepharose leads to separation of a number of structurally closely related forms of domain. (biochemj.org)
  • Furthermore, we have elucidated the thermodynamic and conformational cycle of the helicase-like domain, and predicted the stages fulfilling the requirements for interdomain communication, local duplex DNA unwinding, and the stages where DNA is in a suitable state to support the supercoiling reaction. (unibas.ch)
  • In addition, prolonged incubation of PDE6 with vardenafil or sildenafil (but not 3-isobutyl-1-methylxanthine and zaprinast) induced a distinct conformational change in the catalytic domain without affecting the binding properties of the GAF domains. (unh.edu)
  • Finally, besides the use of smFRET as a tool to investigate conformational changes in solution, we have also provided high-resolution snapshots of the helicase-like domain via X-ray crystallography. (unibas.ch)
  • However, it was unclear whether this domain was shared by the transposases from all superfamilies. (pnas.org)