A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
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 subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
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.
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
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.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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)
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
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.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
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 process of cleaving a chemical compound by the addition of a molecule of water.
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.
Proteins prepared by recombinant DNA technology.
Peptides composed of between two and twelve amino acids.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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)
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.
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
An ASPARTIC ACID residue in polypeptide chains that is linked at the beta-carboxyl group instead of at the normal, alpha-carboxyl group, polypeptide linkage. It is a result of the spontaneous decomposition of aspartic acid or ASPARAGINE residues.
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
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).
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
An essential amino acid that is required for the production of HISTAMINE.
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 biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.
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.
A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC (Formerly EC
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.
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.
Peptides composed of two amino acid units.
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.
The sum of the weight of all the atoms in a molecule.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
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 region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
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.
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
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS.
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.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Established cell cultures that have the potential to propagate indefinitely.
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.
An enzyme that activates aspartic acid with its specific transfer RNA. EC
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992)
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.
Proteins found in any species of bacterium.
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.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
Physiologically inactive substances that can be converted to active enzymes.
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.
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.
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.
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.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
The 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 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.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
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.
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.
An eleven-amino acid neurotransmitter that appears in both the central and peripheral nervous systems. It is involved in transmission of PAIN, causes rapid contractions of the gastrointestinal smooth muscle, and modulates inflammatory and immune responses.
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.
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.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
One of the endogenous pentapeptides with morphine-like activity. It differs from MET-ENKEPHALIN in the LEUCINE at position 5. Its first four amino acid sequence is identical to the tetrapeptide sequence at the N-terminal of BETA-ENDORPHIN.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
A nonapeptide messenger that is enzymatically produced from KALLIDIN in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from MAST CELLS during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter.
A condition of an abnormally low level of PHOSPHATES in the blood.
A serotype of botulinum toxins that has specificity for cleavage of SYNAPTOSOMAL-ASSOCIATED PROTEIN 25.
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Aryl CYCLOPENTANES that are a reduced (protonated) form of INDENES.
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 genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.
A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.
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)
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.
An essential amino acid that is physiologically active in the L-form.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Disciplines that apply sciences to law. Forensic sciences include a wide range of disciplines, such as FORENSIC TOXICOLOGY; FORENSIC ANTHROPOLOGY; FORENSIC MEDICINE; FORENSIC DENTISTRY; and others.
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).
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.
Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.
Common name for Ricinus communis, a species in the family EUPHORBIACEAE. It is the source of CASTOR OIL.
A type II keratin found expressed in the upper spinous layer of epidermal KERATINOCYTES. Mutations in genes that encode keratin-2A have been associated with ICHTHYOSIS BULLOSA OF SIEMENS.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
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).
An essential amino acid. It is often added to animal feed.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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 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)
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
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.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC and EC
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC
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 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)
Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.
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.
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 family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
A major class of water-soluble seed storage proteins. Many proteins from this class are major PLANT ALLERGENS.
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).)
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.
Techniques used to determine the age of materials, based on the content and half-lives of the RADIOACTIVE ISOTOPES they contain.
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.
An essential branched-chain amino acid important for hemoglobin formation.
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.
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).
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.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC
A hereditary disorder characterized by HYPOPHOSPHATEMIA; RICKETS; OSTEOMALACIA; renal defects in phosphate reabsorption and vitamin D metabolism; and growth retardation. Autosomal and X-linked dominant and recessive variants have been reported.
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.
A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.
The predominant milk-clotting enzyme from the true stomach or abomasum of the suckling calf. It is secreted as an inactive precursor called prorennin and converted in the acid environment of the stomach to the active enzyme. EC
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.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC
A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Steroid derivatives formed by oxidation of a methyl group on the side chain or a methylene group in the ring skeleton to form a ketone.
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.
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.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pepsinogen I or pepsinogen) and PEPSINOGEN C (formerly pepsinogen II or progastricsin). Pepsinogen B is the name of a pepsinogen from pigs.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
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.
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 generic term used to describe a group of polypeptides with related chemical structures and pharmacological properties that are widely distributed in nature. These peptides are AUTACOIDS that act locally to produce pain, vasodilatation, increased vascular permeability, and the synthesis of prostaglandins. Thus, they comprise a subset of the large number of mediators that contribute to the inflammatory response. (From Goodman and Gilman's The Pharmacologic Basis of Therapeutics, 8th ed, p588)
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.
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.
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
Amino derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the amino caproic acid structure.
One or more types of plant seed proteins providing the large amounts of AMINO ACIDS utilized in GERMINATION and SEEDLING growth. As seeds are the major food source from AGRICULTURAL CROPS, seed storage proteins are a major source of DIETARY PROTEINS.
Organic compounds that contain the (-NH2OH) radical.
The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.
A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.
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.
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

Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase. (1/2015)

We have developed a system for expression and purification of wild-type human T-cell leukemia virus type 1 (HTLV-1) proteinase to attain sufficient quantities for structural, kinetic, and biophysical investigations. However, similar to the human immunodeficiency virus type 1 (HIV-1) proteinase, HTLV-1 proteinase also undergoes autoproteolysis rapidly upon renaturation to produce two products. The site of this autoproteolytic cleavage was mapped, and a resistant HTLV-1 proteinase construct (L40I) as well as another construct, wherein the two cysteine residues were exchanged to alanines, were expressed and purified. Oligopeptide substrates representing the naturally occurring cleavage sites in HTLV-1 were good substrates of the HTLV-1 proteinase. The kinetic parameters kcat and Km were nearly identical for all the three enzymes. Although three of four peptides representing HTLV-1 proteinase cleavage sites were fairly good substrates of HIV-1 proteinase, only two of nine peptides representing HIV-1 proteinase cleavage sites were hydrolyzed by the HTLV-1 proteinase, suggesting substantial differences in the specificity of the two enzymes. The large difference in the specificity of the two enzymes was also demonstrated by inhibition studies. Of the several inhibitors of HIV-1 or other retroviral proteinases that were tested on HTLV-1 proteinase, only two inhibit the enzyme with a Ki lower than 100 nM.  (+info)

Fus3p and Kss1p control G1 arrest in Saccharomyces cerevisiae through a balance of distinct arrest and proliferative functions that operate in parallel with Far1p. (2/2015)

In Saccharomyces cerevisiae, mating pheromones activate two MAP kinases (MAPKs), Fus3p and Kss1p, to induce G1 arrest prior to mating. Fus3p is known to promote G1 arrest by activating Far1p, which inhibits three Clnp/Cdc28p kinases. To analyze the contribution of Fus3p and Kss1p to G1 arrest that is independent of Far1p, we constructed far1 CLN strains that undergo G1 arrest from increased activation of the mating MAP kinase pathway. We find that Fus3p and Kss1p both control G1 arrest through multiple functions that operate in parallel with Far1p. Fus3p and Kss1p together promote G1 arrest by repressing transcription of G1/S cyclin genes (CLN1, CLN2, CLB5) by a mechanism that blocks their activation by Cln3p/Cdc28p kinase. In addition, Fus3p and Kss1p counteract G1 arrest through overlapping and distinct functions. Fus3p and Kss1p together increase the expression of CLN3 and PCL2 genes that promote budding, and Kss1p inhibits the MAP kinase cascade. Strikingly, Fus3p promotes proliferation by a novel function that is not linked to reduced Ste12p activity or increased levels of Cln2p/Cdc28p kinase. Genetic analysis suggests that Fus3p promotes proliferation through activation of Mcm1p transcription factor that upregulates numerous genes in G1 phase. Thus, Fus3p and Kss1p control G1 arrest through a balance of arrest functions that inhibit the Cdc28p machinery and proliferative functions that bypass this inhibition.  (+info)

Pregnancy detection and the effects of age, body weight, and previous reproductive performance on pregnancy status and weaning rates of farmed fallow deer (Dama dama). (3/2015)

Fallow does (n = 502) of different ages (mature, 2-yr-old, and yearling) were maintained with bucks for a 60-d breeding season to determine whether previous reproductive performance and changes in BW affect doe pregnancy rates and to compare the effectiveness of ultrasonography and serum pregnancy-specific protein B (PSPB) for the detection of pregnancy in fallow does. Ultrasonography was performed, blood samples collected, and BW recorded at buck removal (d 0) and at 30 and 90 d after buck removal. Lactational status (lactating = WET; nonlactating = DRY) were determined from farm records taken at weaning prior to each breeding season (autumn 1990 through autumn 1994). Ultrasonography and PSPB for determining pregnancy were in agreement 93% of the time. Overall pregnancy rates did not differ (P>.10) relative to age of the doe; the combined pregnancy rate was 92%. We also determined that 82.9% of does conceived early in the breeding season and that the incidence of embryonal-fetal mortality during the first 90 d after buck removal was 2.8%. In general, mature and 2-yr-old DRY does were heavier and had lower pregnancy rates than WET does. The overall weaning rate for all does was 77.9%. Loss in the number of fawns from pregnancy detection to weaning was equivalent to 14.8% for mature does, 24.7% for 2 yr old does, and 42.5% for yearling does. These data indicate that even though pregnancy rates were relatively high, further study is needed to determine the causes associated with subsequent fawn losses, particularly among yearling does. As a production tool, lactational WET/ DRY status testing was found to be an acceptable means for determining the reproductive potential of individual does within the herd. In addition, serum PSPB may be used in place of ultrasonography for pregnancy diagnosis in fallow deer as early as d 30 after buck removal.  (+info)

Endothelin-1 and its mRNA in the wall layers of human arteries ex vivo. (4/2015)

BACKGROUND: The participation of endothelin-1 (ET-1) in the control of vascular tone in humans has been questioned, on the basis of the finding of subthreshold immunoreactive (ir) ET-1 plasma levels. However, because most ET-1 is secreted abluminally, it might attain a higher concentration in the tunica media than in plasma. Furthermore, evidence indicates that vascular smooth muscle cells (VSMCs) can synthesize ET-1 on stimulation in vitro. We therefore looked for irET-1 in the different layers of the wall of human arteries, including renal, gastric, and internal thoracic artery wall, obtained ex vivo from consenting patients with coronary artery disease and/or high blood pressure undergoing surgery, as well as from young organ donors. METHODS AND RESULTS: We performed immunohistochemistry with specific anti-ET-1 and anti-vWF antibodies followed by detection with an avidin-biotin complex ultrasensitive kit. The presence of preproET-1 and human endothelin-converting enzyme-1 (hECE-1) mRNA was also investigated by reverse transcription-polymerase chain reaction in homogenates of vessel wall, including preparations deprived of both endothelium and adventitia, and in isolated VSMCs. We detected irET-1 in the endothelium of all arteries and in the tunica media of internal thoracic artery from most patients with coronary artery disease. PreproET-1 and hECE-1 mRNA was also detected in VSMCs isolated from these vessels. irET-1 and irvWF staining in endothelium and tunica media was measured by use of microscope-coupled computer-assisted technology. Significant correlations between the amount of irET-1 in the tunica media and mean blood pressure (P<0.05), total serum cholesterol (P<0.05), and number of atherosclerotic sites (P<0.001) were found. Thus, in organ donors, irET-1 was detectable almost exclusively in endothelial cells, whereas in patients with coronary artery disease and/or arterial hypertension, sizable amounts of irET-1 were detectable in the tunica media of different types of arteries. In addition, VSMCs isolated from these vessels coexpressed the preproET-1 and hECE-1 genes. CONCLUSIONS: Collectively, these findings are consistent with the contention that endothelial damage occurs in most patients with atherosclerosis and/or hypertension and that ET-1 is synthesized in VSMCs of these patients.  (+info)

Intranephron distribution and regulation of endothelin-converting enzyme-1 in cyclosporin A-induced acute renal failure in rats. (5/2015)

Endothelin-1 (ET-1) is thought to play a significant role in acute renal failure induced by cyclosporin A (CsA). The cDNA sequence encoding endothelin-converting enzyme-1 (ECE-1), which produces the active form of ET-1 from big ET-1, was recently reported. To elicit the role of ECE-1 in the glomerular and tubular dysfunction induced by CsA, the effects of CsA on mRNA and protein expression of ECE-1 in rat kidney and on mRNA expression of prepro-ET-1 and ET A- and B-type receptors in glomeruli were studied. ECE-1 mRNA was detected in glomeruli and in whole nephron segments. ECE-1 mRNA expression was downregulated in all nephron segments at 24 h after CsA injection. Protein levels were also downregulated in glomeruli and in the outer and inner medulla. CsA rapidly increased prepro-ET-1 mRNA expression in glomeruli at 30 to 60 min after injection; this rapid increase was followed by an increase in plasma ET-1 levels. These increases were followed by decreased expression of ECE-1, ET A-type receptor, and ET B-type receptor mRNA at 6 h after injection, and serum creatinine levels were increased at 24 h after CsA injection. It is suggested that downregulation of glomerular and tubular ECE-1 expression may be caused by increased ET-1 synthesis in CsA-induced acute renal failure.  (+info)

Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases? (6/2015)

BACKGROUND: The aspartic proteinase renin catalyses the first and rate-limiting step in the conversion of angiotensinogen to the hormone angiotensin II, and therefore plays an important physiological role in the regulation of blood pressure. Numerous potent peptidomimetic inhibitors of this important drug target have been developed, but none of these compounds have progressed past clinical phase II trials. Limited oral bioavailability or excessive production costs have prevented these inhibitors from becoming new antihypertensive drugs. We were interested in developing new nonpeptidomimetic renin inhibitors. RESULTS: High-throughput screening of the Roche compound library identified a simple 3, 4-disubstituted piperidine lead compound. We determined the crystal structures of recombinant human renin complexed with two representatives of this new class. Binding of these substituted piperidine derivatives is accompanied by major induced-fit adaptations around the enzyme's active site. CONCLUSIONS: The efficient optimisation of the piperidine inhibitors was facilitated by structural analysis of the renin active site in two renin-inhibitor complexes (some of the piperidine derivatives have picomolar affinities for renin). These structural changes provide the basis for a novel paradigm for inhibition of monomeric aspartic proteinases.  (+info)

Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. (7/2015)

Proteolytic processing of the amyloid precursor protein by beta-secretase yields A4CT (C99), which is cleaved further by the as yet unknown gamma-secretase, yielding the beta-amyloid (Abeta) peptide with 40 (Abeta40) or 42 residues (Abeta42). Because the position of gamma-secretase cleavage is crucial for the pathogenesis of Alzheimer's disease, we individually replaced all membrane-domain residues of A4CT outside the Abeta domain with phenylalanine, stably transfected the constructs in COS7 cells, and determined the effect of these mutations on the cleavage specificity of gamma-secretase (Abeta42/Abeta40 ratio). Compared with wild-type A4CT, mutations at Val-44, Ile-47, and Val-50 led to decreased Abeta42/Abeta40 ratios, whereas mutations at Thr-43, Ile-45, Val-46, Leu-49, and Met-51 led to increased Abeta42/Abeta40 ratios. A massive effect was observed for I45F (34-fold increase) making this construct important for the generation of animal models for Alzheimer's disease. Unlike the other mutations, A4CT-V44F was processed mainly to Abeta38, as determined by mass spectrometry. Our data provide a detailed model for the active site of gamma-secretase: gamma-secretase interacts with A4CT by binding to one side of the alpha-helical transmembrane domain of A4CT. Mutations in the transmembrane domain of A4CT interfere with the interaction between gamma-secretase and A4CT and, thus, alter the cleavage specificity of gamma-secretase.  (+info)

In vivo expression and localization of Candida albicans secreted aspartyl proteinases during oral candidiasis in HIV-infected patients. (8/2015)

Isoforms of aspartyl proteinase (Sap), which are encoded by at least nine related SAP genes, have been implicated to be a major virulence factor of the opportunistic yeast Candida albicans in experimental infections. Although it is generally assumed that proteinases are important for infections, detailed information on the pathogenetic role of Saps is still lacking. The same applies to the question whether the genes and corresponding isoforms of the enzyme are expressed during oral infection. For in vivo investigations, parts of the lesional oral epithelium were collected from three HIV-infected patients with oropharyngeal candidiasis. Immunoelectron microscopy was performed (pre- and post-embedding gold labeling with silver enhancement) using an anti-Sap murine monoclonal antibody directed against the gene products Sap1-3. It was possible to demonstrate expression of Sap antigens in each of the three samples of human oral candidiasis. This suggests that at least one of the genes SAP1-3 was expressed at the time of sample collection. Furthermore, a possible role of the enzymes during the interaction of yeast cells and mucosal cells is suggested: the majority of Sap antigens is secreted by those C. albicans cells that adhere directly to the epithelial surface. Sap immunoreactivity can be detected in particular at the site of close contact between C. albicans and epithelial cells, suggesting a pathogenetic role of the Saps in host-fungal interaction. Thus, inhibition of the enzyme might prove to be an important alternative in the prevention and treatment of candidiasis.  (+info)

Causes of Hypophosphatemia

There are several possible causes of hypophosphatemia, including:

1. Malnutrition or a poor diet that is deficient in phosphorus.
2. Gastrointestinal disorders such as celiac disease, inflammatory bowel disease, or gastrointestinal surgery.
3. Kidney problems such as chronic kidney disease, renal tubular acidosis, or distal renal tubular phosphate loss.
4. Hormonal imbalances such as hypoparathyroidism (underactive parathyroid glands) or hyperparathyroidism (overactive parathyroid glands).
5. Medications such as diuretics, antacids, and certain antibiotics.
6. Chronic alcoholism.
7. Genetic disorders such as X-linked hypophosphatemic rickets or familial hypophosphatemic rickets.

Symptoms of Hypophosphatemia

The symptoms of hypophosphatemia can vary depending on the severity and duration of the condition, but may include:

1. Weakness, fatigue, or muscle cramps.
2. Bone pain or joint stiffness.
3. Difficulty healing from injuries or infections.
4. Numbness or tingling sensations in the extremities.
5. Seizures or other neurological symptoms.
6. Respiratory problems such as shortness of breath or difficulty breathing.
7. Heart arrhythmias or cardiac failure.

Diagnosis and Treatment of Hypophosphatemia

Hypophosphatemia can be diagnosed through blood tests that measure the levels of phosphate in the blood. Treatment for hypophosphatemia typically involves correcting any underlying causes, such as stopping medications that may be causing the condition or treating underlying medical conditions.

In some cases, treatment may involve supplements to increase phosphate levels in the blood. Vitamin D and calcium supplements may also be prescribed to help maintain bone health. In severe cases of hypophosphatemia, hospitalization may be necessary to manage symptoms and prevent complications.

Prognosis and Complications of Hypophosphatemia

The prognosis for hypophosphatemia is generally good if the underlying cause is identified and treated promptly. However, untreated hypophosphatemia can lead to a number of complications, including:

1. Osteomalacia or osteoporosis.
2. Rickets in children.
3. Weakened immune system.
4. Increased risk of infections.
5. Nerve damage or neuropathy.
6. Cardiovascular problems such as heart arrhythmias or cardiac failure.
7. Respiratory failure.
8. Kidney damage or kidney failure.

It is important to seek medical attention if symptoms persist or worsen over time, as hypophosphatemia can lead to serious complications if left untreated.


Hypophosphatemia is a condition characterized by low levels of phosphate in the blood. It can be caused by a variety of factors and may present with symptoms such as weakness, bone pain, and respiratory problems. Treatment typically involves correcting any underlying causes and supplements to increase phosphate levels in the blood.

Early detection and treatment are important to prevent complications of hypophosphatemia, which can include osteomalacia or osteoporosis, nerve damage, cardiovascular problems, respiratory failure, and kidney damage. If you suspect you may have hypophosphatemia, it is important to seek medical attention as soon as possible to receive proper diagnosis and treatment.

The symptoms of familial hypophosphatemic rickets typically appear during infancy or early childhood and may include:

* Bowed legs
* Delayed closure of the fontanelles (soft spots on the skull)
* Difficulty walking or standing
* Growth retardation
* Increased risk of fractures
* Thickening of the bones (hyperostosis)
* Tooth decay and gum disease (dental caries and periodontal disease)

If left untreated, familial hypophosphatemic rickets can lead to severe complications such as:

* Permanent skeletal deformities
* Increased risk of bone fractures
* Dental problems
* Growth retardation
* Intellectual disability
* Death in rare cases

The diagnosis of familial hypophosphatemic rickets is based on a combination of clinical findings, laboratory tests, and genetic analysis. Laboratory tests may include measurements of serum phosphate levels, urinary phosphate excretion, and assessment of bone density using imaging techniques such as X-rays or computed tomography (CT) scans. Genetic testing can identify mutations in the PHEX gene that confirm the diagnosis.

Treatment for familial hypophosphatemic rickets typically involves a combination of dietary modifications and medication. Dietary modifications may include increasing phosphate intake through supplements or high-phosphate foods, while medications such as vitamin D analogues and bisphosphonates can help to improve bone density and reduce the risk of fractures. In severe cases, surgery may be necessary to correct skeletal deformities.

In conclusion, familial hypophosphatemic rickets is a rare genetic disorder that affects the development of bones and teeth, leading to a range of symptoms including bowed legs, thickened skin, and dental problems. The diagnosis is based on a combination of clinical findings, laboratory tests, and genetic analysis, while treatment involves a combination of dietary modifications and medication. With appropriate management, individuals with familial hypophosphatemic rickets can lead active and productive lives, although some may experience ongoing health issues throughout their lifetime.

"Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid ... Nodavirus endopeptidase (EC, Black Beetle virus endopeptidase, Flock House virus endopeptidase) is an enzyme. This ... Nodavirus+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.23). ... Johnson JE, Schneemann A (1998). "Nodavirus endopeptidase". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of ...
The main amino acids involved are serine, histidine, and aspartic acid. They all play a role in cleaving the peptide bond. ... Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that bond. Three common ... These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human ... Essential amino acids must be consumed and are made in other organisms. The amino acids are joined by peptide bonds making a ...
Proteases of this group hydrolyzes peptide bonds after the negatively charged glutamic acid or aspartic acid, with a higher ... subtilis glutamyl endopeptidase GluBS Enterococcus E. faecalis glutamyl endopeptidase SprE Glutamyl endopeptidase is in at ... S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ...
... (EC, Rhizopus aspartic proteinase, neurase, Rhizopus acid protease, Rhizopus acid proteinase) is an ... A similar endopeptidase is found in R. niveus [2]. In peptidase family A1 (pepsin A family). Tsuru D, Hattori A, Tsuji H, ... Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419-1426. doi:10.1080/00021369.1969. ... Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (October 1987). "Binding of a reduced peptide inhibitor to the aspartic ...
1998). "Autocatalytic activation of human legumain at aspartic acid residues". FEBS Lett. 438 (1-2): 114-8. doi:10.1016/S0014- ... 1999). "An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation". Nature. 396 (6712): 695-9. ... 1998). "Cloning and expression of mouse legumain, a lysosomal endopeptidase". Biochem. J. 335 (Pt 1): 111-7. doi:10.1042/ ... 2003). "Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo". J. Biol. Chem. 278 (40): 38980-90. doi: ...
Alternative names for this enzyme include Nepenthes acid proteinase and Nepenthes aspartic proteinase. Two isozymes have been ... The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the ... 3. Acid proteases in the genus Nepenthes and Drosera peltata". J. Biochem. 72 (1): 73-81. PMID 5069751. Amagase S, Mori M, ... Nepenthesin (also spelled nepenthacin or nepenthasin) is an aspartic protease of plant origin that has so far been identified ...
... especially glutamic acid, and to some extent aspartic acid.. Glutamyl endopeptidase has been shown to cleave certain target ... Glutamyl endopeptidase is in S. aureus expressed from the gene sspA within the operon ssp. Downstream of sspA, the operon also ... Glutamyl endopeptidase is expressed as a zymogen that, in order to become fully active, has been modified both through ... Glutamyl endopeptidase can inhibit the activation of targets within the complement system. It is indicated to cause inhibition ...
Candida albicans secretory acid proteinase, Candida olea acid proteinase, Candida aspartic proteinase, Candida olea aspartic ... Activates trypsinogen, and degrades keratin This endopeptidase is present in yeast Candida albicans. Remold H, Fasold H, Staib ... This enzyme catalyses the following chemical reaction Preferential cleavage at the carboxyl of hydrophobic amino acids, but ... Candidapepsin (EC, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, ...
Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. More recently, aspartic ... LaPointe CF, Taylor RK (January 2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". The ... The MEROPS online database for peptidases and their inhibitors: Aspartic Peptidases Aspartic+Endopeptidases at the US National ... GPR endopeptidase family) Clan AF (e.g. Omptin family) Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are ...
... aspartic; C, cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and ... These endopeptidases include CAAX prenyl protease 1, which proteolytically removes the C-terminal three residues of ... The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are histidine, glutamate ... In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule. In many instances the ...
The defining features of these enzymes are a unique catalytic triad, Ser/Glu/Asp, as well as the presence of an aspartic acid ... The proprotein-processing endopeptidases kexin, furin and related enzymes form a distinct subfamily known as the kexin ... Members of the kexin family, along with endopeptidases R, T and K from the yeast Tritirachium and cuticle-degrading peptidase ... Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. Subtilase is ...
The protein is rich in acidic residues: 30-36% are either aspartic or glutamic acid. OPN is a highly negatively charged, ... PHEX (phosphate-regulating endopeptidase homolog X-linked) is one such enzyme, which extensively degrades OPN, and whose ... Contiguous stretches of high negative charge in OPN have been identified and named the polyAsp motif (poly-aspartic acid) and ... Kiefer MC, Bauer DM, Barr PJ (April 1989). "The cDNA and derived amino acid sequence for human osteopontin". Nucleic Acids ...
... is an aspartic protease, using a catalytic aspartate in its active site. It is one of three principal endopeptidases ( ... "Acid and non-acid reflux in patients with persistent symptoms despite acid suppressive therapy: a multicentre study using ... Weak or non-acid reflux is correlated with reflux symptoms and mucosal injury. Under non-acid conditions (neutral pH), pepsin ... Amino acid residues 1 - 3 (Gln-Phe-Leu) of mature PI-3 bind to P1' - P3' positions of pepsin. The N-terminus of PI-3 in the PI- ...
... aspartic acid, metallo- and acid proteases) nucleophilic so that it can attack the peptide carbonyl group. One way to make a ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). Catalysis is achieved by one of two mechanisms: ... aspartic, and metallo proteases. The threonine and glutamic-acid proteases were not described until 1995 and 2004 respectively ... using a threonine secondary alcohol Aspartic proteases - using an aspartate carboxylic acid Glutamic proteases - using a ...
This endopeptidase is isolated from Scytalidium lignicolum. It is an acid protease, and is most active at pH 2.0 when casein is ... Scytalidium lignicolum aspartic proteinase B, SLB) is a proteolytic enzyme. It was previously thought to be an aspartic ... Eqolosins prefer bulky amino acid residues at the P1 site and small amino acid residues at the P1′ site. The substrate ... "Complete amino acid sequence of Scytalidium lignicolum acid protease B". Journal of Biochemistry. 95 (2): 465-475. doi:10.1093/ ...
Cleavage of Dronc by DrICE occurs at residue D135 (Asp135, an aspartic acid residue). At the beginning of apoptosis, full- ... The main function of this kind of endopeptidases is to catalyze the hydrolysis of peptide bonds in order to cleave proteins ... The Dronc protein has a length of 450 amino acids and a mass of 51,141 Da. Although most human caspases are considered ... It belongs to the cysteine-aspartic proteases family, as it is a protease enzyme that takes part in programmed cell death ...
Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS (April 2004). "IA3, an aspartic ... This family includes PinA, which inhibits the endopeptidase La. It binds to the La homotetramer but does not interfere with the ... Murai H, Hara S, Ikenaka T, Oda K, Murao S (January 1985). "Amino acid sequence of Streptomyces metallo-proteinase inhibitor ... The saccharopepsin inhibitor I34 is highly specific for the aspartic peptidase saccharopepsin. In the absence of saccharopepsin ...
Another family of signal aspartic endopeptidases was found in bacteria. Bacteria produce a number of protein precursors that ... A nine amino acid-long cleavage fragment is then presented on HLA-E receptors and modulates the activity of natural killer ... Martoglio B, Golde TE (October 2003). "Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide ... which differ from mature pilin by virtue of containing a 6-8 residue leader peptide consisting of charged amino acids. Mature ...
"Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11". FEBS Lett. ... in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water ... Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC and determined by the presence of peptidase family M13 as a ... Malfroy B, Schofield PR, Kuang WJ, Seeburg PH, Mason AJ, Henzel WJ (April 1987). "Molecular cloning and amino acid sequence of ...
Family N2: Includes tetraviruses endopeptidases. The known autolytic cleavage is from the C-terminus of the coat protein. The ... ISBN 9780123822208 Guoyao Wu (2013) Amino Acids: Biochemistry and Nutrition. ISBN 9781439861899 Klaudia Brix, Walter Stöcker ( ... Asparagine Lyase Protein precursor Proteolysis Nucleophilic substitution Protease cysteine- serine- threonine- aspartic- ... Reddy, A., Schneemann, A. & Johnson, J.E. Nodavirus endopeptidase. In Handbook of Proteolytic Enzymes, 2 edn (Barrett, A.J., ...
... arginine-glycine-aspartic acid) motif. Most disintegrins contain this conserved RGD motif, but ADAM15 is the only member of the ... MMPs are a large multigene family of zinc-dependent endopeptidases. The collective MMP family is capable of degrading all known ... They include serine, aspartic, and cysteine-type proteases. A highly characterized example of the serine protease family is the ... Aminopeptidases function as exopeptidases which remove amino acids from the amino-terminus of proteins. Aminopeptidase N (CD13/ ...
... (EC, yeast endopeptidase A, Saccharomyces aspartic proteinase, aspartic proteinase yscA, proteinase A ... The lobes are folded so that an aspartic acid from each lobe line up to form the active site of the protein. The structure of ... Structure Proteinase A is relatively simple protein and is 329 amino acid residues in length. It is composed of both alpha ... This enzyme is present in baker's yeast (Saccharomyces cerevisiae). Proteinase A is an aspartic proteinase found in ...
... and a pro-segment carrying 20 and 46 amino acids, respectively. Mature renin contains 340 amino acids and has a mass of 37 kDa ... Renin (etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted ... Renin activates the renin-angiotensin system by using its endopeptidase activity to cleave angiotensinogen, produced by the ... The primary structure of renin precursor consists of 406 amino acids with a pre- ...
... generally a negatively charged aspartic acid or glutamic acid). The S1 pocket of chymotrypsin-like enzymes is more hydrophobic ... Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the ... The carboxyl group on the aspartic acid in turn hydrogen bonds with the histidine, making the nitrogen atom mentioned above ... These three key amino acids each play an essential role in the cleaving ability of the proteases. While the amino acid members ...
It is an aspartic endopeptidase belonging to MEROPS A1 family. It is produced by newborn ruminant animals in the lining of the ... Bovine chymosins A and B differ by one amino acid residue. This is probably an alleic variant, according to Uniprot:P00794. The ... The native substrate of chymosin is K-casein which is specifically cleaved at the peptide bond between amino acid residues 105 ... October 1991). "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin". ...
... s are used as feed additives for livestock to improve the digestibility of proteins and amino acids. Protease ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the US National ... and the aspartic protease precursor pepsinogen. The protease is activated by removal of an inhibitory segment or protein. ... Mitchel RE, Chaiken IM, Smith EL (July 1970). "The complete amino acid sequence of papain. Additions and corrections". The ...
Energy-dependent acid transport was verified and the postulated proton pump purified. With the successful culture of ... The matrix metalloproteinases (MMPs) comprise a family of more than 20 zinc-dependent endopeptidases. The role of matrix ... The function of these cysteine and aspartic proteases is generally unknown within bone, and they are expressed at much lower ... Attachment to the bone matrix is facilitated by integrin receptors, such as αvβ3, via the specific amino acid motif Arg-Gly-Asp ...
... endopeptidase So) EC Now covered by the microbial aspartic proteinases EC (penicillopepsin), EC ( ... The activity may be that of an acid phosphatase EC The activity may be that of an acid phosphatase EC ... Ste24 endopeptidase EC S2P endopeptidase EC ADAM 17 endopeptidase EC ADAMTS13 endopeptidase EC ... Ste24 endopeptidase EC S2P endopeptidase EC ADAM 17 endopeptidase EC ADAMTS13 endopeptidase EC ...
Both 2A(pro) and 3C(pro) induce caspase-8-mediated by activation of caspase-3. Caspase stands for cysteine-aspartic acid ... Picornain 3C's endopeptidase activity is primarily responsible for the catalytic process of selectively cleaving Gln-Gly bonds ... Picornain 3C are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ...
... endopeptidases MeSH D08.811.277.656.300.066 - aspartic endopeptidases MeSH D08.811.277.656.300.066.180 - cathepsin d MeSH ... amino acid oxidoreductases MeSH D08.811.682.664.500.062 - alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid ... endopeptidase clp MeSH D08.811.277.656.300.760.247 - endopeptidase k MeSH D08.811.277.656.300.760.284 - enteropeptidase MeSH ... l-amino acid oxidase MeSH D08.811.682.664.500.724 - leucine dehydrogenase MeSH D08.811.682.664.500.772 - nitric oxide synthase ...
But more often groups in substrate and active site act as Brønsted-Lowry acid and base. This is called general acid and general ... 137-9 Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... 158 In some reactions, protons and hydroxide may directly act as acid and base in term of specific acid and specific base ...
... s share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a ... and aspartic proteases). In humans, there are 11 cysteine cathepsins: B, C, F, H, K, L, O, S, V, X, and W. Most cathepsins are ... Papain-like proteases are usually endopeptidases, but some members of the group are also, or even exclusively, exopeptidases. ... Nucleic Acids Research. 46 (D1): D624-D632. doi:10.1093/nar/gkx1134. PMC 5753285. PMID 29145643. Kamphuis, I.G.; Kalk, K.H.; ...
A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC ... A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC ...
... which mainly includes aspartic acid cathepsin, serine cathepsin, asparagine endopeptidases, and cysteine cathepsins. Among them ... The mRNA expression of PLEKHA4 was detected by PCR in glioma samples and controls and in glioma cells treated with lactic acid ... Lactic acid produced by glycolysis upregulates the expression of PLEKHA4 in glioma cells. ... OBJECTIVE: To investigate the effect of lactic acid-induced upregulation of PLEKHA4 expression on biological behaviors of ...
Carboxyl (Acid) Proteinases use Aspartic Endopeptidases. Carboxyl and Carbamoyl Transferases. Carboxylase Deficiency, Multiple ...
Aspartic Acid Endopeptidases. * Asthma. * Child. * Child, Preschool. * Cockroaches. * Humans. * Immunization. * Insect Proteins ...
Currently, the content of 10-hydroxy-2-decenoic acid (10-HDA), which is a chemically stable fatty acid unique to RJ, is ... μL of 0.005 g/L aspartic protease/100 mM NH4HCO3 (Asp-N, #V162A, Promega K.K., Tokyo, Japan) at 37°C for 16 h (overnight). The ... μL of 0.01 g/L lysyl endopeptidase/100 mM NH4HCO3 (Lys-C, #125-05061, Wako Pure Chemical Industries, Ltd., Osaka, Japan) or ... formic acid/water to 0.1% formic acid/ACN in 80 min) at a flow rate of 0.2 mL/min via an ultraperformance liquid chromatograph ...
Aspartic Acid Proteases. *ATP-Dependent Proteases. *Cathepsins. *Cysteine Proteases. *Endopeptidases. *Exopeptidases. * ...
aspartic-type endopeptidase. F:aspartic-type endopeptidase activity;P:proteolysis;C:endomembrane system;PF. O.I.. H.G.. S.X.. ... protein amino acid phosphorylation;C:plasma membrane;MPOBFVA. O.I.. H.G.. S.X.. Please select. TAIR (integral). KEGG (integral) ...
aspartic-type endopeptidase activity GO:0004190 Molecular Function 0.0. - Sma3. ubiquitin thiolesterase activity GO:0004221 ... Peptidase C45, acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase IPR005079 - 0.0. - ... Peptidase aspartic, catalytic IPR009007 - 0.0. - Sma3. Regulator of chromosome condensation/beta-lactamase-inhibitor protein II ...
aspartic-type endopeptidase activity. IEP. Enrichment. MF. GO:0004375. glycine dehydrogenase (decarboxylating) activity. IEP. ... serine family amino acid metabolic process. IEP. Enrichment. BP. GO:0009071. serine family amino acid catabolic process. IEP. ... carboxylic acid catabolic process. IEP. Enrichment. MF. GO:0051002. ligase activity, forming nitrogen-metal bonds. IEP. ... cellular amino acid catabolic process. IEP. Enrichment. BP. GO:0009069. ...
systemic potential acids have in contents of the transthoracic acid of the optimum problem and therapy to the cardiac and acute ... In our type, the systolic aspartic discriminating neurohormones of the exercise glucose need luminal to its adrenergic Date and ... Web element that is, at no area, Endopeptidases of goals performed by form antihypertensive. treating MEDICAL LIBRARIES ... It has rate to the many and intact Anesthetics markedly with the effective acid of the General example and the nitric ambient ...
It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and ... A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE ... N-Acetylneuraminic Acid. An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, ... Amino Acid Sequence. The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary ...
An alternative hypothesis has also been mentioned that the nearby aspartic acid residue can be the proton-accepting group ... a Zn2+ dependant endopeptidase, specifically binds and cleaves synaptosomal-associated protein of 25 kDa (SNAP-25). Cleavage of ... The choice press are generated with the addition of defined combination of amino acids, vitamin supplements and additional ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Amino acid hydroxylases C. *L-Arginine turnover C *2.1.1.- Protein arginine N-methyltransferases C ... AA: Aspartic (A) Peptidases C*A1: Pepsin C. *AD: Aspartic (A) Peptidases C*A22: Presenilin C ... C48: Ulp1 endopeptidase. *M-: Metallo (M) Peptidases*M79: Prenyl protease 2. *MA: Metallo (M) Peptidases C*M1: Aminopeptidase N ...
Aspartic Acid Endopeptidases Actions. * Search in PubMed * Search in MeSH * Add to Search ... X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor ... An n→π* Interaction in the Bound Substrate of Aspartic Proteases Replicates the Oxyanion Hole. Windsor IW, Gold B, Raines RT. ... The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases. Dunn BM, Hung S. Dunn BM, et al. Biochim ...
MeSH Terms: Animals; Aspartic Acid Endopeptidases/metabolism*; Biofilms/growth & development*; Candida albicans/metabolism*; ...
Aspartic Acid Endopeptidases / antagonists & inhibitors Actions. * Search in PubMed * Search in MeSH ... polyunsaturated fatty acids; ROS, reactive oxygen species; TwX, Twendee X; TXN, taxifolin. ...
Isonicotinic Acids,N0000007955, Aspartic Endopeptidases,N0000007954, Uracil,N0000007953, Tetrahydronaphthalenes,N0000007952, ... Amino Acids, Diamino,N0000007704, Amino Acids, Cyclic,N0000007703, Amino Acids, Branched-Chain,N0000007702, Penicillanic Acid, ... Clavulanic Acid,N0000005804, Benzoic Acid,N0000005803, Omeprazole,N0000005802, Oxalic Acid,N0000005801, Myristic Acid, ... Acids, Noncarboxylic,N0000007630, Acids, Heterocyclic,N0000007629, Acids, Carbocyclic,N0000007628, Acids, Acyclic,N0000007627, ...
Aspartic Acid Proteases [D08.811.277.656.074] * Aspartic Acid Endopeptidases [D08.811.277.656.074.500] * Cathepsin D [D08.811. ... A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.. Terms. Aspartic Acid ... A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.. Entry Term(s). Aspartic ... Aspartic Acid Endopeptidases Preferred Concept UI. M0024885. Registry Number. EC 3.4.23.-. Scope Note. ...
Aspartic Endopeptidases. Aspartic Acid Endopeptidases. Carboxypeptidase C. Cathepsin A. Dipeptidyl Peptidase I. Cathepsin C. ... p-Aminosalicylic Acid. Aminosalicylic Acid. D04 - Polycyclic Compounds. Medroxyprogesterone 17-Acetate. Medroxyprogesterone ...
Aspartic Acid Proteases [D08.811.277.656.074] * Aspartic Acid Endopeptidases [D08.811.277.656.074.500] * Cathepsin D [D08.811. ... A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.. Terms. Aspartic Acid ... A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.. Entry Term(s). Aspartic ... Aspartic Acid Endopeptidases Preferred Concept UI. M0024885. Registry Number. EC 3.4.23.-. Scope Note. ...
Aspartic Endopeptidases. Aspartic Acid Endopeptidases. Carboxypeptidase C. Cathepsin A. Dipeptidyl Peptidase I. Cathepsin C. ... p-Aminosalicylic Acid. Aminosalicylic Acid. D04 - Polycyclic Compounds. Medroxyprogesterone 17-Acetate. Medroxyprogesterone ...
Urocanic Acid) RN - 56-84-8 (Aspartic Acid) RN - 71-00-1 (Histidine) RN - 94242-73-6 (O-methyl-succinyl-alanyl-alanyl-prolyl- ... Endopeptidases) RN - EC 3.4.21.- (Subtilisins) SB - IM MH - Amino Acid Sequence MH - Animals MH - Butanols MH - Cattle MH - ... Aspartic Acid/chemistry MH - Binding Sites MH - Boronic Acids/metabolism MH - Catalysis MH - Histidine/chemistry MH - Hydrogen ... Abscisic Acid) RN - 69-72-7 (Salicylic Acid) RN - 7647-14-5 (Sodium Chloride) SB - IM MH - Abscisic Acid/pharmacology MH - ...
HN - 2010; use ASPARTIC ACID ENDOPEPTIDASES 1991-2009 BX - Aspartic Acid Proteinases BX - Aspartic Proteinases BX - Aspartyl ... Aspartic Acid Proteases UI - D057055 MN - D8.811.277.656.74 MS - A subclass of peptide hydrolases that depend on an ASPARTIC ... AN - do not confuse with CYSTEINE ENDOPEPTIDASES HN - 2010, 1988-1999; use CYSTEINE ENDOPEPTIDASES 2000-2009 BX - Cysteine ... AN - do not confuse with SERINE ENDOPEPTIDASES HN - 2010, 1988-1999; use SERINE ENDOPEPTIDASES 2000-2009 BX - Serine ...
The portion of SNAP-25 from isoleucine-156 to aspartic acid-186 is required for cleavage between arginine-180 and isoleucine- ... Endopeptidase reactions were multiplexed by adding all 4 peptides (1-4) at 1 nmol each to the reaction buffer described above ... formic acid and B: 80:20 acetonitrile:H2O plus 1% (vol/vol) formic acid. Peptides were eluted with a linear gradient of 0% to ... was added to alpha-cyano-4-hydroxy cinnamic acid (CHCA) at 5 mg/mL in 50% acetonitrile, 0.1% trifluoroacetic acid, and 1 mmol/L ...
Aspartic Acid Endopeptidases QU 136 Connect with NLM. *. *. *. National Library of Medicine 8600 Rockville Pike Bethesda, MD ...
HA: Hyaluronic acid; MT1-MMP: Membrane type-1 matrix metalloproteinase; RGD: Arginine-glycine-aspartic acid; TfR: Transferrin ... Membrane Matrix Metalloproteinase Membrane matrix metalloproteinases are a family of zinc-dependent endopeptidases capable of ... Retinoic acid. All-trans retinoic acid. [16]. Retinoic-X receptor. Retinoic acid. All-trans retinoic acid, 9-cis retinoic acid ... by the arginine-glycine-aspartic acid (RGD) sequence. These cell surface receptors are expressed on tumor cells as well as ...
Gainer H, Russell JT and Loh YP (1984) Angiotensin I-generating acid endopeptidase activity in neurosecretory vesicles isolated ... 1995) Characteristics of YAP3, a new prohormone processing aspartic protease from S. cerevisiae. In: Aspartic Proteinases. ... Cawley NX, Wong M, Pu L-P, Tam W and Loh YP (1995) Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminus ... Bamberger AM, Bamberger CM, Pu L-P, Puy LA, Loh YP and Asa SL (1995) Expression of Pit-1 messenger ribonucleic acid and protein ...
Aspartic endopeptidases were predominant endopeptidases, followed by cysteine ones. There were two types of aspartic ... Prolylcarboxypeptidase (PRCP) is a lysosomal serine protease that cleaves peptide substrates when the penultimate amino acid is ... COVID-19 , Choque Séptico , Carboxipeptidases , Dipeptidil Peptidase 4 , Endopeptidases , Gelatinases , Humanos , Proteínas de ... In this study, endopeptidases, aminopeptidases, carboxypeptidases, superoxide dismutases, catalases, and phospholipases with ...
Aspartic Acid Aspartic Acid Endopeptidases Aspartic Acid Proteases Aspartokinase Homoserine Dehydrogenase ... Amino Acids Amino Acids, Acidic Amino Acids, Aromatic Amino Acids, Basic Amino Acids, Branched-Chain Amino Acids, Cyclic Amino ... Acid Ceramidase Acid Etching, Dental Acid Phosphatase Acid Rain Acid Sensing Ion Channel Blockers Acid Sensing Ion Channels ... Acids Acids, Acyclic Acids, Aldehydic Acids, Carbocyclic Acids, Heterocyclic Acids, Noncarboxylic Acidulated Phosphate Fluoride ...
Nucleic acid binding. 786 Select filter option. Transcription factor. 756 Select filter option. Class A rhodopsin like. 732 ... aspartic protease. 23 Select filter option. transcription factor. 21 Select filter option. RNA binding protein. 20 Select ... endopeptidase activity. 47 Select filter option. identical protein binding. 40 Select filter option. calcium ion binding. 36 ... nucleic acid binding. 41 Select filter option. calcium-binding protein. 28 Select filter option. annexin. 26 Select filter ...
Nucleic acid binding. 786 Select filter option. Transcription factor. 756 Select filter option. Class A rhodopsin like. 732 ... aspartic protease. 23 Select filter option. transcription factor. 21 Select filter option. RNA binding protein. 20 Select ... endopeptidase activity. 47 Select filter option. identical protein binding. 40 Select filter option. calcium ion binding. 36 ... nucleic acid binding. 41 Select filter option. calcium-binding protein. 28 Select filter option. annexin. 26 Select filter ...
Receptor for bile acids such as chenodeoxycholic acid, lithocholic acid and deoxycholic acid. Represses the transcription of ... When secreted, it acts primarily as an endopeptidase. " Q62867.1 ... 113858 53.72 napsin A aspartic peptidase Napsa Rattus ... Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA (chenodeoxycholoyl-CoA) substrate. Shows a ... linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid ...
Soluble metallo-endopeptidase (substance) {17023007 , SNOMED-CT } Sorghum aspartic proteinase (substance) {83814001 , SNOMED-CT ... Acylamino-acid-releasing enzyme (substance) {32216001 , SNOMED-CT } Aeromonolysin (substance) {130703007 , SNOMED-CT } Agavain ... Leukocyte-membrane neutral endopeptidase (substance) {42210005 , SNOMED-CT } Lotus aspartic proteinase (substance) {82021009 , ... Aspergillus saitoi aspartic proteinase (substance) {53491008 , SNOMED-CT } Astacin (substance) {130699009 , SNOMED-CT } ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. Prebióticos. ... Endopeptidases Dependentes de ATP. ATP-Dependent Endopeptidases. Endopeptidasas ATP-Dependientes. Histona Desacetilase 1. ...
  • The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic proteinases. (nih.gov)
  • By comparing the residues on the binding surface with those of the other human aspartic proteinases, it has been possible to rationalize some of the experimental data concerning the different specificities. (nih.gov)
  • The product peptides derived from the endopeptidase activities of BoNTs are detected by matrix-assisted laser-desorption ionization time-of-flight mass spectrometry. (cdc.gov)
  • HN - 2010 MH - Aerococcaceae UI - D056567 MN - B3.510.550.30 MS - A family of gram-positive lactic acid-producing bacteria in the order LACTOBACILLALES. (nih.gov)

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