Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Amino Acids: 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.Chromatography, Paper: An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Kinetics: The rate dynamics in chemical or physical systems.Magnetic Resonance Spectroscopy: 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).Anhydrides: Chemical compounds derived from acids by the elimination of a molecule of water.Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Chromatography, Thin Layer: Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Carbohydrates: 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.Molecular Sequence Data: 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.Oligosaccharides: 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.Borohydrides: A class of inorganic or organic compounds that contain the borohydride (BH4-) anion.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Carbohydrate Conformation: The characteristic 3-dimensional shape of a carbohydrate.Hydrogen-Ion Concentration: 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)Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Electrophoresis, Paper: Electrophoresis in which paper is used as the diffusion medium. This technique is confined almost entirely to separations of small molecules such as amino acids, peptides, and nucleotides, and relatively high voltages are nearly always used.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Structure-Activity Relationship: 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.Uronic Acids: Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)Amines: A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (From Grant & Hackh's Chemical Dictionary, 5th ed)Gas Chromatography-Mass Spectrometry: A microanalytical technique combining mass spectrometry and gas chromatography for the qualitative as well as quantitative determinations of compounds.Hydrochloric Acid: A strong corrosive acid that is commonly used as a laboratory reagent. It is formed by dissolving hydrogen chloride in water. GASTRIC ACID is the hydrochloric acid component of GASTRIC JUICE.Sulfuric Acids: Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.Lysine: An essential amino acid. It is often added to animal feed.GlucosamineOptical Rotation: The rotation of linearly polarized light as it passes through various media.Amino Acid Sequence: 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.Escherichia coli: 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.Molecular Structure: 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.Galactose: An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.Chromatography, Gas: Fractionation of a vaporized sample as a consequence of partition between a mobile gaseous phase and a stationary phase held in a column. Two types are gas-solid chromatography, where the fixed phase is a solid, and gas-liquid, in which the stationary phase is a nonvolatile liquid supported on an inert solid matrix.Trifluoroacetic Acid: A very strong halogenated derivative of acetic acid. It is used in acid catalyzed reactions, especially those where an ester is cleaved in peptide synthesis.Periodic Acid: A strong oxidizing agent.Neuraminic AcidsMethylation: 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)Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Polysaccharides, Bacterial: Polysaccharides found in bacteria and in capsules thereof.Indicators and Reagents: Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499)Spectrometry, Mass, Fast Atom Bombardment: A mass spectrometric technique that is used for the analysis of a wide range of biomolecules, such as glycoalkaloids, glycoproteins, polysaccharides, and peptides. Positive and negative fast atom bombardment spectra are recorded on a mass spectrometer fitted with an atom gun with xenon as the customary beam. The mass spectra obtained contain molecular weight recognition as well as sequence information.Chromatography, Ion Exchange: 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.Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.Succinic Anhydrides: A subclass of anhydrides with the general structure of dihydrofurandione. They can be substituted on any carbon atom. They modify and inhibit proteins and enzymes and are used in the acylation of amino- and hydroxyl groups.Molecular Weight: The sum of the weight of all the atoms in a molecule.Adenosine Triphosphate: 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.PolysaccharidesFucoseRhamnose: A methylpentose whose L- isomer is found naturally in many plant glycosides and some gram-negative bacterial lipopolysaccharides.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Protein Binding: 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.Glycosides: Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)Cattle: 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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Sugar AcidsPeptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Acetic Anhydrides: Compounds used extensively as acetylation, oxidation and dehydrating agents and in the modification of proteins and enzymes.Peptides: 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.Monosaccharides: Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)HexosaminesAmino Acid Substitution: 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.Amino Sugars: SUGARS containing an amino group. GLYCOSYLATION of other compounds with these amino sugars results in AMINOGLYCOSIDES.Glycolipids: Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)Cell Wall: The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.Disaccharides: Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.Acylation: The addition of an organic acid radical into a molecule.Protein Conformation: 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).Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Lipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.Spectrophotometry, Ultraviolet: 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)DNA: 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).Cloning, Molecular: 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.Fluorescamine: A nonfluorescent reagent for the detection of primary amines, peptides and proteins. The reaction products are highly fluorescent.Trypsin: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Imidoesters: Esters of the hypothetical imidic acids. They react with amines or amino acids to form amidines and are therefore used to modify protein structures and as cross-linking agents.Molecular Conformation: The characteristic three-dimensional shape of a molecule.Acids: Chemical compounds which yield hydrogen ions or protons when dissolved in water, whose hydrogen can be replaced by metals or basic radicals, or which react with bases to form salts and water (neutralization). An extension of the term includes substances dissolved in media other than water. (Grant & Hackh's Chemical Dictionary, 5th ed)HexosesBase Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Lipopolysaccharides: Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed)EstersGlycopeptides: Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.Phosphates: Inorganic salts of phosphoric acid.Electrophoresis: An electrochemical process in which macromolecules or colloidal particles with a net electric charge migrate in a solution under the influence of an electric current.Mutation: 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.Polyisoprenyl Phosphate Sugars: Compounds functioning as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. They include the polyisoprenyl pyrophosphates.Bacterial Proteins: Proteins found in any species of bacterium.Spectrophotometry, Infrared: Spectrophotometry in the infrared region, usually for the purpose of chemical analysis through measurement of absorption spectra associated with rotational and vibrational energy levels of molecules. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Oxidation-Reduction: 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).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.Rabbits: 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.Alanine: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Hydrofluoric Acid: Hydrofluoric acid. A solution of hydrogen fluoride in water. It is a colorless fuming liquid which can cause painful burns.Temperature: 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.Galactans: Polysaccharides composed of repeating galactose units. They can consist of branched or unbranched chains in any linkages.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Fatty Acids: Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Glycoside HydrolasesTritiumSpectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Adenosine Triphosphatases: A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.Guanosine Diphosphate Mannose: A nucleoside diphosphate sugar which can be converted to the deoxy sugar GDPfucose, which provides fucose for lipopolysaccharides of bacterial cell walls. Also acts as mannose donor for glycolipid synthesis.Sialic Acids: A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.O Antigens: The lipopolysaccharide-protein somatic antigens, usually from gram-negative bacteria, important in the serological classification of enteric bacilli. The O-specific chains determine the specificity of the O antigens of a given serotype. O antigens are the immunodominant part of the lipopolysaccharide molecule in the intact bacterial cell. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Dipeptides: Peptides composed of two amino acid units.Glycine: 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.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Dolichol Phosphates: Phosphoric acid esters of dolichol.Amino Alcohols: Compounds possessing both a hydroxyl (-OH) and an amino group (-NH2).Sequence Alignment: 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.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Protein Structure, Tertiary: 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.Chymotrypsin: 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.Sodium Hydroxide: A highly caustic substance that is used to neutralize acids and make sodium salts. (From Merck Index, 11th ed)Muramidase: A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.GalactosaminePhosphorus Radioisotopes: Unstable isotopes of phosphorus that decay or disintegrate emitting radiation. P atoms with atomic weights 28-34 except 31 are radioactive phosphorus isotopes.Uridine Diphosphate Xylose: The decarboxylation product of UDPglucuronic acid, which is used for formation of the xylosides of seryl hydroxyl groups in mucoprotein synthesis. Also forms plant xylans.Species Specificity: 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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Succinimides: A subclass of IMIDES with the general structure of pyrrolidinedione. They are prepared by the distillation of ammonium succinate. They are sweet-tasting compounds that are used as chemical intermediates and plant growth stimulants.HeptosesSpectrometry, Mass, Electrospray Ionization: A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.Cyanogen Bromide: 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.Methods: A series of steps taken in order to conduct research.Polyisoprenyl Phosphate Monosaccharides: These compounds function as activated monosaccharide carriers in the biosynthesis of glycoproteins and oligosaccharide phospholipids. Obtained from a nucleoside diphosphate sugar and a polyisoprenyl phosphate.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)Bacillus: A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.Acetylglucosamine: The N-acetyl derivative of glucosamine.Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization: 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.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.Solubility: The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Alkalies: Usually a hydroxide of lithium, sodium, potassium, rubidium or cesium, but also the carbonates of these metals, ammonia, and the amines. (Grant & Hackh's Chemical Dictionary, 5th ed)Phosphatidylinositols: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.ImidesPhysicochemical Phenomena: The physical phenomena describing the structure and properties of atoms and molecules, and their reaction and interaction processes.Mannans: Polysaccharides consisting of mannose units.Isodesmosine: 2-(4-Amino-4-carboxybutyl)-1-(5-amino-5-carboxypentyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinium. A rare amino acid found in elastin, formed by condensation of four molecules of lysine into a pyridinium ring.Glucuronates: Derivatives of GLUCURONIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the 6-carboxy glucose structure.Amino Acid Motifs: 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.Swine: 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).Chemistry, Physical: The study of CHEMICAL PHENOMENA and processes in terms of the underlying PHYSICAL PHENOMENA and processes.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Chromatography, Liquid: Chromatographic techniques in which the mobile phase is a liquid.Uridine Diphosphate Glucose: A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.Sulfates: Inorganic salts of sulfuric acid.Glycosphingolipids: Lipids containing at least one monosaccharide residue and either a sphingoid or a ceramide (CERAMIDES). They are subdivided into NEUTRAL GLYCOSPHINGOLIPIDS comprising monoglycosyl- and oligoglycosylsphingoids and monoglycosyl- and oligoglycosylceramides; and ACIDIC GLYCOSPHINGOLIPIDS which comprises sialosylglycosylsphingolipids (GANGLIOSIDES); SULFOGLYCOSPHINGOLIPIDS (formerly known as sulfatides), glycuronoglycosphingolipids, and phospho- and phosphonoglycosphingolipids. (From IUPAC's webpage)Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Chemistry Techniques, Analytical: Methodologies used for the isolation, identification, detection, and quantitation of chemical substances.Biochemistry: The study of the composition, chemical structures, and chemical reactions of living things.MethylglycosidesAmino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Uridine Diphosphate SugarsMaleic Anhydrides: Used in copolymerization reactions, in the Diels-Alder(diene)synthesis, in the preparation of resins, pharmaceuticals and agricultural chemicals. It is a powerful irritant and causes burns.Inosine: A purine nucleoside that has hypoxanthine linked by the N9 nitrogen to the C1 carbon of ribose. It is an intermediate in the degradation of purines and purine nucleosides to uric acid and in pathways of purine salvage. It also occurs in the anticodon of certain transfer RNA molecules. (Dorland, 28th ed)XyloseXylans: Polysaccharides consisting of xylose units.Streptomyces: A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Cellulose: A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.Hexuronic Acids: Term used to designate tetrahydroxy aldehydic acids obtained by oxidation of hexose sugars, i.e. glucuronic acid, galacturonic acid, etc. Historically, the name hexuronic acid was originally given to ascorbic acid.Pyridoxal Phosphate: 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).Cross-Linking Reagents: 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.Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Thermolysin: A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Anti-Bacterial Agents: Substances that reduce the growth or reproduction of BACTERIA.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Citraconic Anhydrides: Methylmaleic anhydrides.Flavonols: A group of 3-hydroxy-4-keto-FLAVONOIDS.Biochemical Phenomena: The chemical processes, enzymatic activities, and pathways of living things and related temporal, dimensional, qualitative, and quantitative concepts.Glycosylation: 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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Ribose: A pentose active in biological systems usually in its D-form.Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.Deoxy SugarsChemical Fractionation: Separation of a mixture in successive stages, each stage removing from the mixture some proportion of one of the substances, for example by differential solubility in water-solvent mixtures. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.HexosephosphatesFormates: Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.Spectrum Analysis: The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Sulfhydryl Compounds: Compounds containing the -SH radical.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Bacteria: One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.Protein Structure, Secondary: 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.Microwaves: That portion of the electromagnetic spectrum from the UHF (ultrahigh frequency) radio waves and extending into the INFRARED RAYS frequencies.Leucine: An essential branched-chain amino acid important for hemoglobin formation.
... zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been ... The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member ... postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a ... Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Ménard R (Nov 2003). "Essential roles of zinc ligation and enzyme ...
A process using an enzyme from Bacillus thermoproteolyticus to catalyze the condensation of the chemically altered amino acids ... then the protecting group is removed from aspartic nitrogen by acid hydrolysis. The drawback of this technique is that a ... In the chemical synthesis, the two carboxyl groups of aspartic acid are joined into an anhydride, and the amino group is ... Aspartame is a methyl ester of the dipeptide of the natural amino acids L-aspartic acid and L-phenylalanine. Under strongly ...
Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding ... Simple hydrolysis will split the polypeptide chain, where the displaced amino group becomes the new N-terminus. This is seen in ... The hydroxylation reaction is catalyzed by an enzyme that requires ascorbic acid (vitamin C), deficiencies in which lead to ... 20 natural amino acid notation Amino Acid 3-Letter[4]. 1-Letter[4]. ...
Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding ... The hydroxylation reaction is catalyzed by an enzyme that requires ascorbic acid (vitamin C), deficiencies in which lead to ... Hydrolysis of the intermediate produces either asparate or the β-amino acid, iso(Asp). For asparagine, either product results ... The positive charge on the N-terminal amino group may be eliminated by changing it to an acetyl group (N-terminal blocking). ...
Hydrolysis of the amino group of glutamine yielding glutamate and ammonium. Catalyzing enzyme: glutaminase (EC 3.5.1.2) 2. ... of acetyl-CoA infiltrated in the citric acid cycle is low and acetyl-CoA is available for de novo synthesis of fatty acids and ... FADH2 catalyzing enzyme: succinate dehydrogenase, EC 1.3.5.1 fumarate + H2O → malate catalyzing enzyme: fumarase, EC 4.2.1.2 ... CO2 catalyzing enzyme: α-ketoglutarate dehydrogenase complex succinyl-CoA + GDP + Pi → succinate + GTP catalyzing enzyme: ...
... ester groups. Enzymes, which are composed of chiral amino acids, catalyze chemical reactions with high stereoselectivity. ... For instance, the introduction of a chiral leaving group on both carboxylic acid groups of a meso diacid leads to selective ... Specifically, esterase enzymes catalyze the hydrolysis of esters to carboxylic acids. This transformation may be rendered ... but the substrate must present an ester group to this residue after binding to the enzyme active site for hydrolysis to take ...
... is an enzyme that catalyzes the hydrolysis of an amide: Thus, the two substrates of this enzyme are monocarboxylic acid amide ... This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, ... Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being ... AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate ...
... that catalyze the hydrolysis of starch into maltose. These enzymes are grouped into three classes based on their amino acid ... The exoenzymatic function allows it to break down the triacylglycerol into two free fatty acids and one molecule of ... Bacteria such as Clostridium do so by using the enzyme to dissolve collagen and hyaluronic acid, the protein and saccharides, ... Pepsin works best at the pH of gastric acid, 1.5 to 2.5, and is deactivated when the acid is neutralized to a pH of 7. Also one ...
The enzyme aspartokinase, which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids ... this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[9] Enzymes involved in a typical ... Amino acids that must be obtained from the diet are called essential amino acids. Nonessential amino acids are produced in the ... Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The ...
... and D are the amino acids histidine (H), lysine (K), aspartic acid (D), while x represents nonconservative amino acids. These ... Utilizing water as a nucleophile, this enzyme catalyzes the cleavage of the phosphodiester bond in structural phospholipids ... The products of this hydrolysis are the membrane-bound lipid phosphatidic acid (PA), and choline, which diffuses into the ... whose small head group promotes membrane curvature. It is thus thought to facilitate membrane-vesicle fusion and fission in a ...
This step often precedes hydrolysis, which is catalyzed by both Bronsted acids and Lewis acids. Enzymes, e.g. peptidases and ... An amide (/ˈæmaɪd/ or /ˈæmɪd/ or /ˈeɪmaɪd/), also known as an acid amide, is a compound with the functional group RnE(O)xNR′2 ( ... Amidogen Amino radical Amidicity Metal amides http://www.collinsdictionary.com/dictionary/english/amide "amide". The American ... While the conjugate acid of an amine has a pKa of about 9.5, the conjugate acid of an amide has a pKa around −0.5. Therefore, ...
"N-alkylated alpha-amino acid". The α-carboxylic acid group of amino acids is a weak acid, meaning that it releases a hydron ( ... this produces an α-amino nitrile as an intermediate. Hydrolysis of the nitrile in acid then yields a α-amino acid. Using ... This aminoacyl-tRNA is then a substrate for the ribosome, which catalyzes the attack of the amino group of the elongating ... D-amino acids are found in some proteins produced by enzyme posttranslational modifications after translation and translocation ...
... making the enzyme a homodimer. To catalyze the hydrolysis of urocanate in the catabolic pathway of L-histidine the enzyme ... The protein itself is composed of 676 amino acids which then fold, producing the final product which has 2 identical subunits, ... The NAD+ groups act as electrophiles, attaching to the top carbon of the urocanate which leads to sigmatropic rearrangement of ... 5-dihydro-4-oxo-5-imidazolepropanoate Inherited deficiency of urocanase leads to elevated levels of urocanic acid in the urine ...
A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its ... are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. ... Cysteine-dependent phosphatases (CDPs) catalyse the hydrolysis of a phosphoester bond via a phospho-cysteine intermediate. The ... and the P-O bond linking the phosphate group to the tyrosine is protonated, either by a suitably positioned acidic amino acid ...
Alpha-amino acids can be generated using the uncatalyzed reaction between alpha-ketoacids, amines, and phenylboronic acid. Heck ... Phenylboronic acid or benzeneboronic acid, abbreviated as PhB(OH)2 where Ph is the phenyl group C6H5-, is a boronic acid ... Sakai, M.; Hayashi, H.; Miyaura, N. (1998). "Rhodium-Catalyzed Addition of Organoboronic Acids to Aldehydes". Angew. Chem. Int ... Phenylsilanes and phenylstannanes transmetalate with BBr3, followed by hydrolysis form phenylboronic acid. Aryl halides or ...
Degradation of branched-chain ketogenic amino acids such as valine, leucine, and isoleucine occurs. These amino acids are ... Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production. ... Choline, in combination with acetyl-CoA, is catalyzed by the enzyme choline acetyltransferase to produce acetylcholine and ... Hydrolysis of the thioester bond is exergonic (−31.5 kJ/mol). CoA is acetylated to acetyl-CoA by the breakdown of carbohydrates ...
... (CH3COCOOH) is the simplest of the alpha-keto acids, with a carboxylic acid and a ketone functional group. ... to catalyze the reverse transformation of pyruvate to PEP. Compound C00074 at KEGG Pathway Database. Enzyme 2.7.1.40 at KEGG ... It can also be used to construct the amino acid alanine and can be converted into ethanol or lactic acid via fermentation. ... or by the hydrolysis of acetyl cyanide, formed by reaction of acetyl chloride with potassium cyanide: CH3COCl + KCN → CH3COCN ...
The removal of the D-glucose leaving group may be facilitated by Mg-dependent acid catalysis. The enzyme is liberated from the ... has a single polypeptide primary structure consisting of 1927 amino acids. It can be divided into five domains: (i) a 19-amino- ... Studies of E. coli lactase have proposed that hydrolysis is initiated when a glutamate nucleophile on the enzyme attacks from ... Lactase also catalyzes the conversion of phlorizin to phloretin and glucose. Preprolactase, the primary translation product, ...
... (abbreviated as Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group ... this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group. Enzymes involved in a typical ... "Protein and Amino Acids". Dietary Reference Intakes for Energy, Carbohydrates, Fiber, Fat, Fatty Acids, Cholesterol, Protein, ... and the serine and threonine dehydratase reactions are probably catalyzed by the same enzyme. Foods high in threonine include ...
... another class of enzymes, that catalyse the hydrolysis of terminal peptide bonds, liberating one free amino acid at a time). ... In acids, the carbonyl group becomes protonated, and this leads to a much easier nucleophilic attack. The products for both ... Strong acids also undergo hydrolysis. For example, dissolving sulfuric acid (H2SO4) in water is accompanied by hydrolysis to ... Acid-base-catalysed hydrolyses are very common; one example is the hydrolysis of amides or esters. Their hydrolysis occurs when ...
... and like all amino acids, exists in different ionic states depending on pH. Both the phosphonic acid and carboxylic acid ... and work-up with hydrochloric acid cleaves the hydroxymethyl group from the nitrogen atom whilst heating speeds the hydrolysis ... It does this by inhibiting the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), which catalyzes the reaction of ... an essential precursor for the amino acids mentioned above. These amino acids are used in protein synthesis and to produce ...
The conversion of amino acids into peptides is a major biochemical process that requires ATP. The hydroxyl group on carboxylic ... Enzymes that catalyze these reactions are known as carboxylases (EC 6.4.1) and decarboxylases (EC 4.1.1). Carboxylic acids are ... Carboxylic acids can also be obtained by the hydrolysis of nitriles, esters, or amides, in general with acid- or base-catalysis ... Carboxylic acids occur widely and include the amino acids (which make up proteins) and acetic acid (which is part of vinegar ...
The amide bonds can be attacked non-specifically by acid or base catalyzed hydrolysis. The polymer's peptide bonds can also be ... Degradation of the polymer occurs at the peptide bonds linking individual amino acids. ... For example, if the first residue is a phenylalanine then the enzyme chymotrypsin will cleave at site 1, and if the third ... This would done with all other reaction groups protected and with the C-terminus activated. The second modification required is ...
Metabolism: Protein metabolism, synthesis and catabolism enzymes. Essential amino acids are in Capitals ... "Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types". Biochem. J. 326 (2): 351-6. ... Kynureninase belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ... Hydrolysis of the acyl-enzyme then yields 3hAnt. The KYNU's reaction mechanism. ...
Main article: Amino acid activation. Aminoacyl-tRNA synthetase enzymes consume ATP in the attachment tRNA to amino acids, ... Knowles, J. R. (1980). "Enzyme-catalyzed phosphoryl transfer reactions". Annu. Rev. Biochem. 49: 877-919. doi:10.1146/annurev. ... ATP is involved signal transduction by serving as substrate for kinases, enzymes that transfer phosphate groups. Kinases are ... The hydrolysis of ATP into ADP and inorganic phosphate releases 30.5 kJ/mol of enthalpy, with a change in free energy of 3.4 kJ ...
... essential fatty acids, and essential amino acids.[4] The five major minerals in the human body are calcium, phosphorus, ... Ashmead, H. DeWayne (1993). The Roles of Amino Acid Chelates in Animal Nutrition. Westwood: Noyes Publications.. ... As a group, minerals are one of the four groups of essential nutrients, the others of which are vitamins, ... A cofactor in enzyme functions Grains, legumes, seeds, nuts, leafy vegetables, tea, coffee[25] manganese deficiency manganism ...
Any of a group of enzymes that catalyze the hydrolysis of single amino acids from the end of a polypeptide chain. ... An enzyme that catalyzes the hydrolysis of the terminal amino acid of a peptide chain (e.g., carboxypeptidase). Compare: ... An enzyme that catalyzes the hydrolysis of the terminal amino acid of a peptide chain; for example, carboxypeptidase. Compare: ... An enzyme that acts to split off AMINO ACIDS or sometimes dipeptides from the ends of a protein molecule.. exopeptidase. a type ...
Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the end that contains a ... enzyme secreted by the pancreas that acts only on the peptide linkage of a terminal amino acid containing a free carboxyl group ... an exopeptidase that catalyses the hydrolysis of amino acids in polypeptide chains from the C-terminal.. carboxypeptidase ( ... Any enzyme (EC 3.4.16 to EC 3.4.18) which hydrolyses (cleaves) the peptide bond of the COOH terminal amino acid from a peptide ...
... zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been ... The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member ... postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a ... Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Ménard R (Nov 2003). "Essential roles of zinc ligation and enzyme ...
Find out information about enzyme. biological catalyst catalyst, substance that can cause a change in the rate of a chemical ... reaction without itself being consumed in the reaction; the... Explanation of enzyme ... An example of a stereospecific enzyme is l -amino acid oxidase. This enzyme catalyzes the oxidation of a variety of amino acids ... as well as decarboxylation and a number of other transformations of amino acids. A prosthetic group of enzymes that catalyze ...
... zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been ... The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member ... postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a ...
... such as the exposure of hydrophobic amino acids, which led to a less efficient, albeit still functional, enzyme-substrate ... Lst-catalyzed hydrolysis of WTA-removed peptidoglycan was nearly 2.6-fold faster than on peptidoglycan containing WTA. This ... S1). However, when the hydroxyl group of glycolic acid was substituted with an amino group (glycine with pKa = 9.8), Lst ... amino acids 1 to 137) and a C-terminal substrate-binding domain (amino acids 154 to 246) joined by a flexible linker (amino ...
A process using an enzyme from Bacillus thermoproteolyticus to catalyze the condensation of the chemically altered amino acids ... then the protecting group is removed from aspartic nitrogen by acid hydrolysis. The drawback of this technique is that a ... In the chemical synthesis, the two carboxyl groups of aspartic acid are joined into an anhydride, and the amino group is ... Aspartame is a methyl ester of the dipeptide of the natural amino acids L-aspartic acid and L-phenylalanine. Under strongly ...
ACY1, SQSTM1 and GPC3 were differentially expressed in each group. For the differential diagnosis of WDHCC from HGDN, the ... zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl groups [31]. SQSTM1 is an ... Gade W, Brown JL: Purification, characterization and possible function of alpha-N-acylamino acid hydrolase from bovine liver. ... Among these, 142 specimens were included in the diagnostic group and 500 in the prognostic group. The baseline characteristics ...
... enzymes catalyze the hydrolysis of the sn-2 ester bond of glycerophospholipids to release fatty acids and lysophospholipids. In ... The amino acid residues in the active site are labeled. As seen in the acetylcholine receptor, the regions of the phospholipase ... PLA2 group X regulates cysteinyl leukotriene synthesis[4]. *PLA2 group XV is located in the endocytic system and may be ... Phospholipase A2 (PLA2) is an enzyme which releases fatty acids from glycerol. It is found in mammals and in snake venoms[1]. ...
Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding ... Simple hydrolysis will split the polypeptide chain, where the displaced amino group becomes the new N-terminus. This is seen in ... The hydroxylation reaction is catalyzed by an enzyme that requires ascorbic acid (vitamin C), deficiencies in which lead to ... 20 natural amino acid notation Amino Acid 3-Letter[4]. 1-Letter[4]. ...
This amino acid is often present in active sites of enzymes wherein the imidazole group acts as a buffer (proton acceptor or ... which is neutral at physiological pH and can be changed to carboxylic acid by hydrolysis to form aspartate amino acid. The ... The enzymatically-catalyzed reaction forms an amide entity: [R1-NH2 + R2-COOH ==, R1-NH-C(=O)-R2 + H2O]. The amide bond has ... Amino Acids[edit]. Amino acids are molecules which contain both a carboxylic acid and an amine group. In amino acid, the ...
L-amino acid oxidase and D-amino acid oxidase, catalyze the oxidation of the L- and D-amino acids, utilizing FAD as their redox ... An N5, N10-methylene-THF synthesizing enzyme (T protein), which accepts a mthylene group from the aminomethyltransferase. ... The urea cycles fifth and final reaction is the arginase-catalyzed hydrolysis of arginine to yield urea and regenerate ... the transfer of their amino group to an α-keto acid to yield the α-keto acid of the original amino acid and a new amino acid, ...
Enzymes that hydrolyze pyrophosphate are called inorganic pyrophosphatases (PPases). Two major types of inorganic ... Both enzymes are heterologous which have difference in structure and amino acid sequences, but they have similar patterns in ... Soluble pyrophosphatases are ubiquitous enzymes that play a key role in phosphorus metabolism by catalyzing the hydrolysis of ... where it is a part of phosphate groups such as pyrophosphate ( PO 3 2 − -O-PO 3 2 − ) . Pyrophosphate is a by-product of ...
The amino acid sequence of atrazine chlorohydrolase is shown to be 98% identical with that of melamine deaminase, an enzyme ... The amino acids serving as metal ligands are maintained across the superfamily. The majority of reactions catalyzed by the ... superfamily involve the hydrolytic removal of amino groups from purine and pyrimidine rings, or amide bond hydrolysis reactions ... 5) Common Ancestry of Escherichia coli Pyruvate Oxidase and the Acetohydroxy Acid Synthase of the Branched-Chain Amino Acid ...
Proteases (peptidases or proteolytic enzymes) constitute a large group of enzymes that catalyse the hydrolysis of peptide bonds ... Extracellular proteases catalyse the hydrolysis of proteins into smaller peptides and amino acids for subsequent absorption ... based on the nature of the amino acid residues at the active site of the enzymes. Endopeptidases are characterized by their ... This group represents one of the largest groups of industrial enzymes and accounts for approximately 60% of the total enzyme ...
Welcome to buy the bulk amino-acid-l-serine-56-45-1 from our factory. ... brings you a large selection of quality amino-acid-l-serine-56-45-1 with reasonable price. All products are extracted from ... Amino acids l-serine plays an important role in the catalytic function of many enzymes. Amino acids l-serine has been shown to ... Reductive amination of this ketone followed by hydrolysis gives serine. Serine hydroxymethyltransferase catalyzes the ...
The enzyme aspartokinase, which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids ... this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[9] Enzymes involved in a typical ... Amino acids that must be obtained from the diet are called essential amino acids. Nonessential amino acids are produced in the ... Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The ...
casein A group of proteins found in milk.. casein hydrolysate Mixture of amino acids and peptides produced by enzymatic or acid ... carboxypeptidases Two enzymes (A and B) found in pancreatic juice. Their role is to remove the C-terminal amino-acid from a ... catalytic antibody (= abzyme) An antibody selected for its ability to catalyse a chemical reaction by binding to and ... hydrolysis of casein. cf organic complex; undefined.. CAT box See CAAT box. ...
The d-amino acid succinyl-N-transferase accepted 16 amino acids, the NSAR was able to racemize 17 succinylamino acids, and the ... the succinyl group is removed during hydrolysis by l-succinylase to leave the lPhe product (17) in a net irreversible fashion, ... The novel C C bond-forming oxidizing reaction catalyzed by BBE and reactions catalyzed by the presumed BBE enzyme homologues ... An example of an enzyme that has been added to the enzyme database is the berberine bridge enzyme (BBE) [EC 1.21.3.3][2a,b] ...
... and the transfer of its γ-glutamyl group to acceptor substrates like water (hydrolysis reaction) or other amino acids or ... GGT is also a key enzyme for other metabolic processes like arachidonic acid metabolism, cyanoamino acid metabolism, gamma- ... It catalyzes the cleavage and transfer of γ-glutamyl moiety of glutathione to either water (hydrolysis) or substrates like ... The threonine and the asparagine residues form hydrogen bonds with amino group of the γ-glutamyl substrate [17, 29-31]. These ...
Peptidases are proteolytic enzymes responsible for fundamental cellular activities in all organisms. Apparently about 2-5% of ... In the serine and cysteine types the catalytic nucleophile can be the reactive group of the amino acid side chain, a hydroxyl ... All peptidases catalyze the same reaction, namely the hydrolysis of a peptide bond, but they are selective for the position of ... Rawlings ND, Morton FR, Barrett AJ: MEROPS : the peptidase database. Nucleic Acids Res 2006, 34: D270-D272. 10.1093/nar/gkj089 ...
... is a recombinant human α-galactosidase A enzyme with the same amino acid sequence as the native enzyme. Purified agalsidase ... α-galactosidase A catalyzes the hydrolysis of globotriaosylceramide (GL-3) and other α-galactyl-terminated neutral ... The mature protein is comprised of two subunits of 398 amino acids (approximately 51 kD), each of which contains three N-linked ... The reduction in plasma GL-3 levels in the Fabrazyme (agalsidase beta) group compared to the placebo group was significant at ...
Zenpep consists of porcine-derived pancreatic enzymes that catalyze the hydrolysis of fats to monoglycerol, glycerol, and fatty ... acids; protein into peptides and amino acids; and starch into dextrins and short chain sugars, thus exerting actions similar to ... Porcine-derived enzyme products may increase blood uric acid levels; caution should be used when prescribed to patients with ... The CFA was found to be statistically higher in the Zenpep group than in the placebo group. The other trial was an open-label, ...
PP2As are multimeric enzymes capable of catalyzing the hydrolysis of phosphate groups from phosphoseryl, phosphothreonyl, and ... amino acids 1 to 164) (N); 4, MBP-C-terminal catalytic domain of Sit4p (amino acids 161 to 302) (C). (B) Yeast PTPA proteins ... NCS1 and YPL152w(which we designate NOH1; also called RRD2[39]) show a great deal of sequence similarity (179 of 393 amino acid ... a C-terminal truncation encoding only the first 164 amino acids, and an N-terminal deletion of the first 161 amino acids ...
In this review, we provide a comprehensive summary of CDP biosynthetic pathways and modifying enzymes. We also discuss the ... which is further modified by tailoring enzymes often associated with CDP biosynthetic gene clusters. ... CDP synthases (CDPSs) and non-ribosomal peptide synthetases (NRPSs) catalyze the biosynthesis of the CDP core structure, ... or connectivity of the constitutive amino acids. Second, tailoring enzymes can be introduced to catalyze specific chemical ...
  • These enzymes can be utilized to transaminate a prochiral ketone with an amino donor (e.g. isopropylamine), to achieve a chiral amine and a carbonyl product (e.g. acetone). (uni-greifswald.de)
  • Sodium ions react very little with hydroxyl ions whereas acetate ions combine with hydrogen ions to produce neutral acetic acid, and the net result is a relative excess of hydroxyl ions, causing a basic solution. (chemistryexplained.com)
  • Their hydrolysis occurs when the nucleophile (a nucleus-seeking agent, e.g., water or hydroxyl ion) attacks the carbon of the carbonyl group of the ester or amide. (chemistryexplained.com)
  • And, this is all caused by messing with a single hydroxyl (OH) group, which is a tiny, but critical portion (the "business end") of acetylcholinesterase. (acsh.org)
  • Note that the acetylcholine (orange oval) is sitting in just the right position so that the hydroxyl group (yellow circle) can reach it. (acsh.org)
  • If the hydroxyl group of acetylcholinesterase is tied up and not available to do its normal job, then the enzyme cannot function, and the synapse will remain full of acetylcholine. (acsh.org)
  • What ties the hydroxyl group up? (acsh.org)
  • The phosphorous atom in Naled reacts with, and forms a chemical bond with, the hydroxyl group of the acetylcholinesterase. (acsh.org)
  • An alternative to antibiotics is the naturally present bacteriolytic enzymes, including endolysins, autolysins, virion-associated lysins, and bacteriolysins, hydrolases that selectively cleave certain structures of bacterial cell wall peptidoglycan ( 1 , 2 ). (asm.org)
  • Insect chitinases belong to the family 18 glycosyl hydrolases, based on the conservation of amino acid sequences and many conserved motifs [ 6 ]. (mdpi.com)
  • In metallopeptidases one or two metal ions hold the water molecule in place and charged amino acid side chains are ligands for the metal ions. (biomedcentral.com)
  • Acid: An acid is a proton donor, i.e., any chemical species (molecule or ion) that is able to '''lose or 'donate'''' a hydrogen ion (proton) in solution. (scribd.com)
  • Conjugate base: is the ion or molecule remaining after the acid has lost a proton and is also referred to as the salt of the acid. (scribd.com)
  • The hydrolysis of NAD itself can be described as a transfer of ADP-ribose onto a water molecule. (iucr.org)
  • In addition, hydrolysis is said to occur when a salt reacts with water to produce new ions or precipitates. (newworldencyclopedia.org)
  • Among them, 2,5-xylidine remarkably stimulated enzyme production while Cu 2+ ions within the tested concentration range (0-0.25 mM) had an opposite effect. (chemweb.com)
  • Because of the high activity of arginase enzyme which catalyzes the hydrolysis of L-arginine into ornithine and urea, the bioavailability of nitrogen oxide decreases. (hindawi.com)
  • The inhibitors of arginase suppress the activity of the given enzyme, raising and production of nitrogen oxide, preventing the development of endothelial dysfunction. (hindawi.com)
  • The impact of five crucial variables on enzyme production, including glucose and nitrogen concentrations and three distinct putative inducers, namely, copper sulphate, 2,5-xylidine and olive-mill wastewater was thoroughly investigated. (chemweb.com)