Catalytic domain. Medical search

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)

... and the calcium ion are present in the catalytic domain approximately 12 Å away from the catalytic zinc. The catalytic zinc ion ... a catalytic domain; and a hemopexin-like domain at the carboxy-terminal. The propeptide consists of approximately 80-90 amino ... The catalytic domain contains two zinc ions and at least one calcium ion coordinated to various residues. One of the two zinc ... The catalytic domain of MMP-3 can be inhibited by tissue inhibitors of metalloproteinases (TIMPs). The n-terminal fragment of ...

https://en.wikipedia.org/wiki/MMP3

... domain; an α-helical membrane-binding moiety; and a C-terminal catalytic domain. PTGS (COX, which can be confused with " ... The catalytic domain is homologous to mammalian peroxidases such as myeloperoxidase. It has been found that human PTGS2 (COX-2 ... Both the cyclooxygenase and the peroxidase active sites are located in the catalytic domain, which accounts for approximately ... Each subunit has three different structural domains: a short N-terminal epidermal growth factor (EGF) ...

https://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase_2

... the catalytic domain (residues 153-425); and the C-terminal domain (residues 426-692), which is further divided into three ... A number of monoclonal antibodies that bind to and inhibit PCSK9 near the catalytic domain were in clinical trials as of 2014[ ... though the N-terminal prodomain retains its association with the catalytic domain. In particular, residues 61-70 in the N- ... domain of the LDLR. While previous studies indicated that the C-terminal domain was uninvolved in binding LDLR, a recent study ...

https://en.wikipedia.org/wiki/PCSK9

Antiparallel orientation of the catalytic domains". J. Biol. Chem. 275 (52): 41476-86. doi:10.1074/jbc.M007480200. PMID ...

https://en.wikipedia.org/wiki/B4GALNT1

Catalytic role of the condensation domain". J. Biol. Chem. 273 (35): 22773-81. doi:10.1074/jbc.273.35.22773. PMID 9712910. This ... In molecular biology, the condensation domain is a protein domain found in many multi-domain enzymes which synthesise peptide ... This domain catalyses a condensation reaction to form peptide bonds in non-ribosomal peptide biosynthesis. It is usually found ... It has been shown that mutations in the HHXXXDG sequence motif in this domain abolish activity suggesting this is part of the ...

https://en.wikipedia.org/wiki/Condensation_domain

Estrella MA, Du J, Korennykh A (2018). "Crystal Structure of Human Nocturnin Catalytic Domain". Scientific Reports. 8 (1): ... It is encoded by the NOCT gene located on chromosome 4. Nocturnin contains a c-terminal structural domain of the Endonuclease/ ... As in the other EEP members, five conserved catalytic residues help coordinate a Magnesium atom, for Nocturnin the divalent ... Nocturnin contains a c-terminal structural domain of the Endonuclease/Exonuclease/phosphatase family (EEP). Its protein fold is ...

https://en.wikipedia.org/wiki/Nocturnin

HDAC10 has two catalytic domains as well. One active domain is located in the N-terminus and a putative catalytic domain is ... However, HDAC6's catalytic domain is most similar to HDAC9. A unique feature of HDAC6 is that it contains two catalytic domains ... 5 and 7 have their catalytic domains located in the C-terminus along with an NLS region while HDAC9 has its catalytic domain ... domain with a HAT domain in-between. The last is TAFII250 which has a Kinase domain at the N-terminus region, two bromodomains ...

https://en.wikipedia.org/wiki/Histone_acetylation_and_deacetylation

This enzyme has 8 helical domains anchoring it in the Golgi membrane of the ER; the catalytic domain is in the cytosol. It is ...

https://en.wikipedia.org/wiki/Juvenile_hormone

The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and ...

https://en.wikipedia.org/wiki/ATP6V1B2

The membrane-bound form has both membrane-binding and catalytic domains. The soluble form has only the catalytic domain. This ... Exon 2 contains the junction of the membrane-binding domain and the catalytic domain of b5R, which shows that there are two ... this isoform has one hydrophobic membrane-anchoring domain and one catalytic domain that is hydrophilic. The other isoform, a ... The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe- ...

https://en.wikipedia.org/wiki/CYB5R3

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 part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L. GRCh38: Ensembl release ...

https://en.wikipedia.org/wiki/ATP6V0C

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 ...

https://en.wikipedia.org/wiki/ATP6V0D1

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 ... 2002). "The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is ...

https://en.wikipedia.org/wiki/ATP6V0E1

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: ...

https://en.wikipedia.org/wiki/ATP6V1E1

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 regulatory H subunit of the V1 domain which is required for catalysis of ATP but not the assembly of V- ... Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL (Oct 2002). "The amino-terminal domain of the E subunit of vacuolar H ...

https://en.wikipedia.org/wiki/ATP6V1H

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 ...

https://en.wikipedia.org/wiki/ATP6V1B1

The similarity in the catalytic domains of C5-cytosine methyltransferases and N6 and N4-adenine methyltransferases provided ... Schluckebier G, O'Gara M, Saenger W, Cheng X (March 1995). "Universal catalytic domain structure of AdoMet-dependent ... Motifs IV-VIII play a role in the catalytic activity, while motifs 1-III and X play a role in binding of the cofactor. For N6- ... based on the sequential order of certain 9 motifs and the Target Recognition Domain (TRD). Motif I consists of a Gly-X-Gly ...

https://en.wikipedia.org/wiki/DNA_adenine_methylase

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 ... V1 domain C subunit isoforms. GRCh38: Ensembl release 89: ENSG00000143882 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...

https://en.wikipedia.org/wiki/ATP6V1C2

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. ...

https://en.wikipedia.org/wiki/ATP6V1G2

https://en.wikipedia.org/wiki/ATPase,_H _transporting,_lysosomal_V0_subunit_a1

It is considered to be the catalytic domain. It has a structure of six beta strands forming a twisted beta sheet with four ... The domains of the monomer show a fair amount of flexibility suggesting that the enzyme can open in close to bind with the ... The C-terminal domain binds to NADPH. It has a special structure, a Rossmann fold, whereby six-stranded twisted and parallel ... The Structure of Shikimate dehydrogenase is characterized by two domains, two alpha helices and two beta sheets with a large ...

https://en.wikipedia.org/wiki/Shikimate_dehydrogenase

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 ... Chang SY, Park SG, Kim S, Kang CY (2002). "Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. ... V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene. This gene encodes a ...

https://en.wikipedia.org/wiki/ATP6V1A

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 part of the transmembrane V0 domain, and is the human counterpart of yeast VMA16. Two alternatively ...

https://en.wikipedia.org/wiki/ATP6V0B

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 the V1 domain F subunit protein. Subunit F is a 16 kDa protein that is required for the assembly and ... Peng SB, Crider BP, Tsai SJ, Xie XS, Stone DK (Jun 1996). "Identification of a 14-kDa subunit associated with the catalytic ...

https://en.wikipedia.org/wiki/ATP6V1F

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: ...

https://en.wikipedia.org/wiki/ATP6V1D

The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. This ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ...

https://en.wikipedia.org/wiki/ATP6V0A4

The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of three V1 domain G subunit proteins. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and ...

https://en.wikipedia.org/wiki/ATP6V1G1

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 is one of two genes that encode the V1 domain C subunit proteins and is found ubiquitously. This C subunit is ...

https://en.wikipedia.org/wiki/ATP6V1C1

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 ...

https://en.wikipedia.org/wiki/ATP6V1G3

"Crystal structure of the catalytic domain of human ADAM33". Journal of Molecular Biology. 335 (1): 129-37. doi:10.1016/j.jmb. ... Zou J, Zhu F, Liu J, Wang W, Zhang R, Garlisi CG, Liu YH, Wang S, Shah H, Wan Y, Umland SP (March 2004). "Catalytic activity of ... Disintegrin and metalloproteinase domain-containing protein 33 is an enzyme that in humans is encoded by the ADAM33 gene. This ... "Entrez Gene: ADAM33 ADAM metallopeptidase domain 33". Davies ER, Kelly JF, Howarth PH, Wilson DI, Holgate ST, Davies DE, ...

https://en.wikipedia.org/wiki/ADAM33

However important the fusion order is, the evolutionary origin of each catalytic domain in UMPS is also a matter of study. Both ... Merging both the fusion order and evolutionary origin, organisms end up having fused UMPS where one of its catalytic domains ... In microorganisms, these two domains are separate proteins, but, in multicellular eukaryotes, the two catalytic sites are ... The covalent union in UMPS stabilizes the domains containing the respective catalytic centers, improving its activity in ...

https://en.wikipedia.org/wiki/Uridine_monophosphate_synthase

c-Src is made up of 6 functional regions: Src homology 4 domain (SH4 domain), unique region, SH3 domain, SH2 domain, catalytic ... It includes an SH2 domain, an SH3 domain and a tyrosine kinase domain. Two transcript variants encoding the same protein have ... group at the 527 position interacts with the SH2 domain which helps the SH3 domain interact with the flexible linker domain and ... Arbesú M, Maffei M, Cordeiro TN, Teixeira JM, Pérez Y, Bernadó P, Roche S, Pons M (March 2017). "The Unique Domain Forms a ...

https://en.wikipedia.org/wiki/Proto-oncogene_tyrosine-protein_kinase_Src

"Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor". Journal of ... Its catalytic site involves sulfohydryl group of Cys-285 and the imidazole ring of its His-237. The caspase-3 His-237 ... What is more, combining C3's amino acids leads to 5 α helices, 4 β lamina and a loop at the catalytic C-terminal which interact ... Lugovskoy AA, Zhou P, Chou JJ, McCarty JS, Li P, Wagner G (December 1999). "Solution structure of the CIDE-N domain of CIDE-B ...

https://en.wikipedia.org/wiki/Caspase-activated_DNase

DnaA has four domains with each domain responsible for a specific task. There are 11 DnaA binding sites/boxes on the E. coli ... The catalytic mechanism of DNA polymerase III involves the use of two metal ions in the active site, and a region in the active ...

https://en.wikipedia.org/wiki/Prokaryotic_DNA_replication

The flow of protons makes the stalk subunit rotate, causing the active site of the synthase domain to change shape and ... Dimroth P, von Ballmoos C, Meier T (March 2006). "Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles ... ISBN 0-19-860783-0. Advanced Price N, Stevens L (1999). Fundamentals of Enzymology: Cell and Molecular Biology of Catalytic ... Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems". European Journal of ...

https://en.wikipedia.org/wiki/Metabolism

Zinc is a critical component of the catalytic site of hundreds of kinds of different metalloenzymes in each human being. In its ... structural role, zinc coordinates with certain protein domains, facilitating protein folding and producing structures such as ' ... catalytic, structural, and regulatory. Zinc (Zn) is only common in its +2 oxidative state, where it typically coordinates with ...

https://en.wikipedia.org/wiki/Zinc_deficiency

This article incorporates text from this source, which is in the public domain. "President Honors Outstanding Early-Career ... Catalytic Molecular Tweezers". Angewandte Chemie International Edition. 43 (41): 5503-5507. doi:10.1002/anie.200460932. ISSN ...

https://en.wikipedia.org/wiki/Nathan_C._Gianneschi

Cyclins form the regulatory subunits and CDKs the catalytic subunits of an activated heterodimer; cyclins have no catalytic ... This article incorporates public domain material from Science Primer. NCBI. Archived from the original on 8 December 2009. ...

https://en.wikipedia.org/wiki/Cell_cycle

One model showed two domains, an alpha-helix-rich domain and a beta-sheet-rich domain. The heme was found to be sandwiched ... Mutagenesis studies that made substitutions at that position resulted in loss of catalytic activity and minimal heme binding. ... Ruan KH, Kulmacz RJ, Wu KK (1994). "Characterization of the Structure and Membrane Interaction of NH2-terminal Domain of ...

https://en.wikipedia.org/wiki/Thromboxane-A_synthase

Allen MD, Buchberger A, Bycroft M (Sep 2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". ... and PNGase F The enzyme uses a catalytic triad of cysteine-histidine-aspartate in its active site for hydrolysis by covalent ...

https://en.wikipedia.org/wiki/Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine_amidase

UBL domains of larger proteins are sometimes known as UBX domains. Ubiquitin is, as its name suggests, ubiquitous in eukaryotes ... while sequence similarity and a common catalytic mechanism link pathway members ThiF and MoeB to ubiquitin-activating enzymes. ... UBLs that do not exhibit covalent conjugation (Type II) often occur as protein domains genetically fused to other domains in a ... and may be proteolytically processed to release the UBL domain or may function as protein-protein interaction domains. ...

https://en.wikipedia.org/wiki/Ubiquitin-like_protein

Munro AW; Girvan HM; McLean KJ (June 2007). "Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions ... the conserved stretch of 23 hydrophobic residues in the N-terminus that make up a transmembrane-anchoring domain (residues 3-27 ... near the catalytic center of the enzyme (5.7Å from the iron core of the heme molecule to allow oxyferryl intermediates to ... it has been shown that the deletion of this region results in a two-fold decrease in the enzyme's catalytic efficiency. Binding ...

https://en.wikipedia.org/wiki/Cholesterol_24-hydroxylase

Epoxide hydrolase: 15-Deoxy-Δ12,14-PGJ2 inhibits soluble epoxide hydrolase 2 by forming adducts with its catalytic cysteine ( ... and Src homology 2 domain-containing protein phosphatase 2 pathways to inhibit the actions of pro-inflammatory cytokines; c) ...

https://en.wikipedia.org/wiki/Cyclopentenone_prostaglandins

This article incorporates text from a publication now in the public domain: Chisholm, Hugh, ed. (1911). "Ammonia". Encyclopædia ... which is the principle behind the catalytic converter. Nitrogen oxides can be formed as kinetic products in the presence of ... catalytic, electrochemical). Holographic sensors have been proposed for detecting concentrations up to 12.5% in volume. ...

https://en.wikipedia.org/wiki/Ammonia

... form a catalytic triad with the substrate for acetyl transfer. There are eight alpha helices that form the N-terminal domain. ... The N-terminal domain of the protein Serine acetyltransferase helps catalyse acetyl transfer. This particular enzyme catalyses ... In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses ... The amino-terminal alpha-helical domain particularly the amino acid residues His158 (histidine in position 158) and Asp143 ( ...

https://en.wikipedia.org/wiki/Serine_O-acetyltransferase

F13A1 exon(s) 1 code 5' UTR 2 code activation peptide 2-4 code β-sandwich 4-12 code catalytic domain 12-13 code β-barrel 1 13- ... Each has a mass of about 80 kDa (8.5% of the mass is from carbohydrates), 641 residues and 10 sushi domains. Each domain has ... catalytic domain (185-515), in which the residues C314, H373, D396 and W279 partake in catalysis β-barrel 1 (516-628) β-barrel ... Exons 2-12 code the 10 different sushi domains. Factor XIII of human blood is a heterotetramer of two A and two B linear ...

https://en.wikipedia.org/wiki/Factor_XIII

D: Biological domain of the source: A: archaea - B: bacteria - E: eukarya. SCL: Subcellular genome: chloro: chloroplast - chrm ... encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces ... its domains structure, post-translational modifications, variants, etc.), a minimal level of redundancy and high level of ...

https://en.wikipedia.org/wiki/List_of_homing_endonuclease_cutting_sites

Calalb MB, Polte TR, Hanks SK (1995). "Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain ... The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain ... This protein has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting ... 1995). "The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R". J. Biol. Chem. 270 (25 ...

https://en.wikipedia.org/wiki/Adapter_molecule_crk

Highly conserved phosphatase domain is in central part of the protein. This catalytic domain is flanked on the N-terminal side ... PTB domain). Phosphatase activity of SHIP1 can be allosteric regulated by phosphorylation of the catalytic domain on serine 440 ... At the N-terminus of the protein, SH2 domain is formed. This domain is important for the interaction of SHIP1 with the ... there is an attempt to increase SHIP1 catalytic activity by binding the small molecule to the C2 domain. This molekule should ...

https://en.wikipedia.org/wiki/INPP5D

The thiamine diphosphate-binding site rests on the subunit-subunit interface between two of the domains, which is commonly seen ... as do the presence of vestigial FAD-binding pockets that play no role in either enzyme's catalytic activity. The binding of FAD ... Oxalyl-CoA decarboxylase is tetrameric, and each monomer consists of three α/β-type domains. ...

https://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase

The catalytic domain of PRMTs consists of a SAM binding domain and substrate binding domain (about 310 amino acids in total). ... 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 ...

https://en.wikipedia.org/wiki/Histone_methyltransferase

The kinase domain has some similarity to the MEKK protein kinase family. As a member of the WNK family, the kinase's catalytic ... An autoinhibitory domain is located within the C-terminal domain along with a HQ domain that is needed for WNK1 interactions ... ion to WNK1's catalytic domain. Furthermore, WNK1 and WNK4 may interact to form heterodimers that inhibit WNK1 function. WNK4 ... Phosphorylation of SPAK's T loop located in its catalytic domain will activate SPAK, which will go on to phosphorylation the ...

https://en.wikipedia.org/wiki/WNK1

The POLG2 gene encodes a 55 kDa accessory subunit protein that imparts high processivity and salt tolerance to the catalytic ... This article incorporates text from the United States National Library of Medicine, which is in the public domain. (Source ... The encoded protein forms a heterotrimer containing one catalytic subunit and two processivity subunits. This protein enhances ... which is in the public domain. "POLG2 - DNA polymerase subunit gamma-2, mitochondrial precursor - Homo sapiens (Human) - POLG2 ...

https://en.wikipedia.org/wiki/POLG2

Several amino acids within the catalytic pocket have been identified as important to DLD function, including R281 and N473. ... With its proteolytic function, DLD removes a functionally vital domain from the N-terminus of frataxin, a mitochondrial protein ... center domain". Journal of Biomedical Science. 14 (2): 203-10. doi:10.1007/s11373-006-9136-0. PMID 17171578. Foster LJ, Rudich ... which is in the public domain. (Articles with short description, Short description is different from Wikidata, Genes on human ...

https://en.wikipedia.org/wiki/Dihydrolipoamide_dehydrogenase

These family members lack the catalytic lysine in subdomain II, and instead have a conserved lysine in subdomain I. This family ... 2008). "WNK3 and WNK4 amino-terminal domain defines their effect on the renal Na+-Cl− cotransporter". Am. J. Physiol. Renal ... This article incorporates text from the United States National Library of Medicine, which is in the public domain. Portal: ...

https://en.wikipedia.org/wiki/WNK3

There are two distinct domains in each monomer: the N-terminal domain from residues 1-212 and the C-terminal domain from ... Wijayasinghe YS, Pavlovsky AG, Viola RE (August 2014). "Aspartoacylase catalytic deficiency as the cause of Canavan disease: a ... whereas the C-domain sterically hinders access to the active site in aspartoacylase. Instead, the N-domain and C-domain of ... The N-terminal domain of aspartoacylase is similar to that of zinc-dependent hydrolases such as carboxypeptidaseA. However, ...

https://en.wikipedia.org/wiki/Aspartoacylase

Dinoflagellate luciferase is a multi-domain eukaryote protein, consisting of an N-terminal domain, and three catalytic domains ... The structure of the dinoflagellate luciferase catalytic domain has been solved. The core part of the domain is a 10 stranded ... Luciferase and its domains are not active at pH 8 but they are extremely active at the optimum pH of 6.3 whereas LBP binds ... The helical bundle domain has a three helix bundle structure that holds four important histidines that are thought to play a ...

https://en.wikipedia.org/wiki/Luciferase

Biotin protein ligases may also have an additional N-terminal domain required for DNA binding, although this domain is not ... Reche PA (October 2000). "Lipoylating and biotinylating enzymes contain a homologous catalytic module". Protein Sci. 9 (10): ... They transfer lipoic acid or octanoate from lipoyl domains and transfer to other lipoyl domains. In Bacillus subtilis, the ... In molecular biology, the Cofactor transferase family is a family of protein domains that includes biotin protein ligases, ...

https://en.wikipedia.org/wiki/Cofactor_transferase_family

... catalytic domain - CCR5 receptor - CD4 antigen - CD45 antigen - CD95 antigen - CDC28 protein kinase - cell - cell adhesion ... SH3 domain - SI - sigma factor - signal peptide - signal recognition particle - signal sequence - signal transduction - ... structural domain - Structural formula - structural motif - substance P - substrate - sugar - sulfur - supercoil - superfamily ...

https://en.wikipedia.org/wiki/Index_of_biochemistry_articles

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 structure of a minimum ... Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle.. Reynolds, R.A., Yem ...

https://www.rcsb.org/structure/1cws

... ...

https://www.ncbi.nlm.nih.gov/Structure/pdb/4CRQ

Timeline for Protein Chitinase B, catalytic domain from c.1.8.5: Type II chitinase: *Protein Chitinase B, catalytic domain from ... catalytic domain from c.1.8.5: Type II chitinase appears in SCOP 1.59. *Protein Chitinase B, catalytic domain from c.1.8.5: ... Domains for 1e15: *. Domain d1e15a2: 1e15 A:3-291,A:380-446 [29006]. Other proteins in same PDB: d1e15a1, d1e15a3, d1e15b1, ... Domains for 1e6n: *. Domain d1e6na2: 1e6n A:3-291,A:380-446 [59309]. Other proteins in same PDB: d1e6na1, d1e6na3, d1e6nb1, ...

https://scop.berkeley.edu/sunid=51546&ver=1.57

Clarke DJ, Azuma Y. Non-Catalytic Roles of the Topoisomerase IIα C-Terminal Domain. International Journal of Molecular Sciences ... However, the enzyme also possesses a C-terminal domain (CTD) that is largely dispensable for the strand passage reaction but is ...

https://kuscholarworks.ku.edu/handle/1808/26775

Inhibition of human FGFR2 N549H mutant catalytic domain expressed in baculovirus assessed as substrate phosphorylation using ...

https://pubchem.ncbi.nlm.nih.gov/bioassay/1078739

Crystal structure of the C-terminal catalytic domain of Plasmodium falciparum CTP:phosphocholine cytidylyltransferase in ... Structural determinants of the catalytic mechanism of Plasmodium CCT, a key enzyme of malaria lipid biosynthesis. ...

https://3dprint.nih.gov/discover/3DPX-016470

The 28-kDa peptide, corresponding to the N-terminal domain of the recombinant adenylate cyclase, exhibited very low catalytic ... These fragments, each containing a single Trp residue, were purified and analyzed for their catalytic and calmodulin-binding ... The 19-kDa peptide, corresponding to the C-terminal domain of the recombinant adenylate cyclase, interacted only with ... which shows similar catalytic properties to intact adenylate cyclase. ...

https://hal-pasteur.archives-ouvertes.fr/pasteur-00167100

... catalytic domain family. Additional information, provided for both this family and the superfamily it belongs to, includes ... SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model ... Cell cycle control phosphatase, catalytic domain family. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [. 0] (11) ... Document: WP annotation of SCOP domains. Fly Phenotype (FP). (show details) Highlighted in gray are those with FDR_all>0.001. ...

https://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=52822

Genetic analysis of the catalytic domain of the GAP gene in human lung cancer cell lines. Hum Genet. 1994 Jan; 93(1):27-31. ... Genetic analysis of the catalytic domain of the GAP gene in human lung cancer cell lines.. ...

https://profiles.uchicago.edu/profiles/display/241677

PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of ... PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of ... PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of ... PH domain leucine-rich repeat-containing protein phosphatase 2. Names. GTPase activating protein and VPS9 domains 1. NP_ ...

https://www.ncbi.nlm.nih.gov/gene/?term=244650

Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp ... Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp. Enzymatic activity of Catalytic Domain of Human ... The structure of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp, PDB code: 1tb5 was solved by K.Y.J.Zhang, ... The structure of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Amp also contains other interesting chemical ...

http://magnesium.atomistry.com/pdb1tb5.html

Biochemical assays show that these two domains interact with each other, which is required for FTO catalytic activity. In ... FTO comprises an amino-terminal AlkB-like domain and a carboxy-terminal domain with a novel fold. ...

https://pubmed.ncbi.nlm.nih.gov/20376003/

We found that the catalytic domain of PARG is predicted to contain a mostly beta sheet structure and a secondary structure ... Identification of catalytic acidic residues along with recent identification of a polymer binding residue Y796 and a glycine ... The mutants were purified and catalytic activity as well as binding to a PARG inhibitor, ADP-HPD, was performed to show that ... other members of this family of enzymes contain catalytic acidic residues surrounding the labile glycosidic bond. Previously an ...

https://medscitechnol.com/abstract/index/idArt/15116

Severe factor X deficiency due to a homozygous mutation (Cys364Arg) that disrupts a disulphide bond in the catalytic domain. ... 15, 16, 17, 18, 19, 20, 21] Mutations in the Gla-domain of factor X, a 39 residue peptide that is part of its light chain, have ... A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo). Br J ... which normally undergoes gamma-carboxylation within the gamma-carboxyglutamic acid-rich domain. [23] A factor X-deficient woman ...

https://www.medscape.com/answers/209867-172694/what-is-the-pathophysiology-of-factor-x-deficiency

Structure of Karilysin Mmp-Like Catalytic Domain in Complex with Inhibitory Tetrapeptide Swfp ... The structure of Structure of Karilysin Mmp-Like Catalytic Domain in Complex with Inhibitory Tetrapeptide Swfp also contains ... The structure of Structure of Karilysin Mmp-Like Catalytic Domain in Complex with Inhibitory Tetrapeptide Swfp, PDB code: 4in9 ... In total only one binding site of Potassium was determined in the Structure of Karilysin Mmp-Like Catalytic Domain in Complex ...

http://potassium.atomistry.com/pdb4in9.html

MMP-12 (Catalytic Domain), human recombinant. Cat.Number : AS-55525-1 $103.00 Excl. Tax ...

https://www.anaspec.com/en/catalog/sensolyte-490-mmp-12-assay-kit-fluorimetric-1-kit~01bd0aa3-20ef-4d01-93bd-c3d436e19518

High-resolution structure of the catalytic region of MICAL, a multi-domain flavoenzyme-signaling molecule ... High-resolution structure of the catalytic region of MICAL, a multi-domain flavoenzyme-signaling molecule ...

https://www.camsoxford.ox.ac.uk/coi-publications/publications/27767

Description: the structure of the isolated catalytic domain of diphtheria toxin. Class: toxin. Keywords: toxin. Deposited on ... Uniprot P00588 (0-189) Domains in SCOPe 2.08: d1dtpa_*Heterogens: APU, HOH PDB Chain Sequences:. *Chain A:. Sequence; same ...

http://scop.berkeley.edu/pdb/code=1dtp

Medium-chain alcohol dehydrogenases, catalytic domain. The name of this superfamily has been modified since the most recent ...

http://www.cathdb.info/version/v4_3_0/superfamily/3.90.180.10/funfam/1/taxonomy_sunburst

USA 113, 1790-1795 (2016). Identification of a subclass of GGDEF-domain-containing dinucleotide cyclases with broad catalytic ... Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: clues from the structure of the catalytic domain. ... Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron ... YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase ...

https://www.nature.com/articles/nchembio.2337?error=cookies_not_supported&code=585565b1-ca3a-4516-ba19-23b4046c28c5

THE STRUCTURE OF THE M60 CATALYTIC DOMAIN FROM CLOSTRIDIUM PERFRINGENS ZMPC IN COMPLEX THE SIALYL T ANTIGEN - 6XT1 , canSARS ... THE STRUCTURE OF THE M60 CATALYTIC DOMAIN FROM CLOSTRIDIUM PERFRINGENS ZMPC IN COMPLEX THE SIALYL T ANTIGEN ... THE STRUCTURE OF THE M60 CATALYTIC DOMAIN FROM CLOSTRIDIUM PERFRINGENS ZMPC IN COMPLEX THE SIALYL T ANTIGEN ...

https://corona-1.cansar.icr.ac.uk/structure/6XT1/3d/6XT1_A

Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso ... The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2- ... A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Catalytic Domain of ... A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Catalytic Domain of ...

http://calcium.atomistry.com/pdb3f18.html

RIP2 KINASE CATALYTIC DOMAIN COMPLEX WITH 2(4[(1,3BENZOTHIAZOL5YL) AMINO]6(2METHYLPROPANE2SULFONYL)QUINAZOLIN7YL)OXY)ETHYL ... RIP2 KINASE CATALYTIC DOMAIN COMPLEX WITH 2(4[(1,3BENZOTHIAZOL5YL) AMINO]6(2METHYLPROPANE2SULFONYL)QUINAZOLIN7YL)OXY)ETHYL ... RIP2 KINASE CATALYTIC DOMAIN COMPLEX WITH 2(4[(1,3BENZOTHIAZOL5YL) AMINO]6(2METHYLPROPANE2SULFONYL)QUINAZOLIN7YL)OXY)ETHYL ...

https://corona-1.cansar.icr.ac.uk/structure/6RN8/3d/6RN8_A

Crystal Structure of the Catalytic Domain of Mmp-13 Complexed with N- (3-Methoxybenzyl)-4-Oxo-3,4-Dihydrothieno[2,3-D] ... The structure of Crystal Structure of the Catalytic Domain of Mmp-13 Complexed with N- (3-Methoxybenzyl)-4-Oxo-3,4- ... A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Catalytic Domain of ... A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the Catalytic Domain of ...

http://sodium.atomistry.com/pdb3wv3.html

Membrane binding of Escherichia coli RNaseE catalytic domain stabilizes protein structure and increases RNA substrate affinity. ...

https://ir.sinica.edu.tw/handle/201000000A/7442

Catalytic Domain, THR315ALA Mutant Mono- Zinc and Phosphoethanolamine Complex ... Catalytic Domain, THR315ALA Mutant Mono- Zinc and Phosphoethanolamine Complex within 5.0Å range: probe atom residue distance (Å ... Catalytic Domain, THR315ALA Mutant Mono- Zinc and Phosphoethanolamine Complex within 5.0Å range: probe atom residue distance (Å ... Catalytic Domain, THR315ALA Mutant Mono- Zinc and Phosphoethanolamine Complex, PDB code: 6bnd was solved by P.J.Stogios, E. ...

http://zinc.atomistry.com/pdb6bnd.html

Role Of The Regulatory Domain Of Protein Kinase D2 In Phorbol Ester Binding; Catalytic Activity; And Nucleocytoplasmic ...

https://www.mattek.com/reference-library/role-of-the-regulatory-domain-of-protein-kinase-d2-in-phorbol-ester-binding-catalytic-activity-and-nucleocytoplasmic-shuttling/

Binding of Mg nucleotides to the nucleotide-binding domains (NBDs) of SUR1 stimulates channel opening and leads to membrane ... of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide-binding domains. ... of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide-binding domains. ... Binding of Mg nucleotides to the nucleotide-binding domains (NBDs) of SUR1 stimulates channel opening and leads to membrane ...

https://www.dpag.ox.ac.uk/publications/100627

To test whether there is an inhibitory domain located outside the catalytic core of the γ subunit, full-length wild-type and seven truncated forms of γ were expressed inE. (semanticscholar.org)
The catalytic subunit of phosphorylase b kinase and an engineered truncated form (gamma-trc) have been expressed in Escherichia coli and properties that are characteristic of the holoenzyme and the isolated gamma subunit are observed. (semanticscholar.org)
Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain. (semanticscholar.org)
Expression of a cDNA for the catalytic subunit of skeletal-muscle phosphorylase kinase in transfected 3T3 cells. (semanticscholar.org)
Their work revealed that the 14 subunits of SWR1 associate as 4 functional modules: the catalytic subunit Swr1, two multi-subunit modules that interact with the substrate nucleosome and the H2A.Z/H2B dimer, and the putative hexameric AAA+ proteins Rvb1/Rvb2. (harvard.edu)

Membrane binding of Escherichia coli RNaseE catalytic domain stabilizes protein structure and increases RNA substrate affinity. (sinica.edu.tw)

The mutants were purified and catalytic activity as well as binding to a PARG inhibitor, ADP-HPD, was performed to show that the mutations did not interfere with the ability to detect a substrate like moiety. (medscitechnol.com)

However, the enzyme also possesses a C-terminal domain (CTD) that is largely dispensable for the strand passage reaction but is nevertheless important for the fidelity of cell division. (ku.edu)
Structural determinants of the catalytic mechanism of Plasmodium CCT, a key enzyme of malaria lipid biosynthesis. (nih.gov)
Structural and biochemical characterizations of the novel autolysin Acd24020 from Clostridioides difficile and its full-function catalytic domain as a lytic enzyme. (expasy.org)
It is an amazingly complex enzyme, combining two catalytic domains with three binding modules. (nrel.gov)
The assembly of one of Nature's most elaborate multienzyme complexes, the cellulosome, results from the binding of enzyme-borne dockerins to reiterated cohesin domains located in a non-catalytic primary scaffoldin. (jbc.org)

Building performant informatics systems that fits how researchers work is complex and requires a mix of world class software engineering and life sciences domain expertise. (catalyticds.com)
We founded Catalytic Data Science to solve this exact challenge for life sciences researchers. (catalyticds.com)

Orthologous to human PHLPP2 (PH domain and leucine rich repeat protein phosphatase 2). (nih.gov)
Endothelial Scaffolding Protein ENH (Enigma Homolog Protein) Promotes PHLPP2 (Pleckstrin Homology Domain and Leucine-Rich Repeat Protein Phosphatase 2)-Mediated Dephosphorylation of AKT1 and eNOS (Endothelial NO Synthase) Promoting Vascular Remodeling. (nih.gov)
Some members of this domain family coexist with a C-terminal trehalose phosphatase domain. (unl.edu)

Poly(ADP-ribose) glycohydrolase (PARG) is an O-glycosidase, other members of this family of enzymes contain catalytic acidic residues surrounding the labile glycosidic bond. (medscitechnol.com)
writers - a host of enzymes capable of modifying nucleotide base and specific amino acid residues on histones, erasers - a group of enzymes proficient in removing these marks, and readers - a diverse range of proteins that possess specialized domains recognizing specific epigenetic marks in a locus. (enzolifesciences.com)
These enzymes and protein domains together constitute the epigenetics tools as shown Table 1. (enzolifesciences.com)
These enzymes and protein domains carry out most of the epigenetic modifications on DNA and histone tails. (enzolifesciences.com)
For application in bioethanol production, novel enzymes with high catalytic activity against recalcitrant lignocellulosic material are being explored and developed. (jbc.org)
The endoglucanase CenA from Cellulomonas fimi is a member of family B. All enzymes from this family are believed to hydrolyze beta-1,4-glucosidic bonds using a general acid-base catalytic mechanism resulting in inversion of anomeric configuration at the scissile bond. (ubc.ca)

Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase. (archives-ouvertes.fr)

Identification of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide-binding domains. (ox.ac.uk)
Four yeast proteins (Prp16p, Prp17p, Prp18p, and Slu7p) function exclusively in the second catalytic step. (bdbiosciences.com)

The catalytic cysteine residue, Cys473, can be oxidized to form a disulfide linkage to Cys426. (rcsb.org)
These fragments, each containing a single Trp residue, were purified and analyzed for their catalytic and calmodulin-binding properties. (archives-ouvertes.fr)
15, 16, 17, 18, 19, 20, 21] Mutations in the Gla-domain of factor X, a 39 residue peptide that is part of its light chain, have been documented in at least 15 cases of factor X deficiency. (medscape.com)
Identification of catalytic acidic residues along with recent identification of a polymer binding residue Y796 and a glycine rich region 745GGG747 allowed us to define a PARG 'signature sequence' [DFA-X4-GGg-X6-7-vQEEIRf-X3-YTGY] which we have used in conjunction with PHI-BLAST to identify distantly related PARG sequences. (medscitechnol.com)
The interaction of FRS2 with FGFR1 occurs via the PTB domain of FRS2 binding to a 12-residue segment in the juxtamembrane region of FGFR1. (novusbio.com)

A series of minimal domain Cdc25B constructs maintaining catalytic activity have been expressed. (rcsb.org)
The Cdc25B constructs, with various truncations of the C-terminal residues, are shown to have potent catalytic activity. (rcsb.org)
The 28-kDa peptide, corresponding to the N-terminal domain of the recombinant adenylate cyclase, exhibited very low catalytic activity, and was still able to bind calmodulin weakly, as evidenced by using a fluorescent derivative of the activator protein. (archives-ouvertes.fr)
Biochemical assays show that these two domains interact with each other, which is required for FTO catalytic activity. (nih.gov)
The catalytic activity of the mitogen-activated protein kinase extracellular signal-regulated kinase 3 is required to sustain CD4+ CD8+ thymocyte survival. (atlasgeneticsoncology.org)
Autophosphorylation sites located within the catalytic domain are crucial for stimulation of kinase activity, while autophosphorylation sites located in other regions are usually involved in the recruitment of cellular target proteins. (novusbio.com)
The tetramer can be artificially maintained by disulfide bond formation, which fully displaces the zinc but largely preserves the catalytic activity. (ox.ac.uk)
Thus, catalytic activity does not require zinc directly but does require the quaternary structure, for which the metal is essential. (ox.ac.uk)
Therefore, perovskite oxides with different structures were prepared and were used to support Au catalysts, in order to obtain excellent catalytic activity and high stability. (pku.edu.cn)
The perovskite-supported Au catalyst was prepared by the deposition precipitation method and its catalytic activity for CO oxidation was evaluated. (pku.edu.cn)
As shown in characterization results, after the catalyst was calcined at high temperatures (700 and 900 ℃), the Au nanoparticle size on the Au/LaMnO 3 -AE catalyst was lower than those on Au/LaMnO 3 and Au/LaMn 1.2 O 3 catalysts, leading to high reducibility and catalytic activity of the Au/LaMnO 3 -AE catalyst. (pku.edu.cn)
Catalytic Activity of Au Nanoparticles Supported on LaMnO 3 Perovskite with Different Composition and Structure[J].Acta Physico-Chimica Sinica, 2019, 35(4): 422-430. (pku.edu.cn)
On the other hand, the longer gene had almost all amino acids that were expected to be involved in substrate binding and catalytic activity. (archive.org)

Figure 4: Tripartite transmembrane signaling through HAMP-domaincontaining proteins with active or degenerate GGDEF and EAL domains. (nature.com)
There are 12028 ARF domains in 11995 proteins in SMART's nrdb database. (embl.de)
Taxonomic distribution of proteins containing ARF domain. (embl.de)
The complete taxonomic breakdown of all proteins with ARF domain is also avaliable . (embl.de)
Click on the protein counts, or double click on taxonomic names to display all proteins containing ARF domain in the selected taxonomic class. (embl.de)
The data also indicate that the SH4-Unique-SH3-SH2 domains of c-Yes work cooperatively and prevent activation of signaling proteins associated with Src527F transformation, including activation of phosphatidylinositol 3-kinase, phosphorylation of c-Raf and Akt and downregulation of RhoA-GTP. (cdc.gov)
This domain occurred 360 times on human genes ( 816 proteins). (umbc.edu)
This domain is present in retroviral nucleocapsid proteins and in several splicing factors. (bdbiosciences.com)

The candidate cysteines are part of a motif that is conserved in the RNase E protein family, and mutation of these residues causes the partial loss of zinc, the complete disruption of the tetramer into dimers, and effective catalytic inactivation. (ox.ac.uk)

Serine/Threonine Kinases (STKs), PFTAIRE-2 subfamily, catalytic (c) domain. (umbc.edu)
The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. (umbc.edu)
C-terminal, AAA lid domain, Clp amino terminal domain, AAA domain (Cdc48 subfamily), ATPase family associated with various cellular activities (AAA) [Interproscan]. (ntu.edu.sg)

A presence/absence matrix is generated using protein domain architecture data for all genomes in SUPERFAMILY. (cam.ac.uk)
A presence/absence matrix is generated using protein domains and supradomains for all genomes in SUPERFAMILY. (cam.ac.uk)

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase. (umbc.edu)

FRS2 contains both a consensus myristylation sequence, involved in its recruitment to the cell membrane and a putative phosphotyrosine binding (PTB)domain in its amino-terminus. (novusbio.com)

Reassociation was enhanced by calmodulin itself, which 'trapped' the two complementary peptides into a stable, native-like, ternary complex, which shows similar catalytic properties to intact adenylate cyclase. (archives-ouvertes.fr)
Structure of the Catalytic Domain of the Tannerella Forsythia Matrix Metallopeptidase Karilysin in Complex with A Tetrapeptidic Inhibitor. (atomistry.com)
The bacterium first found in heated freshwater pools, Caldicellulosiruptor bescii, secretes the cellulase, CelA, which has the complex arrangement of two catalytic domains separated by linker peptides and cellulose binding modules. (nrel.gov)
Fas ligand binds to the receptor and forms the death-inducing signalling complex, including the Fas-associated death domain, death-domain associated protein, and caspase-10. (smpdb.ca)
The authors also characterized a SWR1-nucleosome co-complex, revealing a significant conformational change involving the catalytic ATPase and the H2A.Z/H2B-binding module. (harvard.edu)

A major question in the chromatin field is how the diversity in cis -regulatory domains and accessory subunits gives rise to the functional specialization of remodelers. (harvard.edu)

The 19-kDa peptide, corresponding to the C-terminal domain of the recombinant adenylate cyclase, interacted only with calmodulin as indicated by a shift in its intrinsic fluorescence emission spectrum or by the enhancement of fluorescence of dansyl-calmodulin. (archives-ouvertes.fr)

FRY2/CPL1 encodes a novel transcriptional repressor harboring two double-stranded RNA-binding domains and a region homologous to the catalytic domain of RNA polymerase II C-terminal domain phosphatases found in yeast and in animals that regulate gene transcription. (edu.sa)

The catalytic domain of chitinase A1 from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. (ncku.edu.tw)

Backbone resonance assignments of the catalytic and regulatory domains of Ca/calmodulin-dependent protein kinase 1D. (cdc.gov)

The kinase domain of death-associated protein kinase is inhibitory for tubulointerstitial fibrosis in chronic obstructive nephropathy. (elsevier.com)

In order to begin to understand why c-Yes is unable to compensate for c-Src signaling, we used a series of Src/Yes chimeras in which the non-catalytic functional domains of Src527F were replaced by those of c-Yes. (cdc.gov)

Genetic analysis of the catalytic domain of the GAP gene in human lung cancer cell lines. (uchicago.edu)
The human ERK3 protein is made of 721 amino acids and contains a typical kinase domain located at the N-terminal extremity. (atlasgeneticsoncology.org)

Another region with homology to the MAP kinase ERK4 (C34 domain) has been identified after the kinase domain. (atlasgeneticsoncology.org)
ERK3 display 73% amino acid identity with ERK4 in the kinase domain. (atlasgeneticsoncology.org)
We have shown that the kinase domain of DAPK is crucial for the induction of renal tubular cell apoptosis in chronic obstructive uropathy (COU) created by unilateral ureteral ligation. (elsevier.com)
DAPK-mutant mice, generated by deletion of 74 amino acids from the catalytic kinase domain, were used to investigate the role of the DAPK kinase domain in renal fibrosis following COU. (elsevier.com)
Furthermore, deletion of the kinase domain from DAPK significantly increased the appearance of alpha-SMA-positive myofibroblasts in the renal interstitium during COU. (elsevier.com)
Thus, our results suggest that the kinase domain deleted by gene targeting plays a suppressive role for the development of renal fibrosis through inhibition of the tubular epithelial-to-mesenchymal transition in a mouse model of COU. (elsevier.com)

The catalytic recombination of the ions by the cold wall along with accurately linearized mass diffusion fluxes ensures a realistic behavior of the ionized species and enhances the numerical stability of the linear system. (umn.edu)

The histograms below the weblogo indicate mutations found on the domain. (umbc.edu)

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)
There is a pocket extending from the catalytic site to an anion-binding site containing a chloride about 14 A away. (rcsb.org)
Binding of Mg nucleotides to the nucleotide-binding domains (NBDs) of SUR1 stimulates channel opening and leads to membrane hyperpolarization and inhibition of insulin secretion. (ox.ac.uk)
CoA binding domain [Interproscan]. (ntu.edu.sg)

A carefully designed non-uniform grid is employed with a periodic tracking of the shock front location, and the grid resoultion in the computational domain is such that the regions near strong discontinuities and large viscous gradients are well resolved at all times. (umn.edu)

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)
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)
Zn-link": a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E. (ox.ac.uk)

We have shown earlier that the highly conserved catalytic domain of E. coli RNase E is a homotetramer [Callaghan, A. J. et al. (ox.ac.uk)

Sequence homology analysis of these genes with other species threonyl-tRNA synthetase showed that the shorter gene did not possess motif-2 and motif-3 of catalytic core that were conserved in class II aminoacyl-tRNA synthetases. (archive.org)

genetic organization and occurrence of conserved domains in isoenzymes. (nature.com)

The catalytic domains of beta-1,4-glucanases can be grouped into families of related amino acid sequences. (ubc.ca)

Splicing, the removal of introns from pre-mRNA, is mediated by spliceosomal complexes and occurs in two distinct catalytic steps. (bdbiosciences.com)

The overall folding and structure of the domain is similar to that found for Cdc25A. (rcsb.org)
We found that the catalytic domain of PARG is predicted to contain a mostly beta sheet structure and a secondary structure pattern similar to that observed in the ADP-ribosyltransferase fold found in PARP-1 and bacterial toxin ADP-ribosyltransferases. (medscitechnol.com)

IclR helix-turn-helix domain, Bacterial transcriptional regulator [Interproscan]. (ntu.edu.sg)

This family represents the catalytic domain of the TPS. (unl.edu)
One area of focus in the lab has centered on catalytic HECT-type E3 ubiquitin ligases of the Nedd4-family. (upenn.edu)

Anatomy13

Organisms15

Chemicals and Drugs112

Analytical, Diagnostic and Therapeutic Techniques and Equipment38

Phenomena and Processes78

Disciplines and Occupations1

Technology, Industry, Agriculture1

Information Science4

Health Care1

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

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

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

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

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

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

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

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

Catalytic Domain

Sequence Homology, Amino Acid

Molecular Sequence Data

Amino Acid Sequence

Binding Sites

Sequence Alignment

Cloning, Molecular

Recombinant Proteins

Models, Molecular

Crystallography, X-Ray

Protein Conformation

Recombinant Fusion Proteins

Catalysis

Protein Binding

Base Sequence

Mutagenesis, Site-Directed

Protein Structure, Secondary

Protein Structure, Tertiary

src Homology Domains

Protein Interaction Domains and Motifs

Escherichia coli

Structure-Activity Relationship

Kinetics

Substrate Specificity

DNA, Complementary

Amino Acid Motifs

Dimerization

Conserved Sequence

Phosphorylation

Mutation

Sequence Deletion

Cellulase

Chitinase

Peptide Fragments

DNA Primers

Transfection

Mutagenesis

Bacterial Proteins

Enzyme Activation

Protein Folding

Amino Acid Substitution

Hydrolysis

Cell Line

Membrane Proteins

DNA

DNA-Binding Proteins

Point Mutation

PDZ Domains

Protein Structure, Quaternary

Signal Transduction

Saccharomyces cerevisiae

Cell Membrane

Plasmids

Electrophoresis, Polyacrylamide Gel

Carrier Proteins

Endo-1,4-beta Xylanases

Protein Kinases

Transcription Factors

Crystallization

Enzyme Stability

Peptides

Two-Hybrid System Techniques

Phylogeny

Structural Homology, Protein

Cellulose

Protein Multimerization

HeLa Cells

Nuclear Magnetic Resonance, Biomolecular

Ligands

Protein Tyrosine Phosphatases

Glycoside Hydrolases

Isoenzymes

Cysteine

Protein-Tyrosine Kinases

Metalloendopeptidases

Biocatalysis

Xylosidases

Protein Transport

Cercopithecus aethiops

Restriction Mapping