An essential amino acid. It is often added to animal feed.
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.
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 parts of a macromolecule that directly participate in its specific combination with another molecule.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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).
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.
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.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The rate dynamics in chemical or physical systems.
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 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 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.
Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Proteins prepared by recombinant DNA technology.
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.
Formation of an acetyl derivative. (Stedman, 25th ed)
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An essential amino acid that is physiologically active in the L-form.
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.
An essential amino acid that is required for the production of HISTAMINE.
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.
Drugs and their metabolites which are found in the edible tissues and milk of animals after their medication with specific drugs. This term can also apply to drugs found in adipose tissue of humans after drug treatment.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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 region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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.
Established cell cultures that have the potential to propagate indefinitely.
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).
Pesticides or their breakdown products remaining in the environment following their normal use or accidental contamination.
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.
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)
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.
Proteins found in any species of bacterium.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
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.
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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)
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.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
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.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
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).
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The process of cleaving a chemical compound by the addition of a molecule of water.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
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.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A metabolite in the principal biochemical pathway of lysine. It antagonizes neuroexcitatory activity modulated by the glutamate receptor, N-METHYL-D-ASPARTATE; (NMDA).
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.
The sum of the weight of all the atoms in a molecule.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.
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.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
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)
A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
Proteins obtained from ESCHERICHIA COLI.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.
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 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 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.
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.
Measurement of the intensity and quality of fluorescence.
The thermodynamic interaction between a substance and WATER.
Preservative for wines, soft drinks, and fruit juices and a gentle esterifying agent.
The accumulation of an electric charge on a object
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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).)
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.
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.
Compounds used extensively as acetylation, oxidation and dehydrating agents and in the modification of proteins and enzymes.
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 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.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
Transport proteins that carry specific substances in the blood or across cell membranes.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
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.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A sulfur-containing essential L-amino acid that is important in many body functions.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Enzymes that catalyse the removal of methyl groups from LYSINE or ARGININE residues found on HISTONES. Many histone demethylases generally function through an oxidoreductive mechanism.
The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.
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.
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 subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
Deletion of sequences of nucleic acids from the genetic material of an individual.
Peptides composed of between two and twelve amino acids.
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)
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
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.
An essential branched-chain amino acid important for hemoglobin formation.
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.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
A reagent that is highly selective for the modification of arginyl residues. It is used to selectively inhibit various enzymes and acts as an energy transfer inhibitor in photophosphorylation.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.
Amino acids with side chains that are positively charged at physiological pH.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The characteristic three-dimensional shape of a molecule.
Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.
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 mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Biochemical identification of mutational changes in a nucleotide sequence.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
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.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
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.
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.
Sites on an antigen that interact with specific antibodies.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
The amounts of various substances in food needed by an organism to sustain healthy life.
A class of inorganic or organic compounds that contain the borohydride (BH4-) anion.
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.
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.
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.
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.
The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.
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.
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.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
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 brominating agent that replaces hydrogen atoms in benzylic or allylic positions. It is used in the oxidation of secondary alcohols to ketones and in controlled low-energy brominations. (From Miall's Dictionary of Chemistry, 5th ed; Hawley's Condensed Chemical Dictionary, 12th ed,).
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.
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
A family of histone demethylases that share a conserved Jumonji C domain. The enzymes function via an iron-dependent dioxygenase mechanism that couples the conversion of 2-oxoglutarate to succinate to the hydroxylation of N-methyl groups.
A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.
Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.
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 cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
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.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
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 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.
The functional hereditary units of BACTERIA.
The characteristic 3-dimensional shape of a carbohydrate.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Foodstuff used especially for domestic and laboratory animals, or livestock.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Corrosive oxidant, explosive; additive to diesel and rocket fuels; causes skin and lung irritation; proposed war gas. A useful reagent for studying the modification of specific amino acids, particularly tyrosine residues in proteins. Has also been used for studying carbanion formation and for detecting the presence of double bonds in organic compounds.
A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
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.
Proteins found in any species of virus.
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.
A foul-smelling diamine formed by bacterial decarboxylation of lysine.
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)
Compounds containing the -SH radical.
Elements of limited time intervals, contributing to particular results or situations.
The relationships of groups of organisms as reflected by their genetic makeup.
A 1.5-kDa small ubiquitin-related modifier protein that can covalently bind via an isopeptide link to a number of cellular proteins. It may play a role in intracellular protein transport and a number of other cellular processes.
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
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.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
Computer-based representation of physical systems and phenomena such as chemical processes.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Baynes JW, Thorpe SR, Murtiashaw MH (1984). "Nonenzymatic glucosylation of lysine residues in albumin". Methods in Enzymology. ... It forms after glucose reacts with primary amino groups of lysine or arginine found in proteins. Because of the increased ... lysine, and pentosidine. 3DG as well as AGEs play a role in the modification and cross-linking of long-lived proteins such as ...
Proteins are usually ubiquinated at lysine residues. Human [[p14ARF]], however, does not contain any lysines, and mouse p19Arf ... Penultimate residues affect the efficiency of acetylation, in that acetylation is promoted by acidic residues and inhibited by ... If the mouse lysine is replaced with arginine, there is no effect on its degradation, suggesting it is also ubiquinated at the ... and it contains little or no lysine. Due to these characteristics, ARF is likely to be unstructured unless it is bound to other ...
Proteins are usually glycated through their lysine residues. In humans, histones in the cell nucleus are richest in lysine, and ... Ansari NA, Moinuddin, Ali R (2011). "Glycated lysine residues: a marker for non-enzymatic protein glycation in age-related ... Semba, R.; Najjar, S.; Sun, K.; Lakatta, E.; Ferrucci, L. (2009). "Serum carboxymethyl-lysine, an advanced glycation end ...
To produce carnitine, lysine residues are methylated to trimethyllysine. Four enzymes are involved in the conversion of ...
The metabolite is generated from a lysine residue after lysine reacts with cyanate. Cyanate is present in the human body in ... Carbamylation of nucleophilic amino groups, for example lysine residues, can modify protein structures and ultimately cause ... Increased levels of cyanate can now carbamylate lysine residues. Myeloperoxidase released from neutrophils converts thiocyanate ... These are lysine, arginine, and ornithine. These amino acids are found in many protein-rich foods. Since in this disorder the ...
Digestion with a proteinase having specificity for lysine residues". Biochem. J. 149: 497-506. PMC 1165654. PMID 1239277. Lewis ...
Ubiquitin residues are usually added to the lysine at position 120 on histone H2B. Ubiquitinating this lysine residue activates ... Adding an acetyl group to lysine residues in one of several positions in the amino acid tail contributes to the activation of ... Furthermore, acetylation of a specific lysine residue binds to bromine-containing domains of certain transcription and ... When a cell experiences metabolic stress, an AMP-activated protein kinase phosphorylates the lysine at position 36 in histone ...
... is modified by a different group of enzymes than other H4 lysines. Proteins are typically acetylated on lysine residues ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ... is a mark indicating the acetylation at the 8th lysine residue of the histone H4 protein. It has been implicated in the ...
These lysine residues are located within the DNA-binding domain; acetylation inhibits the ability of FOXO1 to interact with the ... It is primarily regulated through phosphorylation on multiple residues; its transcriptional activity is dependent on its ...
It is a mark that indicates the acetylation at the 5th lysine residue of the histone H2B protein. H2BK5ac is involved in ... Proteins are typically acetylated on lysine residues and this reaction relies on acetyl-coenzyme A as the acetyl group donor. ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ...
It is a mark that indicates the acetylation at the 36th lysine residue of the histone H3 protein. H3K36ac has not been widely ... Proteins are typically acetylated on lysine residues and this reaction relies on acetyl-coenzyme A as the acetyl group donor. ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ...
It is a mark that indicates the acetylation at the 91st lysine residue of the histone H4 protein. No known diseases are ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... Proteins are typically acetylated on lysine residues and this reaction relies on acetyl-coenzyme A as the acetyl group donor. ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ...
It is a mark that indicates the di-methylation at the 79th lysine residue of the histone H3 protein. H3K79me2 is detected in ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The di-methylation denotes the methylation present in ... Chen Y, Zhu WG (July 2016). "Biological function and regulation of histone and non-histone lysine methylation in response to ...
"PARP1 ADP-ribosylates lysine residues of the core histone tails". Nucleic Acids Research. 38 (19): 6350-6362. doi:10.1093/nar/ ... It was later reported that branching can occur every 20 to 30 ADP residues. The first appearance of mono-ADP-ribosylation ... In order for this step to occur, the arginine nucleophile is deprotonated by a glutamate residue on the catalyzing enzyme[ ... However, many other ADP-ribose acceptor sites such as serine, arginine, cysteine, lysine, diphthamide, phosphoserine, and ...
It is a mark that indicates the mono-methylation at the 4th lysine residue of the histone H3 protein and often associated with ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The mono-methylation denotes the methylation present in ... Hyun, Kwangbeom; Jeon, Jongcheol; Park, Kihyun; Kim, Jaehoon (2017). "Writing, erasing and reading histone lysine methylations ...
4 ubiquitination sites are found on Four different Lysine residues. They can be found at Lys78, Lys103, Lys113, Lys339. ... Of the 42 conserved amino acid residues found within the IFFO1 sequence, 33 of them are found in the filament region. When ... IFFO1 contains a highly conserved filament domain that spans 299 amino acids from amino residue 230 to 529. This region has ... Multiple sequence alignments indicated that the Proline-Rich region from amino residues 39 to 61 near the 5' end of the ...
Second, some of the lysine residues are hydroxylated or glycosylated, and some lysine as well as hydroxylysine residues undergo ... In addition, crosslinks form between certain lysine and hydroxylysine residues. In the extracellular space in tissues, type III ... When the right-handed super-helix is formed, the glycine residues of each of the monomers is positioned at the center of the ... First, on the order of 145 prolyl residues of the 239 in the triple-helical domain are hydroxylated to 4-hydroxyproline by ...
These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... Lysine methylation is the addition of a methyl group to the lysine of histone proteins. This occurs via histone lysine ... the mono-methylation at the 36th lysine residue of the histone H3 protein. There are diverse modifications at H3K36, such as ... This diagram shows the progressive methylation of a lysine residue. The mono-methylation denotes the methylation present in ...
It is a mark that indicates the acetylation at the 56th lysine residue of the histone H3 protein. It is a covalent modification ... Proteins are typically acetylated on lysine residues and this reaction relies on acetyl-coenzyme A as the acetyl group donor. ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ...
It is a mark that indicates the mono-methylation at the 20th lysine residue of the histone H4 protein. This mark can be di- and ... It is also the only identified methylated lysine residue on the H4 histone. Each degree of methylation at H4K20 has a very ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The mono-methylation denotes the methylation present in ...
It is a mark that indicates the di-methylation at the 9th lysine residue of the histone H3 protein. H3K9me2 is strongly ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... "Histone-lysine N-methyltransferase, H3 lysine-9 specific 3". HIstome: The Histone Infobase. Retrieved 8 June 2018. Cloos PA, ... This diagram shows the progressive methylation of a lysine residue. The di-methylation denotes the methylation present in ...
It is a mark that indicates the acetylation at the 23rd lysine residue of the histone H3 protein. H3K23ac is not well studied ... Proteins are typically acetylated on lysine residues and this reaction relies on acetyl-coenzyme A as the acetyl group donor. ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal ...
It is a mark that indicates the di-methylation at the 36th lysine residue of the histone H3 protein. There are diverse ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The di-methylation denotes the methylation present in ... H3K36me2 indicates dimethylation of lysine 36 on histone H3 protein subunit: ...
These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The tri-methylation denotes the methylation present in ... It is a mark that indicates the tri-methylation of lysine 27 on histone H3 protein. This tri-methylation is associated with the ... A polycomb repressive complex (PRC); PRC2, mediates the tri-methylation of histone 3 on lysine 27 through histone methyl ...
It is a mark that indicates the tri-methylation at the 36th lysine residue of the histone H3 protein and often associated with ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The tri-methylation denotes the methylation present in ... H3K36me3 indicates trimethylation of lysine 36 on histone H3 protein subunit: ...
Lysine residues can be singly, doubly and even triply methylated. Methylation does not alter the positive charge on the side ... methylation Several protein residues can be methylated, most notably the positive groups of lysine and arginine. Arginine ... Functionally, however, the acetylation of lysine residues is used to regulate the binding of proteins to nucleic acids. The ... hydroxylation Proline residues may be hydroxylates at either of two atoms, as can lysine (at one atom). Hydroxyproline is a ...
It is a mark that indicates the tri-methylation at the 4th lysine residue of the histone H3 protein and often involved in the ... These core histones are rich in lysine and arginine residues. The carboxyl (C) terminal end of these histones contribute to ... This diagram shows the progressive methylation of a lysine residue. The tri-methylation denotes the methylation present in ... The name denotes the addition of three methyl groups (trimethylation) to the lysine 4 on the histone H3 protein. H3 is used to ...
Two acylation sites are located at lysine residues K860 and K983. The part of the toxin from residue 400 to the C-terminus, ... between residues 500 and 700, there is a hydrophobic domain; and from residue 1000 to the C-terminus, there are calcium binding ... The acylation of lysines is required for the pore-forming cytotoxic effects of all the RTX proteins. Toxins from many known ... The protein consists of three domains: from the N-terminus up to roughly residue 400, there is an adenylate-cyclase domain; ...
... by lysyl oxidase which links hydroxylysine and lysine residues. Multiple collagen fibrils form into collagen fibers. Collagen ... The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp, where X may be any of various other amino acid residues. Proline ... Hydroxylation of lysine and proline amino acids occurs inside the lumen. This process is dependent on and consumes ascorbic ... In collagen, Gly is required at every third position because the assembly of the triple helix puts this residue at the interior ...
... is an acidic protein overall, with a predicted isoelectric point of approximately 5. TMEM171 has fewer lysine residues ... Despite the fact that its alias is proline-rich protein 2, TMEM171 in humans does not have more proline residues than expected ... More distant orthologs, including Xenopus tropicalis, do have significantly more proline residues than expected. TMEM171 has 3 ... The tertiary structure includes 2 predicted disulfide bridges, which occur between highly conserved cysteine residues in the ...
The single cysteine residue of A1AT in position 256 (UniProtKB nomenclature) is found to be covalently linked to a free single ... PiZ is caused by a glutamate to lysine mutation at position 342 (366 in pre-processed form) PiS is caused by a glutamate to ... a residue essential for binding elastase; this is thought to be one of the primary mechanisms by which cigarette smoking (or ...
High residue diet. *List of diets. *National Weight Control Registry. *Nutrigenomics. *Nutrition psychology ...
In peptides, L-amino acid residues slowly racemize, resulting in the formation of some D-amino acid residues. Racemization ... Some amino acids are prone to racemization, one example being lysine, which racemizes via formation pipecolic acid. ... Several antibiotics, e.g. bacitracin, contain D-amino acid residues.[1] Reference[edit]. *^ a b Mendel Friedman (1999). " ... D-Amino acids are most occasionally found in nature as residues in proteins. They are formed from ribosomally-derived D-amino ...
So H3K4me1 denotes the monomethylation of the 4th residue (a lysine) from the start (i.e., the N-terminal) of the H3 protein. ... Lysine methylation[edit]. The addition of one, two, or many methyl groups to lysine has little effect on the chemistry of the ... Lysine acetylation[edit]. Addition of an acetyl group has a major chemical effect on lysine as it neutralises the positive ... All histones have a highly positively charged N-terminus with many lysine and arginine residues. ...
Proteins are targeted for degradation by the proteasome with covalent modification of a lysine residue that requires the ... Each catalytic β subunit also possesses a conserved lysine residue required for proteolysis.[22] ... Ubiquitin contains seven lysine residues to which another ubiquitin can be ligated, resulting in different types of ... instead reducing the substrate to short polypeptides typically 7-9 residues long, though they can range from 4 to 25 residues, ...
Walker, K. C.; Goette, M. B.; Batchelor, G. S. (1954). "Pesticide Residues in Foods, Dichlorodiphenyltrichloroethane and ...
Two enzymes (ε-N-trimethyl-L-lysine hydroxylase and γ-butyrobetaine hydroxylase) that are necessary for synthesis of carnitine. ... Peptidylglycine alpha-amidating monooxygenase amidates peptide hormones by removing the glyoxylate residue from their c- ... that are required for the hydroxylation of proline and lysine in the synthesis of collagen.[92][93][94] These reactions add ... terminal glycine residues. This increases peptide hormone stability and activity.[99][100] ...
Low-fiber/low-residue diet - Diet that limits stool. *Protein-sparing modified fast ...
Acetylation occurs on the lysine residues found at the amino N-terminal of histone tails. Histone acetylation is most commonly ... Acetylation of lysine residues on histone tails is typically associated with transcriptional activation, whereas deacetylation ... most commonly on lysine residues.[4] CpG refers to a dinucleotide composed of a cytosine deoxynucleotide immediately adjacent ... The effects of histone methylation are residue dependent (e.g. which amino acid on which histone tail is methylated) therefore ...
Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine". The Journal of ... AKR1B1 consists of 316 amino acid residues and weighs 35853Da. It does not possess the traditional dinucleotide binding fold. ... Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK (August 1993). "Identification of the reactive cysteine residue in human placenta ... lined by seven aromatic and four other non-polar residues.[7] ...
11-cis-retinal + aporhodopsin → rhodopsin + H2O; forms Schiff base linkage to lysine, -CH=N+H-, ... Bovine rhodopsin contains 348 amino acid residues. The retinal chromophore binds at Lys296. ... Retinal binds covalently to a lysine on the transmembrane helix nearest the C-terminus of the protein through a Schiff base ... Schiff base linkage involves removing the oxygen atom from retinal and two hydrogen atoms from the free amino group of lysine, ...
... lysine and arginine methylation, serine and threonine phosphorylation, and lysine ubiquitination and sumoylation) play central ... "Genome-wide mapping of methylated adenine residues in pathogenic Escherichia coli using single-molecule real-time sequencing" ... For example, lysine acetylation may create a binding site for chromatin-modifying enzymes (or transcription machinery as well ... For example, acetylation of the K14 and K9 lysines of the tail of histone H3 by histone acetyltransferase enzymes (HATs) is ...
Essential binding site residues (Backbone Brackets and Arginine Tweezers) are colored. N-terminal residues are highlighted in ... While class I binds via interactions mediated by backbone hydrogen bonds, class II uses a pair of arginine residues to ...
Low-fiber/low-residue diet. *Monotrophic diet. *NPO. *Renal diet. *Soft diet ...
Next, a nearby tyrosine residue deprotonates the ε-amino group of the lysine residue.[10] The lysine chain then makes a ... Unlike the SET domain, which targets the lysine tail region of the histone, Dot1 methylates a lysine residue in the globular ... Active site of Histone Lysine N-Methyltransferase. Lysine residue (in yellow) and S-Adenosyl methionine (SAM) (in blue) clearly ... The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4.[1] Two ...
The standard replacement, Forane 141 is much less effective, and tends to leave a residue. 1,1,1-Trichloroethane was used as a ...
... acidic residues red, basic residues blue, polar residues green, nonpolar residues white). ... which catalyses the first step in the synthesis of lysine, methionine, and threonine from aspartate. If amino acids are present ... The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino ... However, the boundary between the two is not well defined and usually lies near 20-30 residues.[5] Polypeptide can refer to any ...
This widely held belief stems from some people mistaking the thin coat of residue left behind after consuming milk or ice cream ...
Its amino acid sequence is highly conserved in eukaryotes, differing by only a few residues. In more than thirty species, 34 of ... Ng S, Smith MB, Smith HT, Millett F (Nov 1977). "Effect of modification of individual cytochrome c lysines on the reaction with ... It has the heme-attachment site towards the N terminus of histidine and the sixth ligand provided by a methionine residue ... or nitrogen dioxide NO2 in the mitochondria can be lethal since they nitrate tyrosine residues of cytochrome c which leads to ...
Methylation: Both lysine and arginine residues are known to be methylated. Methylated lysines are the best understood marks of ... Similarly, the combination of phosphorylation of serine residue 10 and acetylation of a lysine residue 14 on histone H3 is a ... And this does not include lysine acetylation (known for H3 at nine residues), arginine methylation (known for H3 at three ... Methylation of lysines H3K9 and H3K27 is correlated with transcriptional repression.[3] Particularly, H3K9me3 is highly ...
... prodrugs transfer acyl group to 36th cysteine residue of NCp7 and the acyl group then migrates to neighboring lysine residue ... In the same manner as ADA, the compounds interact with an 18-residue polypeptide on the N terminal zinc knuckle region of the ... They react with the cysteine residues on the zinc finger of the NCp7 and cause a covalent conformation change which ejects the ... HIV nucleocapsid protein which causes ejection of the zinc from the region by covalently modifying the cysteine residues. ...
The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target ... is responsible for binding the target protein substrate and transferring the ubiquitin from the E2 cysteine to a lysine residue ... first activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. The activated ubiquitin ...
... in the cytoplasm of some cells are basic because they are positively charged due to the arginine and lysine amino-acid residues ... It binds to acidophilic substances such as positively charged amino-acid side chains (e.g. lysine, arginine). ...
by mouth, rectal, lysine acetylsalicylate may be given intravenously or intramuscularly. ATC code. *A01AD05 (WHO) B01AC06 (WHO ... Aspirin acts as an acetylating agent where an acetyl group is covalently attached to a serine residue in the active site of the ...
... is the cross-linking of a glutamine residue from the gliadin peptide to a lysine residue of tTg in a reaction that is catalysed ... Deamidation is the reaction by which a glutamate residue is formed by cleavage of the epsilon-amino group of a glutamine side ...
The electrons yielded are transferred to a redox-active tyrosine residue that then reduces the oxidized P680. This resets the ...
... nucleotide in the siRNA and a conserved tyrosine residue. This site is thought to form a nucleation site for the binding of the ... "Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi". Science. 297 (5588): 1833-7. Bibcode ...
In animals apoptosis is induced by caspases and in fungi and plants, apoptosis is induced by arginine and lysine-specific ... a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of ...
... which binds to acetylated lysine residues.[5] Those in the MYST family have HAT domains that are about 250 residues in length. ... Lysines 9, 14, 18, and 23 of H3 and lysines 5, 8, 12, and 16 of H4 are all targeted for acetylation.[3][22] Lysines 5, 12, 15, ... This happens to be the case as well for Sas3, which is observed to acetylate H3K9 and H3K14 in vivo as well as lysine residues ... In human p300, Tyr1467 acts as a general acid and Trp1436 helps orient the target lysine residue of the histone substrate into ...
Each MurNAc is attached to a short (4- to 5-residue) amino acid chain, containing L-alanine, D-glutamic acid, meso- ... L-lysine, and D-alanine with a 5-glycine interbridge between tetrapeptides in the case of Staphylococcus aureus (a Gram- ... The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM ... Some archaea have a similar layer of pseudopeptidoglycan (also known as pseudomurein), in which the sugar residues are β-(1,3) ...
Lysine residues, or arginine residues in some bacteria, and their positive charges are intrinsic components of many of these ... the lysine residues at the beginning of the C-terminal α-helix are purple, and alanine residues that influence the symmetry of ... The region of the c11-ring in contact with the outer leaflet of the membrane has no lysine residues in the head-group region ... Larger rings of known structure, from c9-c15 in eubacteria and chloroplasts, conserve either a lysine or an arginine residue in ...
Ubiquitination of RasG occurred on K-Ras specific lysine residues. A, ubiquitination (Ub.) sites in RasG was identified by ... Degradation of activated K-Ras orthologue via K-Ras-specific lysine residues is required for cytokinesis.. Sumita K1, Yoshino H ... Degradation of Activated K-Ras Orthologue via K-Ras-specific Lysine Residues Is Required for Cytokinesis ... Degradation of Activated K-Ras Orthologue via K-Ras-specific Lysine Residues Is Required for Cytokinesis ...
Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila ... H4 acetylated at lysine 16 is found at numerous sites along the transcriptionally hyperactive X chromosome in male larvae, but ... beta-Heterochromatin in the chromocenter is depleted in these isoforms, but relatively enriched in H4 acetylated at lysine 12. ... Histone H4 isoforms acetylated at lysines 5, 8, 12, or 16 have been shown, by indirect immunofluorescence with site-specific ...
We demonstrated that chemical modification of lysine residues resulted in loss of ligand binding activity. Of the 27 lysine ... We conclude that the three lysine residues Lys-82, Lys-163, and Lys-170 are crucial for the binding of DbpA to decorin. ... Analysis of recombinant DbpA in which individual lysine residues have been mutated to alanine suggested that three of the ... We have now examined the importance of individual amino acid residues in DbpA for decorin binding. ...
... amino group of a lysine residue and is important for regulating protein functions in various organisms from bacteria to humans ... Lysine acetylation refers to addition of an acetyl moiety to the epsilon‐ ... Lysine acetylation refers to addition of an acetyl moiety to the epsilon‐amino group of a lysine residue and is important for ... Comprehensive lysine acetylomes emerging from bacteria to humans. Trends Biochem. Sci. 36:211‐220. doi: 10.1016/j.tibs.2010.10. ...
Abstract 20476: Cardiac Myosin Heavy Chain Isoforms Are Acetylated at Lysine Residues, Resulting in Enhanced Enzymatic and ... Abstract 20476: Cardiac Myosin Heavy Chain Isoforms Are Acetylated at Lysine Residues, Resulting in Enhanced Enzymatic and ... Abstract 20476: Cardiac Myosin Heavy Chain Isoforms Are Acetylated at Lysine Residues, Resulting in Enhanced Enzymatic and ... Abstract 20476: Cardiac Myosin Heavy Chain Isoforms Are Acetylated at Lysine Residues, Resulting in Enhanced Enzymatic and ...
... mediated phosphorylation of specific serine residues in the C-terminal domain of p100, leading to recruitment of the S … ... We identified a single lysine residue, K855, that serves as the ubiquitin-anchoring residue required for signal-induced ... identification of the specific polyubiquitin chain-anchoring lysine residue and analysis of the role of NEDD8-modification on ... In contrast, p105, the p100 homologue, lacks a similar Lys residue. We also demonstrate that the NEDD8 pathway is essential for ...
In contrast, lysine methylation did not affect the binding affinity of Tat peptide to TAR RNA at K50, nonetheless three fold ... Lysine can undergo various PTMs and thereby contribute to the regulation of different cellular processes. It can be reversibly ... Here we have delineated the thermodynamic and kinetic effects of N-acetylation and N-monomethylation of lysine on interaction ... In spite of large enthalpy-entropy compensation, lysine methylation seems to have more pronounced position specific effect on ...
In conclusion, lysine residues at positions 4 and 7 on Nef were found to be indispensable for interacting with calnexin and ... Abstract 151: Lysine Residues at Positions 4 and 7 on Nef are Critical for Interaction with Calnexin and Drive Inhibition of ... Abstract 151: Lysine Residues at Positions 4 and 7 on Nef are Critical for Interaction with Calnexin and Drive Inhibition of ... Abstract 151: Lysine Residues at Positions 4 and 7 on Nef are Critical for Interaction with Calnexin and Drive Inhibition of ...
Extensive phosphorylation of serine residues at the largest RNAPII subunit occurs at its structura … ... Methylation of RNA polymerase II non-consensus Lysine residues marks early transcription in mammalian cells Elife. 2015 Dec 19; ... and di-methylation of CTD Lysine-7 residues (K7me1 and K7me2). K7me1 and K7me2 are observed during the earliest transcription ... In vertebrates, the CTD has eight non-canonical substitutions of Serine-7 into Lysine-7, which can be acetylated (K7ac). Here, ...
Biotinylation of lysine residues was decreased by acetylation of adjacent lysines but was increased by dimethylation of ... histone H2A is unique among histones in that its biotinylation sites include amino acid residues from the C-terminus. ... Biotinylation of lysine residues was decreased by acetylation of adjacent lysines but was increased by dimethylation of ... Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase ...
... Gunasekera ... A small 12-residues peptide, referred as KR-12, derived from LL-37, has been reported to have selective toxic effect on ... Residues 18-29 in LL-37 have previously been identified as a minimal peptide (KR-12) that retains antibacterial activity with ... Analogues of KR-12 were generated in the form of Alanine and Lysine scans to find out the positions important for improved ...
The LH3 has been shown to modify the lysine residues both in collagens and also in some collagenous proteins. In this study we ... Furthermore, loss of the terminal glucose units on the derivatized lysine residues in mouse embryonic fibroblasts lacking the ... Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin..pdf. Published (publisher ... Lysyl Hydroxylase 3 Modifies Lysine Residues to Facilitate Oligomerization of Mannan-Binding Lectin. ...
... novel Maillard reaction products and cross-links from the reaction of triose sugars with lysine and arginine residues ... novel Maillard reaction products and cross-links from the reaction of triose sugars with lysine and arginine residues. ... novel Maillard reaction products and cross-links from the reaction of triose sugars with lysine and arginine residues. Biochem ... From the incubation of glyceraldehyde with Nα-acetyl-l-lysine and Nα-acetyl-l-arginine, we isolated four new Maillard reaction ...
Maleimide-functionalized closo-dodecaborate albumin conjugates (MID-AC): Unique ligation at cysteine and lysine residues ... Maleimide-functionalized closo-dodecaborate albumin conjugates (MID-AC): Unique ligation at cysteine and lysine residues ... Maleimide-functionalized closo-dodecaborate albumin conjugates (MID-AC): Unique ligation at cysteine and lysine residues ... Unique ligation at cysteine and lysine residues enables efficient boron delivery to tumor for neutron capture therapy. ...
... in which the active site lysine residue has been exchanged for a histidine residue, retain partial catalytic competence [Ziak ... in which the active site lysine residue has been exchanged for a histidine residue, retain partial catalytic competence [Ziak ... The replacement of the active site K258 by a histidine residue resulted only in local structural adaptations necessary to ... The replacement of the active site K258 by a histidine residue resulted only in local structural adaptations necessary to ...
... modified the lysine residues of the beta subunit of ATP synthase. Except for lysine residues in the N-terminal and C-terminal ... EFFECTS OF ENERGIZATION AND SUBSTRATES ON THE REACTIVITIES OF LYSINE RESIDUES OF THE CHLOROPLAST ATP SYNTHASE BETA SUBUNIT. ... Publications] Mizuho Komatsu-Takaki: Effects of energization and substrates on the reactivities of lysine residues of the ... Publications] MIZUHO KOMATSU-TAKAKI: EFFECTS OF ENERGIZATION AND SUBSTRATES ON THE REACTIVITIES OF LYSINE RESIDUES OF THE ...
... reveal that one end of the H2DIDS reacts covalently with a lysine residue that is between about 70 and 168 residues from the C ... The cleavage site, in human band 3, corresponds to Lys-761 in mouse band 3; the site is 168 residues from the C terminus of the ... terminus of band 3. In addition to placing restrictions on the location of the H2DIDS-binding lysine, these studies provide ... Localization of proteolytic cleavage sites and stilbenedisulfonate-binding lysine residues.}, author={Michael L Jennings and ...
Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin ... Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin ... Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin ... Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin ...
Site-specific glutamine conjugation with small peptides containing a lysine residue and a functional moiety is also described. ... site-specific conjugation to glutamine and lysine residues of IgG1 antibody. ... In addition it is showed that immobilized MTG shows enhanced selectivity towards a certain residue in the presence of several ... It is also reported on the site-specific lysine conjugation of antibodies using potent glutamine containing peptides with ...
GO:0018024 histone-lysine N-methyltransferase activity GO:0031151 histone methyltransferase activity (H3-K79 specific) ... Per-residue features. Residue annotation. Colour by help domain relationship. source database. ...
Lysine-tRNA ligase, class II (IPR002313)*Bacterial/eukaryotic lysine-tRNA ligase, class II (IPR034762) ... Per-residue features. Residue annotation. Colour by help domain relationship. source database. ...
Introduction of lysine residues into the mouse receptor can increase sensitivity to NF449. A, representative traces of membrane ... fig3: Introduction of lysine residues into the mouse receptor can increase sensitivity to NF449. A, representative traces of ... fig3: Introduction of lysine residues into the mouse receptor can increase sensitivity to NF449. A, representative traces of ... The results explain the marked species difference in antagonist sensitivity and identify an ectodomain lysine residue that ...
TG2 primarily targets lysine residues in Ab hinge regions. To find out which Ab lysine residues serve as TG2 substrates and ... Identification of target lysine residues. To identify Ab lysine residues targeted by TG2, cross-linking was carried out as ... In IgD, all eight hinge lysine residues were replaced with alanine to obtain the mutant H:K. Six additional lysine residues ... a lysine residue in the middle part of the CH2 region (K282) was picked up. Interestingly, this lysine residue is predicted to ...
A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation ... R)-N6-(S8-succinyldihydrolipoyl)-L-lysine residue*Search proteins in UniProtKB for this molecule. ... R)-N6-dihydrolipoyl-L-lysine residue*Search proteins in UniProtKB for this molecule. ... Dihydrolipoyllysine-residue succiny.... Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate ...
Identification of Catalytic Cysteine, Histidine, and Lysine Residues in Escherichia coli Homoserine Transsuccinylase † ...
SucStruct: Prediction of succinylated lysine residues by using structural properties of amino acids. ... Prediction of succinylated lysine residues by using structural properties of amino acids. Analytical Biochemistry, 527 . 24 - ... Lysine succinylation, Structural features, Protein sequences, Amino acids, Prediction. Subjects:. Q Science , Q Science ( ... It alters the chemical structure of lysines, leading to remarkable changes in the structure and function of proteins. In ...
Interaction of arginine, lysine, and guanidine with surface residues of lysozyme: Implication to protein stability. Journal of ... Interaction of arginine, lysine, and guanidine with surface residues of lysozyme : Implication to protein stability. / Shah, ... Interaction of arginine, lysine, and guanidine with surface residues of lysozyme : Implication to protein stability. In: ... Interaction of arginine, lysine, and guanidine with surface residues of lysozyme: Implication to protein stability. ...
Several global lysine acetylome analyses have been carried out in various bacteria, but thus far there have been no reports of ... Several global lysine acetylome analyses have been carried out in various bacteria, but thus far there have been no reports of ... In this study, we analyzed the lysine acetylproteome of the human pathogen V. cholerae V52. By applying a combination of immuno ... In this study, we analyzed the lysine acetylproteome of the human pathogen V. cholerae V52. By applying a combination of immuno ...
Six lysine residues on c-Myc are direct substrates for acetylation by p300. / Zhang, Kangling; Faiola, Francesco; Martinez, ... Zhang K, Faiola F, Martinez E. Six lysine residues on c-Myc are direct substrates for acetylation by p300. Biochemical and ... Six lysine residues on c-Myc are direct substrates for acetylation by p300. In: Biochemical and Biophysical Research ... Zhang, K., Faiola, F., & Martinez, E. (2005). Six lysine residues on c-Myc are direct substrates for acetylation by p300. ...
  • Reversible lysine-acetylation of proteins is regulated by histone acetyl transferases and deacetylases (HDACs). (ahajournals.org)
  • MHC isoforms were prepared from control and PTU-treated mice, and examined for acetylation by western analysis with use of an anti-acetyl-lysine antibody. (ahajournals.org)
  • Biotinylation of lysine residues was decreased by acetylation of adjacent lysines but was increased by dimethylation of adjacent arginines. (unl.edu)
  • Protein lysine acetylation is recognized as an important reversible post translational modification in all domains of life. (frontiersin.org)
  • While its primary roles appear to reside in metabolic processes, lysine acetylation has also been implicated in regulating pathogenesis in bacteria. (frontiersin.org)
  • Several global lysine acetylome analyses have been carried out in various bacteria, but thus far there have been no reports of lysine acetylation taking place in the important human pathogen Vibrio cholerae . (frontiersin.org)
  • In conclusion, this is the first global protein lysine acetylome analysis of V. cholerae and should constitute a valuable resource for in-depth studies of the impact of lysine acetylation in pathogenesis and other cellular processes. (frontiersin.org)
  • Zhang, K , Faiola, F & Martinez, E 2005, ' Six lysine residues on c-Myc are direct substrates for acetylation by p300 ', Biochemical and Biophysical Research Communications , vol. 336, no. 1, pp. 274-280. (utmb.edu)
  • This histone mark poses unique features that differ from the widely studied histone lysine acetylation (K ac ) and methylation (K me ) marks. (nature.com)
  • Similarly, the combination of phosphorylation of serine residue 10 and acetylation of a lysine residue 14 on histone H3 is a tell-tale sign of active transcription . (wikipedia.org)
  • 2009 ). Lysine acetylation is deeply implicated in the control of highly regulated biological functions. (springer.com)
  • Acetylation/deacetylation of lysine residues. (springer.com)
  • The reaction of acetylation on the ε-nitrogen of lysine residues is catalyzed by enzymes within the histone acetyl transferase (HAT) family, using acetyl-coenzyme A (acetyl-CoA) as donor of acetyl moiety. (springer.com)
  • Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation. (yeastgenome.org)
  • Acetylation of lysine residues within proteins has emerged as an important mechanism used by cells to overcome this repression. (abcam.com)
  • The reversible lysine acetylation of histones and non-histone proteins plays a vital role in the regulation of many cellular processes including chromatin dynamics and transcription, gene silencing, cell cycle progression, apoptosis, differentiation, DNA replication, DNA repair, nuclear import, and neuronal repression. (abcam.com)
  • Interestingly, instead of directly acetylating NFAT, Gcn5 catalyzes histone H3 lysine H9 acetylation to promote IL-2 production. (jimmunol.org)
  • Acetylation is catalyzed by histone acetyltransferases (HATs), which add acetyl groups to lysine residues in their targets. (jimmunol.org)
  • As an HAT, Gcn5 has been shown to regulate gene transcription by catalyzing the acetylation of lysine residues on multiple histones including H2B, H3, and H4 ( 9 - 11 ). (jimmunol.org)
  • Lysine acetylation and its regulatory enzymes are known to have pivotal roles in mammalian cellular physiology. (mcponline.org)
  • Here we report the first global screening of lysine acetylation, identifying 138 modification sites in 91 proteins from Escherichia coli . (mcponline.org)
  • The new dataset suggests that lysine acetylation could be abundant in prokaryotic cells. (mcponline.org)
  • In addition, these results also imply that functions of lysine acetylation beyond regulation of gene expression are evolutionarily conserved from bacteria to mammals. (mcponline.org)
  • Furthermore, we demonstrate that bacterial lysine acetylation is regulated in response to stress stimuli. (mcponline.org)
  • Lysine acetylation is a dynamic, reversible, and regulatory post-translational modification in mammalian cells. (mcponline.org)
  • Lysine acetylation status and its regulatory enzymes have been shown to influence several fundamental cellular pathways in mammalian cells, including cell survival and apoptosis, cellular differentiation, and metabolism. (mcponline.org)
  • Emerging evidence suggests diverse non-nuclear roles of lysine acetylation and its regulatory enzymes, in addition to its well recognized functions in DNA-templated processes. (mcponline.org)
  • The roles of lysine acetylation in metabolism are further exemplified by the facts that the modification is present in more than 20% of mitochondrial proteins and is highly enriched among metabolic enzymes ( 11 - 14 ). (mcponline.org)
  • Although the inventory and biological functions of lysine acetylation substrates in eukaryotic cells have begun to unfold, especially in histone proteins and transcription factors ( 15 - 19 ), the nature of lysine acetylation substrates in prokaryotic cells remains largely unknown. (mcponline.org)
  • The high abundance of lysine acetylation in mammalian mitochondrial proteins implies the possible widespread existence of the modification in prokaryotes, given the evolutionary lineage of eukaryotic mitochondria from bacteria ( 20 ). (mcponline.org)
  • In Salmonella enterica, the lysine acetylation status of acetyl-CoA synthetase is regulated by CobB deacetylase, a Sir2 homolog in bacteria ( 21 , 26 ), as well as Pat acetyltransferase ( 27 ). (mcponline.org)
  • Despite evidence of the presence and roles of lysine acetylation in prokaryotes, the extent of lysine acetylation has not been carefully examined before. (mcponline.org)
  • Here we report the first global analysis of lysine acetylation in Escherichia coli . (mcponline.org)
  • The screening identified 138 lysine acetylation sites in 91 proteins in E. coli , of which 25% had mammalian orthologues. (mcponline.org)
  • Following ZEB1 induction, acetylation of histone H4 and histone H3 on lysine 9 (H3K9) and 27 (H3K27) was decreased on ZEB1 binding sites on these genes as demonstrated by chromatin immunoprecipitation. (mdpi.com)
  • Larger rings of known structure, from c 9 -c 15 in eubacteria and chloroplasts, conserve either a lysine or an arginine residue in the equivalent position. (pnas.org)
  • To understand this, we herein perform molecular dynamics simulations of lysozyme in the presence of three commonly used additives: arginine, lysine, and guanidine. (edu.kz)
  • arginine and lysine have aliphatic side chain, while arginine has a guanidinium group. (edu.kz)
  • Contact coefficient, quantified from contact frequencies, is helpful in analyzing the interactions with the guanidine groups as well as aliphatic side chains of arginine and lysine. (edu.kz)
  • Further analysis suggests that the hydration layer around the protein surface is depleted more in the presence of arginine, followed by lysine and guanidine. (edu.kz)
  • These results collectively indicate that the aliphatic chain of arginine and lysine plays a critical role in the stabilization of the protein. (edu.kz)
  • Shah, D & Shaikh, AR 2016, ' Interaction of arginine, lysine, and guanidine with surface residues of lysozyme: Implication to protein stability ', Journal of Biomolecular Structure and Dynamics , vol. 34, no. 1, pp. 104-114. (edu.kz)
  • Molecular modelling was used to identify three light chain constant domain surface arginine residues, R154, R187 and R210, which were mutated to lysine residues. (vtt.fi)
  • We conclude that selected lysine and arginine residues on the surface of DNase I constitute the major elements of the phosphotransferase recognition domain present on this secretory glycoprotein. (wustl.edu)
  • Both lysine and arginine residues are known to be methylated. (wikipedia.org)
  • Chemical modification of histidine and arginine residues does not inhibit the amidolytic activity of activated Hageman factor. (biomedsearch.com)
  • B ) HepG2 cells were transfected with empty vector (Control), wild-type Flag-SRSF3 (WT), or a series of single lysine-to-arginine mutants (K11R, K23R, K85R), double lysine mutants (K11/23R, K23/85R), or a triple lysine mutant (3KR) as indicated. (jci.org)
  • Treating wheat gluten, soy protein, and lactalbumin under alkaline conditions at 65°C for various times destroys part of the threonine, cystine, lysine, tyrosine, and arginine residues in these proteins. (springer.com)
  • It forms after glucose reacts with primary amino groups of lysine or arginine found in proteins. (wikipedia.org)
  • One is an enzymatic process, catalyzed by a protein acetyltransferase, where the acetyl group of acetyl coenzyme A is transferred to a lysine residue of a target protein. (frontiersin.org)
  • The other is non-enzymatic, where the acetyl group of acetyl phosphate is transferred directly to the lysine residue. (frontiersin.org)
  • Acetyl-coenzyme A (CoA) synthetase, CheY, and Alba are the only proteins in prokaryotes known to be lysine-acetylated ( 4 , 21 - 24 ). (mcponline.org)
  • Here, we describe mono- and di-methylation of CTD Lysine-7 residues (K7me1 and K7me2). (nih.gov)
  • Furthermore through the use of an activity-based strategy we determined METTL20 as an extremely specific MTase in charge of methylation of ETFβ and offer direct biochemical proof that METTL20 can be focusing on ETFβ at two residues specifically Lys200 and Lys203. (ranscombehouseglynde.com)
  • Histone methylation can be associated with either active or repressive signals and has also recently been discovered to be a dynamic process regulated not only by the addition of methyl groups by histone methyltransferases, but also by removal of methylation catalyzed by lysine-specific demethylase 1 (LSD1) and JmjC domain demethylases ( 6 - 10 ). (pnas.org)
  • Methylation of lysines H3K4 and H3K36 is correlated with transcriptional activation while demethylation of H3K4 is correlated with silencing of the genomic region. (wikipedia.org)
  • Methylation of lysines H3K9 and H3K27 is correlated with transcriptional repression. (wikipedia.org)
  • [4] Methylation of histone lysine also has a role in DNA repair . (wikipedia.org)
  • Chromatin modifications, including methylation of histone H3 at lysine 27 (H3K27me) by the Polycomb group proteins, play a broadly conserved role in the maintenance of cell fate. (genetics.org)
  • SIRT6 (sirtuin 6) belongs to the Sir2 (silencing information regulator 2) family of nicotinamide adenine dinucleotide (NAD + )-dependent protein lysine deacylases. (elifesciences.org)
  • Publications] Mizuho Komatsu-Takaki: 'Effects of energization and substrates on the reactivities of lysine residues of the chloroplast ATP synthase β subunit' Eur.J.Biochem. (nii.ac.jp)
  • These include chains anchored to residues other than internal lysine in the substrates, chains assembled through linking residues other than lysine 48 in ubiquitin, and mixed chains made of both ubiquitin and a ubiquitin-like protein. (biologists.org)
  • Ubiquitin is activated by an ubiquitin-activating enzyme (E1), transferred to a ubiquitin-conjugating enzyme (E2) and, with the help of an ubiquitin ligase (E3), is covalently attached to lysine residues on specific substrates [ 2 ]. (hindawi.com)
  • Ubiquitin has seven lysine residues. (nature.com)
  • Ubiquitin itself contains seven lysine residues (K6, K11, K27, K29, K33, K48, and K63), and recent studies suggest that all seven lysines and the amino terminus of ubiquitin can be utilized to form a variety of branched or linear chains that are thought to determine the ultimate cellular fate of the ubiquitinated protein [ 9 , 10 ]. (hindawi.com)
  • Mapping data showed that multiple lysine residues are SUMO1 acceptors within S-HDAg. (pubmedcentralcanada.ca)
  • Interestingly, six of the candidates analyzed in this manner ( A-E and G ) appear as multiple bands in the SUMO sample, suggesting they have poly-SUMO chains, are sumoylated on multiple lysine residues, and/or are modified by both SUMO and Ub. (mcponline.org)
  • Mass spectrometry and Edman degradation of proteolytic products from mature toxin activated in vitro with tritium-labeled acylACP revealed two fatty-acylated internal lysine residues, lysine 564 and lysine 690. (sciencemag.org)
  • Understanding the role of internal lysine residues of serum albumins in conformational stability and bilirubin binding. (um.edu.my)
  • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. (nih.gov)
  • Dimethyl-lysine 4 histone H3 (H3K4me2) is a transcription-activating chromatin mark at gene promoters, and demethylation of this mark by the lysine-specific demethylase 1 (LSD1), a homologue of polyamine oxidases, may broadly repress gene expression. (pnas.org)
  • A key positive chromatin mark found associated with promoters of active genes is histone 3 dimethyl-lysine 4 (H3K4me2) ( 11 , 12 ). (pnas.org)
  • Furthermore, recent findings suggest that bromodomain/acetylated-lysine recognition can serve as a regulatory mechanism in protein-protein interactions in numerous cellular processes such as chromatin remodeling and transcriptional activation. (abcam.com)
  • tagging system conserved in and (50) that mediates the covalent attachment of Pup to the lysine residues of target proteins (99). (molecularcircuit.com)
  • Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137). (genecards.org)
  • This antibody recognizes proteins acetylated on lysine residues. (abcam.com)
  • Pendant amino groups on lysine residues, guys. (nature.com)
  • 2 Side Chain Amino Groups of Lysine and Ornithine. (indigo.ca)
  • Furthermore, loss of the terminal glucose units on the derivatized lysine residues in mouse embryonic fibroblasts lacking the LH3 protein leads to defective disulphide bonding and oligomerization of rat MBL-A, with a decrease in the proportion of the larger functional MBL oligomers. (le.ac.uk)
  • In mouse embryonic fibroblasts (MEFs), Sirt6 knockout (KO) increased R-Ras2 lysine fatty acylation. (elifesciences.org)
  • Substitution of these lysine residues with arginines (4KR-RasG) diminished RasG ubiquitination and increased RasG protein stability. (nih.gov)
  • When Arg-27 was replaced with a lysine, phosphorylation increased to 54%, showing that phosphotransferase prefers lysine residues to arginines. (wustl.edu)
  • Degradation of activated K-Ras orthologue via K-Ras-specific lysine residues is required for cytokinesis. (nih.gov)
  • wherein the substantially monodispersed insulin polypeptide-oligomer conjugates comprise an insulin polypeptide and an oligomer and wherein the oligomer is coupled to a lysine at the B29 position of the insulin polypeptide. (google.com)
  • Chicken mitochondrial and Escherichia coli aspartate aminotransferases K258H, in which the active site lysine residue has been exchanged for a histidine residue, retain partial catalytic competence [Ziak et al. (uzh.ch)
  • The replacement of the active site K258 by a histidine residue resulted only in local structural adaptations necessary to accommodate the imidazole ring. (uzh.ch)
  • Activation is also inhibited by alteration of the other two basic amino acid residues present, lysine and histidine. (biomedsearch.com)
  • NF-kappa B-inducing kinase (NIK) induces I kappa B kinase alpha (IKK alpha)-mediated phosphorylation of specific serine residues in the C-terminal domain of p100, leading to recruitment of the SCF(beta-TrCP) ubiquitin ligase. (nih.gov)
  • Extensive phosphorylation of serine residues at the largest RNAPII subunit occurs at its structurally-disordered C-terminal domain (CTD), which is composed of multiple heptapeptide repeats with consensus sequence Y1-S2-P3-T4-S5-P6-S7. (nih.gov)
  • To identify the amino acid residues of DNase I that are required for interaction with phosphotransferase, wild-type and mutant forms of bovine DNase I were expressed in COS-1 cells and the extent of oligosaccharide phosphorylation determined. (wustl.edu)
  • Phosphorylation of DNase I oligosaccharides decreased from 12.6% to 2.3% when Lys-50, Lys-124, and Arg- 27 were mutated to alanines, indicating that these residues are required for the basal level of phosphorylation. (wustl.edu)
  • Mutation of lysines at other positions did not impair phosphorylation, demonstrating the selectivity of this process. (wustl.edu)
  • Mutation of Asn-74 to a lysine also increased phosphorylation to 50.3%, and the double mutant (R27K/N74K) was phosphorylated 79%, equivalent to the values obtained with lysosomal hydrolases. (wustl.edu)
  • Finally, mutation of Lys-117 to an alanine stimulated phosphorylation, demonstrating that some residues may be negative regulators of this process. (wustl.edu)
  • For example, phosphorylation of serine residues 10 and 28 on histone H3 is a marker for chromosomal condensation. (wikipedia.org)
  • Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. (uzh.ch)
  • Incubation of chloroplast thylakoids with pyridoxal 5'-phosphate for a short time (5s) modified the lysine residues of the beta subunit of ATP synthase. (nii.ac.jp)
  • SRSF3 was selectively neddylated at lysine 11 and mutation of this residue (SRSF3-K11R) was sufficient to prevent both SRSF3 degradation and alterations in RNA splicing. (jci.org)
  • Mutation of lysine 11 prevented SRSF3 protein degradation. (jci.org)
  • Prokaryotes form ubiquitin (Ub)-like isopeptide bonds on the lysine residues of proteins by at least two distinct pathways that are reversible and regulated. (molecularcircuit.com)
  • TtuB (tRNA-two-thiouridine B) which differ from Ub in sequence but share a common compact globular β-grasp fold (27 77 These Ub-fold proteins are linked by Gimatecan isopeptide bonds to lysine residues of protein targets by mechanisms that appear to be simple versions of ubiquitylation in their requirement for E1 (but not E2 or E3) enzyme homologs. (molecularcircuit.com)
  • The accepted 'canonical' signal for proteasomal recognition is a polyubiquitin chain that is anchored to a lysine residue in the target substrate, and is assembled through isopeptide bonds involving lysine 48 of ubiquitin. (biologists.org)
  • Abstract 20476: Cardiac Myosin Heavy Chain Isoforms Are Acetylated at Lysine Residues, Resulting in Enhanced Enzymatic and Contractile Activities of the Myosin Motor. (ahajournals.org)
  • SETD8/SET8/Pr-SET7/KMT5A is the only known lysine methyltransferase (KMT) that monomethylates lysine 20 of histone H4 (H4K20) in vivo. (biomedcentral.com)
  • We identified a single lysine residue, K855, that serves as the ubiquitin-anchoring residue required for signal-induced processing of p100. (nih.gov)
  • C ) HepG2 cells were transfected with Flag-SRSF3 or single lysine mutants (K11R, K23R, K85R) as indicated and treated with 500 μM PA for 12 hours. (jci.org)
  • Despite many modifications with important roles in cellular activity, lysine succinylation has recently emerged as an important PTM mark. (usp.ac.fj)
  • To test these proposed roles, the effects of mutations of each of these residues on the kinetic parameters and on the Mn 2+ , Mg 2+ , and substrate binding properties were examined. (elsevier.com)
  • Site-directed mutagenesis was used to investigate the roles of three lysine residues (K83, K196, and K215) situated near two metal-binding sites in bacteriophage T5 5'- 3' exonuclease. (elsevier.com)
  • Residues 18-29 in LL-37 have previously been identified as a minimal peptide (KR-12) that retains antibacterial activity with decreased cytotoxicity. (diva-portal.org)
  • A small 12-residues peptide, referred as KR-12, derived from LL-37, has been reported to have selective toxic effect on bacteria. (diva-portal.org)
  • This last type of peptide is characterized by the following two distinct features: 1) a missed tryptic cleavage at the modified lysine and 2) a 484.2-amu mass addition to this same lysine that corresponds to the five most C-terminal amino acids of SUMO (EQIGG). (mcponline.org)
  • The proteomics study involves efficient affinity enrichment of lysine-acetylated, tryptic peptides with anti-acetyllysine antibodies and subsequent peptide identification for nano-HPLC/mass spectrometric analysis. (mcponline.org)
  • Identification of critical lysine residues in DbpA required for decorin binding. (prohealth.com)
  • Neither K196 nor K215 was essential for either the exo- or the endonuclease activity, but mutation of these residues increased the dissociation constant for the substrate from 5 nM to 200 nM (K196A) and 50 nM (K215A). (elsevier.com)
  • Instead of using lysine 48 for the linkage, polyubiquitin chains can also be assembled through one of the six additional lysine residues in the molecule. (biologists.org)
  • Ubiquitin can form polyubiquitin chains via seven different lysine residues. (hindawi.com)
  • Substitution of the two lysines confirmed that they were the only sites of acylation and showed that although each was acylated in the absence of the other, both sites were required for in vivo toxin activity. (sciencemag.org)
  • They are also precursors for protein post-translational lysine acylation modifications. (nature.com)
  • However, the key elements that regulate this post-translational lysine acylation pathway remain unknown. (nature.com)
  • These results not only illustrate the landscape of this new lysine acylation pathway, but also open new avenues for studying diverse functions of cellular metabolites associated with this pathway. (nature.com)
  • Here, we report that a novel posttranslational mechanism, reversible lysine fatty acylation, regulates R-Ras2, a member of the Ras family. (elifesciences.org)
  • SIRT6, a sirtuin with established tumor suppressor function, regulates the lysine fatty acylation of R-Ras2. (elifesciences.org)
  • Lysine fatty acylation promotes the plasma membrane localization of R-Ras2 and its interaction with phosphatidylinositol 3-kinase PI3K, leading to activated Akt and increased cell proliferation. (elifesciences.org)
  • Our study establishes lysine fatty acylation as a previously unknown mechanism that regulates the Ras family of GTPases and provides an important mechanism by which SIRT6 functions as a tumor suppressor. (elifesciences.org)
  • Amino acid analysis of alkali-treated acylated proteins revealed that acylation by acetic and succinic anhydrides prevents or minimizes destruction of lysine residues and the formation of lysinoalanine in wheat gluten and soy protein and, in wool, minimizes destruction of cystine and lysine residues and the formation of lanthionine lysinoalanine. (springer.com)
  • Identified residues were mutated to confirm loss of interaction and this loss of interaction was found to associate with rescue of ABCA1 expression and restoration of cholesterol efflux. (ahajournals.org)
  • Lysines K82, K163, and K170 of DbpA are known to be important for in vitro interaction with decorin, and the DbpA structure, initially solved by nuclear magnetic resonance (NMR) spectroscopy, suggests these lysine residues colocalize in a pocket near the C terminus of the protein. (elsevier.com)
  • Taken together, these data showed that lysines K82, K163, and K170 potentiate the binding of DbpA to dermatan sulfate and that an interaction(s) mediated by these lysines is essential for B. burgdorferi murine infection. (elsevier.com)
  • Moreover, lysine residues appear to play a crucial role in the protein-protein interaction as binding of plasminogen was inhibited by the lysine analog tranexamic acid as well as increasing ionic strength. (frontiersin.org)
  • Concerning the involvement of specific amino acids in the interaction with plasminogen, lysine residues located at the C-terminus are frequently involved in the binding as reported for various other plasminogen-interacting proteins of Lyme disease spirochetes. (frontiersin.org)
  • However, binding of plasminogen to the mutated CbiA proteins was not affected, suggesting that lysine residues distant from the C-terminus might be involved in the interaction. (frontiersin.org)
  • Analysis of recombinant DbpA in which individual lysine residues have been mutated to alanine suggested that three of the conserved residues distributed throughout the DbpA sequence are required for decorin binding. (prohealth.com)
  • Analogues of KR-12 were generated in the form of Alanine and Lysine scans to find out the positions important for improved activity and selectivity. (diva-portal.org)
  • Lysine residues located within the C-terminal domain were substituted with alanine to generate single, double, triple, and quadruple point mutants. (frontiersin.org)
  • Our data suggest that LH3 is commonly involved in biosynthesis of collagenous proteins and the glucosylation of galactosylhydroxylysines residues by LH3 is crucial for the formation of the functional high-molecular weight MBL oligomers. (le.ac.uk)
  • Methylated lysines are the best understood marks of the histone code, as specific methylated lysine match well with gene expression states. (wikipedia.org)
  • Gene silencing by Polycomb group proteins is mediated in part through the di/trimethylation of histone H3 at lysine (K) 27 (H3K27me) by Polycomb Repressive Complex 2 (PRC2). (genetics.org)
  • Histone deacetylase inhibitors (HDACi) are epigenetically active drugs that induce the hyperacetylation of lysine residues within histone and non-histone proteins, thus affecting gene expression and cellular processes such as protein-protein interactions, protein stability, DNA binding and protein sub-cellular localization. (springer.com)
  • The mutations did not influence the affinity of the lysine-enriched Fab fragment and its labelling efficiency was found to be ∼40% higher than that of the wildtype Fab fragment With low degree of labelling, the affinities of the two Fab fragments were identical and comparable with that of the original monoclonal anti-hAFP IgG. (vtt.fi)
  • Untreated HeLa cells (upper panel), or overnight nocodazole treated HeLa cells (lower panel) stained with purified mouse monoclonal antibody against Acetylated Lysine (clone 15G10), followed by Rhodamine Red-X conjugated Donkey anti-mouse IgG and DAPI. (biolegend.com)
  • We hypothesized that species differences might result from differences in positive residues presented by the large receptor ectodomain. (nih.gov)
  • The results explain the marked species difference in antagonist sensitivity and identify an ectodomain lysine residue that plays a key role in the binding of both suramin and NF449 to P2X(1) receptors. (nih.gov)
  • Two-dimensional 1 H- 15 N HSQC and three- dimensional 1 H- 15 N NOESY-HSQC spectra of the kinetically damaged E53Q and E56Q mutants showed largely intact proteins with structural changes near the mutated residues. (elsevier.com)
  • 1 H- 15 N HSQC titrations of the E53Q, E56Q, and E44D mutants with dGTP showed changes in chemical shifts of residues lining the active site cleft, and revealed tighter nucleotide binding by these mutants, indicating an intact substrate binding site. (elsevier.com)
  • The infectivity of B. burgdorferi expressing individual dbpA lysine point mutants was assessed in mice challenged via needle inoculation. (elsevier.com)
  • Lysine residues at antibody surfaces are ready targets for labelling by an isothiocyanate derivative of the europium chelate (Eu3+). (vtt.fi)
  • [13] BARD1 tandem BRCA1 C-terminus (BRCT) motifs fold into a binding pocket with a key lysine residue (K619), and bind to poly(ADP-ribose) (PAR), which targets the BRCA1/BARD1 heterodimer to damaged DNA sites. (wikipedia.org)
  • In this paper, we propose an approach that utilizes structural features of amino acids to improve lysine succinylation prediction. (usp.ac.fj)
  • Ubiquitin can also be conjugated to the ε-NH 2 group of the N-terminal residue of the substrate. (biologists.org)
  • Covalent attachment of a single ubiquitin to the -amino group of a lysine residue in substrate proteins (monoubiquitination) can regulate their activity, ability to interact with other proteins, subcellular localization or trafficking. (hindawi.com)
  • We demonstrated that chemical modification of lysine residues resulted in loss of ligand binding activity. (prohealth.com)
  • It alters the chemical structure of lysines, leading to remarkable changes in the structure and function of proteins. (usp.ac.fj)
  • The effect of chemical modification of basic amino acid residues on the activation and amidolytic activity of Hageman factor (factor XII). (biomedsearch.com)
  • Thus, basic amino acid residues essential to the activation or activity of Hageman factor appear to be variably accessible to chemical modification. (biomedsearch.com)
  • In 2013, researchers found that SIRT6 can remove chemical groups known as fatty acyl groups from the lysine residues of proteins. (elifesciences.org)
  • The LH3 has been shown to modify the lysine residues both in collagens and also in some collagenous proteins. (le.ac.uk)
  • Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. (hmdb.ca)