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)

Meredith, J.E.; Thompson, L.A.; Toyn, J.H.; Marcin, L.; Barten, D.M.; Marcinkeviciene, J.; Kopcho, L.; Kim, Y.; Lin, A.; Guss, V.; Burton, C.; Iben, L.; Polson, C.; Cantone, J.; Ford, M.; Drexler, D.; Fiedler, T.; Lentz, K.A.; Grace, J.E.; Kolb, J.; Corsa, J.; Pierdomenico, M.; Jones, K.; Olson, R.E.; Macor, J.E.; Albright, C.F., 2008: P-glycoprotein efflux and other factors limit brain amyloid beta reduction by beta-site amyloid precursor protein-cleaving enzyme 1 inhibitors in mice
Endothelin-converting enzyme (ECE-1) is a type II integral membrane protein which plays a key role in the biosynthetic pathway of the vasoconstricting endothelins. Three ECE-1 isoforms, differing by their N-terminal cytoplasmic tails, are generated from a single gene. When expressed in CHO cells, they display comparable enzymatic activity but whereas ECE-1a is strongly expressed at the cell surface, ECE-1b is exclusively intracellular and ECE-1c presents an intermediate distribution. In the present study these different localizations were further described at the ultrastructural level, by electron microscope immunocytochemistry. To characterize the motifs responsible for the intracellular localization of ECE-1b we constructed chimeric proteins and point mutants. Two di-leucine-based motifs, contained in the N-terminal part of ECE-1b, were thus identified. One of these motifs (LV), displayed by both ECE-1b and ECE-1c, accounts for the reduced surface expression of ECE-1c as compared to ECE-1a. ...
Secretory aspartyl proteinases (Sap) have long been considered key virulence traits of C. albicans, with rather strong experimental and clinical evidence for a major role in vaginal candidiasis (1, 3). However, the mechanisms by which this family of enzymes is involved in vaginal disease have remained unclear. Sap are active enzymes with a wide range of substrate specificities (26). Since some of these substrates (e.g., complement, histatins, and E-cadherin, and also Abs) play critical roles in both innate and adaptive immune responses, Sap expression is thought to enable the fungus to evade host immunity by enzymatic proteolysis of one or more of the above factors (1, 3). Concurrently, studies in well-established animal models and reconstituted human vaginal epithelia have provided indirect clues for a role of some members of the Sap family in facilitating fungus adherence and penetration into epithelial tissues (27-30). Evidence gathered with the use of anti-Sap Abs supports this proadherence ...
A new aspartic protease from Saccharomyces cerevisiae, with a high degree of similarity with yapsin 1 and yapsin 2 and a specificity for basic residue cleavage sites of prohormones, has been cloned. This enzyme was named yapsin 3. Expression of a C-terminally truncated non-membrane anchored yapsin 3 in yeast yielded a heterogeneous protein between 135-200 kDa which, upon treatment with endoglycosidase H, migrated as a 60 kDa form. Amino-acid analysis of the N-terminus of expressed yapsin 3 revealed two different N-terminal residues, serine-48 and phenylalanine-54, which followed a dibasic and a monobasic residue respectively. Cleavage of several prohormones by non-anchored yapsin 3 revealed a specificity distinct from that of yapsin 1.. ...
Fingerprint Dive into the research topics of The endothelin-converting enzyme-1/endothelin-1 pathway plays a critical role in inflammation-associated premature delivery in a mouse model. Together they form a unique fingerprint. ...
Our goal in this work was to determine if signal peptide peptidase is necessary for normal animal development. We present data showing that Drosophila Spp encodes the fly ortholog of human signal peptide peptidase and show that Drosophila Spp provides an essential function required during the larval stages. We also show that SPP is strongly expressed in only a limited set of cells and that the mutant phenotype is consistent with a need for its function in these tissues. Further work will be needed to establish whether the role of Drosophila SPP is a general one that cleanses membranes of signal peptides or if it has specific targets and generates essential products through its action.. Human SPP is an intramembrane aspartyl protease whose active site is predicted to be buried within the lipid bilayer. It belongs to a family of enzymes conserved among animals, plants, and fungi (Ponting et al. 2002; Weihofen et al. 2002). The Drosophila and human SPPs have strong sequence similarity, with the ...
This chapter elaborates the structural chemistry and the biological aspects of plasmepsins. Plasmepsin I is capable of cleaving native human hemoglobin and acid-denatured globin, with a pH optimum around 5. Plasmepsin I, II, IV and HAP are made as 51 kDa precursors that are cleaved to 37 kDa mature forms. There are two disulfide bonds predicted. The second domain contains an active-site Asp-Ser-Gly instead of the usual aspartic protease Asp-Thr-Gly. HAP is an exception to this. A molecular model of plasmepsin I has been constructed, based on the crystal structure of the highly homologous plasmepsin II. The modeled structure bears general features of mammalian and fungal aspartic proteases, and among mammalian orthologs shares greatest structural similarity with cathepsin D. Pepstatin is bound in the active site with enough conformational difference from mammalian homologs to give hope for development of a selective inhibitor. Native plasmepsin I, II and HAP can be prepared in nanogram to low ...
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This paper focuses deals with the cleavage of NaVβ2 via BACE-1 (Beta-site APP-cleaving enzyme 1), leading to increased NaV1.1 levels, which do not translocate to the cell plasma membrane. Reinforcing that decreased NaV1.1 levels are involved in AD development/progression. This work cites the use of Alomone Labs Anti-SCN1A (NaV1.1) Antibody (#ASC-001) and Anti-NaVβ2 Antibody (#ASC-007).. The early stages of Alzheimers disease (AD), an incurable neurological affliction with adverse effects on memory and cognition, are often accompanied by aberrant neuronal activity and epileptic seizures - events which are increasingly seen as having a direct influence on ADs progression. Cortical accumulation of amyloid β (Aβ), a peptide derived from amyloid precursor protein (APP), seems to play a prominent role on the onset of AD. Beta-site APP-cleaving enzyme 1 (BACE1) - the rate-determining factor in Aβ synthesis - is significantly high in both AD patients and APP mice (transgenic line with ...
Authors: Moussavi Nik, Seyyed Hani , Wilson, Lachlan , Newman, Morgan , Croft, Kevin , Mori, Trevor A. , Musgrave, Ian , Lardelli, Michael Article Type: Research Article Abstract: Oxygen homeostasis is essential for the development and normal physiology of an organism. Hypoxia causes the mitochondrial electron transport chain to generate higher levels of reactive oxygen species resulting in oxidative stress. Hypoxia can be a direct consequence of hypoperfusion, a common vascular component among Alzheimers disease (AD) risk factors, and may play an important role in AD pathogenesis. Beta-site amyloid-β A4 precursor protein-cleaving enzyme 1 (BACE1) is responsible, with γ-secretase, for cleavage of the amyloid-β protein precursor (AβPP) to produce amyloid-β (Aβ) peptide. A recent study observed that oxidative stress increases BACE1 expression via a regulatory pathway dependent on …γ-secretase cleavage of AβPP and this increases Aβ peptide production. Zebrafish embryos represent normal ...
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ENDOTHIAPEPSIN(2s)-1-{[(2r)-1-{[(2s,3r)-1-Cyclohexyl-3-Hydroxy-4-(Pyridin-4-Yloxy)butan-2-Yl]amino}-3-(Methylsulfanyl)-1-Oxopropan-2-Yl]amino}-1-Oxo-3-Phenylpropan-2-Yl 4-Aminopiperidine-1-Carboxylate
Reagents, Tools and Custom Services for molecular biology, specializing in the fields of Nano-Antibody development (nAb), Cellular Reprogramming (iPSC), Genome Editing, Fluorescent Proteins, RNAi, Viral Packaging and Protein expression.
Intramembrane proteases cleave peptide bonds within cellular membranes and thereby control important processes ranging from transcription regulation to growth factor secretion (Lemberg, 2011). The largest and most diverse group of these unusual enzymes is formed by the GxGD aspartyl proteases including presenilin/γ‐secretase as well as signal peptide peptidase (SPP) (Wolfe, 2009; Lichtenthaler et al, 2011). SPP localizes to the endoplasmic reticulum (ER) where it cleaves signal peptides that have been removed from precursors of secretory and membrane proteins (Weihofen et al, 2002). Like for most characterized intramembrane proteases, this release is part of a two‐step mechanism: First signal peptidase cleaves off the substrate proteins ectodomains, which enables the subsequent SPP‐catalyzed intramembrane cut (Lemberg & Martoglio, 2002). So far, known functions of SPP include generation of signal peptide‐derived bioactive peptides in immune surveillance and proteolytic maturation of ...
In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs YD and GxGD in adjacent transmembrane domains (TMDs). Its sequences is highly conserved in different vertebrate species. SPP cleaves remnant signal peptides left behind in membrane by the action of signal peptidase and also plays key roles in immune surveillance and the maturation of certain viral proteins. Physiologically SPP processes signal peptides of classical MHC class I preproteins. A nine amino acid-long cleavage fragment is then presented on HLA-E receptors and modulates the activity of natural killer cells. SPP also plays a pathophysiological role; it cleaves the structural nucleocapsid protein (also known as core protein) of the Hepatitis C virus and thus influences viral reproduction rate. In mice, a nonamer peptide originating from the SPP protein serves as minor ...
3RTM: From Fragment Screening to In Vivo Efficacy: Optimization of a Series of 2-Aminoquinolines as Potent Inhibitors of Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE1).
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
A phosphoramidon-sensitive metalloendopeptidase in peptidase family M13 (neprilysin family). An integral membrane protein predominantly of endothelial cells, which genera
BACE1 - BACE1 (untagged)-Human beta-site APP-cleaving enzyme 1 (BACE1), transcript variant a available for purchase from OriGene - Your Gene Company.
Isoform Delta of Protachykinin-1 contains a PF02202 domain.. Isoform Delta of Protachykinin-1 contains a PF02202 domain.. Isoform Delta of Protachykinin-1 is proteolytically cut by dipeptidyl-peptidase II (S28.002) cleavage. --RP-KPQQ.. Isoform Delta of Protachykinin-1 is proteolytically cut by (S9F.001) cleavage. FFGL-MNH2--.. Isoform Delta of Protachykinin-1 is proteolytically cut by penicillolysin (M35.001) cleavage. RPKP-QQFF.. Isoform Delta of Protachykinin-1 is proteolytically cut by aminopeptidase P1 (M24.009) cleavage. ---R-PKPQ.. Isoform Delta of Protachykinin-1 is proteolytically cut by endothelin-converting enzyme 1 (M13.002) cleavage. PQQF-FGLM.. Isoform Delta of Protachykinin-1 is proteolytically cut by endothelin-converting enzyme 1 (M13.002) cleavage. KPQQ-FFGL.. Isoform Delta of Protachykinin-1 is proteolytically cut by neprilysin (M13.001) cleavage. PQQF-FGLM.. Isoform Delta of Protachykinin-1 is proteolytically cut by neprilysin (M13.001) cleavage. KPQQ-FFGL.. Isoform Delta of ...
Multiple myeloma (MM) can be an indolent B-cell disease that develops in the bone tissue marrow and it is connected with osteolytic lesions in 1174043-16-3 the advanced phases [1]. site thats turned on in Tyr1356 and Tyr1349. The phosphorylation of the region leads to the induction of MET signaling through the activation of many downstream …Read More. ...
Intramembrane proteolysis, Alzheimer´s disease, Parkinsons disease, type-2 diabetes, γ-secretase, signal peptide peptidase , substrate enzym interactions, TMD, DFG Verbundprojekt, Lemberg, Fluhrer, Lichtenthaler, Steiner, Langosch, Haass, Frishman, Scharnagl, Luy, Huster,
Intramembrane proteolysis, Alzheimer´s disease, Parkinsons disease, type-2 diabetes, γ-secretase, signal peptide peptidase , substrate enzym interactions, TMD, DFG Verbundprojekt, Lemberg, Fluhrer, Lichtenthaler, Steiner, Langosch, Haass, Frishman, Scharnagl, Luy, Huster,
TY - JOUR. T1 - Arresting inflammation: Contributions of plasma membrane and endosomal signalling to neuropeptide-driven inflammatory disease. AU - Cattaruzza, Fiore. AU - Poole, Daniel Philip. AU - Bunnett, Nigel William. PY - 2013. Y1 - 2013. N2 - GPCR (G-protein-coupled receptor) signalling at the plasma membrane is under tight control. In the case of neuropeptides such as SP (substance P), plasma membrane signalling is regulated by cell-surface endopeptidases (e.g. neprilysin) that degrade extracellular neuropeptides, and receptor interaction with ?-arrestins, which uncouple receptors from heterotrimeric G-proteins and mediate receptor endocytosis. By recruiting GPCRs, kinases and phosphatases to endocytosed GPCRs, ?-arrestins assemble signalosomes that can mediate a second wave of signalling by internalized receptors. Endosomal peptidases, such as ECE-1 (endothelin-converting enzyme-1), can degrade SP in acidified endosomes, which destabilizes signalosomes and allows receptors, freed from ...
1OEX: Atomic Resolution Analysis of the Catalytic Site of an Aspartic Proteinase and an Unexpected Mode of Binding by Short Peptides
Recombinant Human BACE1 precursor extracellular domain (Met 1-Thr 457) (NP_036236.1), fused with a C-terminal polyhistidine tag, was produced in Human Cell.
Complete information for SPPL3 gene (Protein Coding), Signal Peptide Peptidase Like 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for SPPL2B gene (Protein Coding), Signal Peptide Peptidase Like 2B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Vitae Pharmaceuticals BACE inhibitor, VTP-37948, lowered cerebrospinal fluid Aβ by up to 80 percent in healthy volunteers, according to topline data from a Phase 1 clinical trial. A second Phase 1 trial that used a single-ascending-dose strategy suggested that volunteers tolerated the drug well. Vitae chief scientific officer Richard Gregg told Alzforum that the companies will soon test the inhibitor in multiple rising dose trials. Results should be available early next year, said Vitae CEO Jeffrey Hatfield. The company will develop the inhibitor, also known as BI 1181181, in partnership with Boehringer Ingelheim.. Vitae used a structure-based approach to develop the drug, which fits the catalytic pocket of the aspartyl protease. VTP-37948 joins BACE inhibitors being developed by other pharmaceutical companies including Merck, AstraZeneca/Lilly, and Novartis. The Vitae inhibitor, like the other compounds under development, does not discriminate between β-secretase isoforms, blocking both ...
Ece1 - Ece1 (untagged) - Mouse endothelin converting enzyme 1 (Ece1), (10ug) available for purchase from OriGene - Your Gene Company.
ECE1 overexpression lysate, 0.1 mg. Transient overexpression lysate of endothelin converting enzyme 1 (ECE1), transcript variant 1
We acknowledge that the UBC Point Grey campus is situated on the traditional, ancestral, and unceded territory of the xʷməθkʷəy̓əm (Musqueam ...
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Beta Secretase 1 (Aspartyl Protease 2 or Beta Site Amyloid Precursor Protein Cleaving Enzyme 1 or Memapsin 2 or Membrane Associated Aspartic Protease 2 or BACE1 or EC - Pipeline Review, H2 2018
The insidious progression of AD (Alzheimers disease) is believed to be linked closely to the production, accumulation and aggregation of the ∼4.5 kDa protein fragment called Aβ (amyloid β-peptide). Aβ is produced by sequential cleavage of the amyloid precursor protein by two enzymes referred to as β- and γ-secretase. β-Secretase is of central importance, as it catalyses the rate-limiting step in the production of Aβ and was identified 7 years ago as BACE1 (β-site APP-cleaving enzyme 1). Soon afterwards, its homologue BACE2 was discovered, and both proteins represent a new subclass of the aspartyl protease family. Studies examining the regulation and function of β-secretase in the normal and AD brain are central to the understanding of excessive production of Aβ in AD, and in targeting and normalizing this β-secretase process if it has gone awry in the disease. Several reports indicate this, showing increased β-secretase activity in AD, with recent findings by our group showing ...
Candida albicans secreted aspartyl proteinases (Sap), products of the SAP genes, which are presumed to act as virulence factors. In the C. albicans strain WO-1, the ability to secrete Sap1 is regulated with switch phenotype, another putative virulence factor. KpnI restriction fragment length polymorphisms differentiate between several distinct SAP1 alleles in laboratory and clinical strains. Both SAP1 alleles from strain WO-1 along with their 5- and 3-flanking regions were cloned and sequenced, as were both alleles from another strain, SS. The 5-flanking regions were remarkably similar in all four of the sequenced alleles over approximately 1,500 nucleotides. S1 analysis revealed that both alleles of WO-1 are transcribed. Characterization of the one allele from strain WO-1 identified a 284-nucleotide insertion flanked by 8-bp direct repeats that shows homology to the CARE2 repetitive element and that is not present in the other alleles. Characterization of the SAP1 alleles also identified a ...
The present invention provides compounds having the formula: wherein R1, R′, R2, R3, R3′, R4, X1, X2 and X3 are as defined herein, and pharmaceutical compositions thereof. The present invention also provides methods of inhibiting proteases, more specifically aspartyl proteases. In certain embodiments, compounds inhibit BACE (β-site APP-cleaving enzyme), and thus are useful in the treatment or prevention of a disease characterized by β-amyloid deposits in the brain (including, but not limited to, Alzheimers Disease). The present invention also provides methods for preparing compounds of the invention.
The present study describes a novel sensitive live-cell assay for studying ECE activity. ET-1 is formed from its precursor preproET-1 via the cleavage of the intermediate bigET-1 by ECE-1. However, the subcellular site at which this step occurs is not clear: It could occur intravesicularly along the secretory pathway or bigET-1 may be released and processed extracellularly. To address this point, we have developed an integrated autocrine system.. Until now, ECE activity has been evaluated in solubilized membrane fractions by high-performance liquid chromatography assays,32 immunoassays,12 fluorogenic determinations,33 receptor assays,34 and fluorescence polarization assays.35 Most of these assays require an incubation in vitro with high concentrations of substrate, and all of them need an independent second step to measure the product, ET-1.. In the present study, a recombinant CHO reporter cell line permanently expressing the human ETA receptor and a reporter gene sensitive to its activation ...
TY - JOUR. T1 - APH1, PEN2, and Nicastrin increase Aβ levels and γ-secretase activity. AU - Marlow, Laura. AU - Canet, Rosa M.. AU - Haugabook, Sharie J.. AU - Hardy, John A.. AU - Lahiri, Debomoy K.. AU - Sambamurti, Kumar. PY - 2003/6/6. Y1 - 2003/6/6. N2 - A major component of the amyloid plaque core in Alzheimers disease (AD) is the 40-42-residue amyloid β peptide (Aβ). Mutations linked to AD such as those in presenilins 1 (PS1) and 2 (PS2) invariably increase the longer Aβ42 species that forms neurotoxic oligomers. It is believed that PS1/2 constitute the catalytic subunit of the γ-secretase responsible for the final step in Aβ biogenesis. Recent genetic studies have identified a number of additional genes encoding APH1a, APH1b, PEN2, and Nicastrin proteins, which are part of the γ-secretase complex with PS1. Further, knockout studies using RNAi showed that these components are essential for γ-secretase activity. However, the nature of γ-secretase and how the aforementioned ...
cansSAR 3D Structure of 2OHR | X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6A | 2OHR_A | Beta-secretase 1 - Also known as BACE1_HUMAN, BACE1, BACE, KIAA1149. Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (PubMed:10656250, PubMed:10677483, PubMed:20354142). Cleaves CHL1 (By similarity). Monomer. Interacts (via DXXLL motif) with GGA1, GGA2 and GGA3 (via their VHS domain); the interaction highly increases when BACE1 is phosphorylated at Ser-498 (PubMed:14567678, PubMed:15886016). Interacts with RTN3 and RTN4 (PubMed:15286784, PubMed:16965550, PubMed:16979658). Interacts with SNX6 (PubMed:20354142). Interacts with PCSK9 (PubMed:18660751). Interacts with NAT8 and NAT8B (PubMed
Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin. Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised.[1] More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin[2] and archaean preflagellin have been described.[3][4] Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral duplication. Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. Each domain contributes a catalytic Asp residue, with an extended active ...
The intramembrane aspartyl protease gamma-secretase plays a fundamental role in several signaling pathways involved in cellular differentiation and has been linked with a variety of human diseases, including Alzheimers disease. Here, we describe a transgenic Drosophila model for in vivo-reconstituted gamma-secretase, based on expression of epitope-tagged versions of the four core gamma-secretase components, Presenilin, Nicastrin, Aph-1, and Pen-2. In agreement with previous cell culture and yeast studies, coexpression of these four components promotes the efficient assembly of mature, proteolytically active gamma-secretase. We demonstrate that in vivo-reconstituted gamma-secretase has biochemical properties and a subcellular distribution resembling those of endogenous gamma-secretase. However, analysis of the cleavage of alternative substrates in transgenic-fly assays revealed unexpected functional differences in the activity of reconstituted gamma-secretase toward different substrates, ...
Alzheimers disease (AD) is characterized by extracellular accumulation of amyloid-β peptide (Aβ), generated by proteolytic processing of the amyloid precursor protein (APP) by β- and γ-secretase. Aβ generation is inhibited when the initial ectodomain shedding is caused by α-secretase, cleaving APP within the Aβ domain. Therefore, an increase in α-secretase activity is an attractive therapeutic target for AD treatment. APP and the APP-cleaving secretases are all transmembrane proteins, thus local membrane lipid composition is proposed to influence APP processing. Although several studies have focused on γ-secretase, the effect of the membrane lipid microenvironment on α-secretase is poorly understood. In the present study, we systematically investigated the effect of fatty acid (FA) acyl chain length (10:0, 12:0, 14:0, 16:0, 18:0, 20:0, 22:0, 24:0), membrane polar lipid headgroup (phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine), saturation grade and the FA double-bond
Signal sequences are the addresses of proteins destined for secretion. In eukaryotic cells, they mediate targeting to the endoplasmic reticulum membrane and insertion into the translocon. Thereafter, signal sequences are cleaved from the pre-protein and liberated into the endoplasmic reticulum membrane. We have recently reported that some liberated signal peptides are further processed by the intramembrane-cleaving aspartic protease signal peptide peptidase. Cleavage in the membrane-spanning portion of the signal peptide promotes the release of signal peptide fragments from the lipid bilayer. Typical processes that include intramembrane proteolysis is the regulatory or signalling function of cleavage products. Likewise, signal peptide fragments liberated upon intramembrane cleavage may promote such post-targeting functions in the cell.. ...
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Novel Aspartic Proteinase of the PepSIN Family (Napsin A, or NAPSA) belongs to the peptidase A1 family and plays a role in pneumocyte surfactant processing. It is also known as aspartyl protease 4 (ASP4), KAP, Kdap, napsin-1, NAP1, NAPA, and SNAPA. Two closely related proteins are known, Napsin A and Napsin B. Napsin A is a single-chain, 38-kDa protein. It is expressed at high levels in human lung and kidney, and at lower levels in spleen. Napsin A expression has been detected in type II pneumocytes and in lung adenocarcinomas.. ...
www.MOLUNA.de Aspartic Proteinases [4193983] - The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32
X-converting enzyme (XCE) involved in nervous control of respiration, is a member of the M13 family of zinc peptidases, for which no natural substrate has been identified yet. In contrast, its well characterized homologue endothelin-converting enzyme-1 (ECE-1) showed broad substrate specificity and acts as endopeptidase as well as dipeptidase. To explore the structural differences between XCE and ECE-1, homology model of XCE was built using the complex structure of ECE-1 with phosphoramidon (pdb-id: 3DWB) as template. Phosphoramidon was docked into the binding site of XCE whereas phosphate oxygen of the inhibitor was used as water molecule to design the apo forms of both enzymes. Molecular dynamics simulation of both enzymes was performed to analyze the dynamic nature of their active site residues in the absence and presence of the inhibitor. Homology model of XCE explained the role of non-conserved residues of its S2 subsite. Molecular dynamics (MD) simulations identified the flexible transitions of
Integral membrane proteins (ECEs) that are zinc-binding metallopeptidases of the same family as neprilysin with a role in processing various neuropeptides. ECE-1 (EC, 770 aa) converts big endothelin-1 (ET-1) to active ET-1 and is important in regulating blood pressure. Isoforms of endothelin-converting enzyme-1 (ECE-1a-d) are present in early endosomes, where they degrade various neuropeptides and regulate postendocytic sorting of receptors. Defects in the ECE-1 gene are associated with Hirschsprungs disease. ECE-2 (883 aa) has been implicated in Alzheimers disease and knockout mice show deficiencies in learning and memory. ...
Beta Secretase Substrate Functional Assay Kits datasheet (ab101160). Abcam offers quality products including antibodies, assays and other reagents.
Hypertension is largely attributed to abnormal renal sodium handling; however, a growing body of evidence now suggests that primary abnormalities in vessels can also cause aberrations in blood pressure. Very often, the source of the abnormality resides in the endothelial cells that regulate the functional state of the entire vessel, and this knowledge has directed our search for new diagnostic and therapeutic targets. To date, the role of transcriptional mechanisms in blood pressure regulation is poorly characterized. In this study, we found that E2F2, a transcription factor involved in cell-cycle control, regulates blood pressure by modulating vessel contractility. This previously unknown function of E2F2 evolves from the unique role of the molecule in endothelial cells: suppression of endothelin-converting enzyme 1 (ECE-1). ECE-1 converts the inactive precursor molecule big endothelin-1 into the potent vasoconstrictor endothelin-1, and genetic deletion of E2F2 in mice was associated with both ...
Hansson CA, Frykman S, Farmery MR, Tjernberg LO, Nilsberth C, Pursglove SE, Ito A, Winblad B, Cowburn RF, Thyberg J, Ankarcrona M. Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria ...
Regulated intramembrane proteolysis is certainly a central mobile practice included in sign membrane layer and transduction proteins turnover. condition of MHCII-containing endosomes, highlighting SPPL2a as a possible medicinal focus on for using up and/or modulating T cells. The concept of intramembrane proteases (I-CLIPs) cleaving within the phospholipid bilayer was originally place forwards structured on digesting of the sterol regulatory elementCbinding proteins (SREBP; Goldstein and Brown, 1997; Kopan and Wolfe, 2004). Generally, I-CLIPs operate as component of a proteolytic series known to as governed intramembrane proteolysis (Split; Lichtenthaler et al., 2011). Intracellular websites (ICDs) of many Split substrates function as signaling elements after their proteolytic discharge as exemplified by the Level path (De Strooper et al., 1999; Freeman and Urban, 2002). Structured on their catalytic middle, serine, metallo, or aspartyl I-CLIPs (Wolfe, 2009) can end up being differentiated. The ...
Kuruppu, Sanjaya, Rajapakse, Niwanthi W. and Smith, A. Ian (2013). Endothelin-converting enzyme-1 inhibition and renoprotection in end-stage renal disease. Pflugers Archiv - European Journal of Physiology, 465 (7), 929-934. doi: 10.1007/s00424-013-1216-1 ...
Long-time readers will recall that the Klebe group assembled a library of 361 fragments, some of which violated strict rule of 3 guidelines. These were screened in a high-concentration functional assay against the model aspartic protease endothiapepsin, resulting in 55 hits, of which 11 provided crystal structures. The authors wondered how other techniques would fare. In the new paper, they retested their entire library against the same protein using a reporter displacement assay (RDA), STD-NMR, a thermal shift assay (TSA), native electrospray mass spectrometry (ESI-MS), and microscale electrophoresis (MST). To the extent possible they tried to use similar conditions (such as pH) for the different assays, though the fragment concentrations ranged from a low of 0.1 mM (for ESI-MS) to a high of 2.5 mM (for TSA), while protein concentrations ranged between 4 nM (for the biochemical assay) to 20 µM (for ESI-MS ...
Related Articles. Structure-Based Design of Inhibitors of the Aspartic Protease Endothiapepsin by Exploiting Dynamic Combinatorial Chemistry.. Angew Chem Int Ed Engl. 2014 Feb 14 ...
The study and understanding of Alzheimers disease on protein level is fundamentally important in the search for its treatment and there is a demand for proteins that can be used together with candidate drugs in crystallography trials. The refolding time reaching up to three weeks for beta-site APP cleaving enzyme 1 (BACE1), the proposed disease-generating protein, is presently not optimal and new protein constructs are needed. In attempts to shorten the refolding time the six cysteins in BACE1 were substituted to hydrophobic valine or alanine residues. The proteins, both wild type and mutant BACE1, were expressed in Escherichia coli, refolded for one week and purified by ion exchange chromatography and gel filtration. The final products were characterised by measuring stability, homogeneity and enzyme activity. There was significantly lower protein yield for the mutants compared to the wild type BACE1, indicating that generation of the disulphide bonds are important for correctly folded and ...
The neurons of the sympathetic nervous system have distinct properties that allow them to regulate a particular end organ. Various models have been proposed to explain how such precise wiring of neurons to their synaptic targets might come about during development. The neurons might grow in a relatively random manner and then adopt appropriate characteristics after interacting with their target tissue, or there might be molecular markers that guide particular neurons to the right target. Makita et al. provide new evidence in favor of the latter scheme for a set of neurons of the superior cervical ganglia (SCG) that follow along the external carotid artery to reach their salivary gland targets. The authors examined mRNA from external carotid artery in microarray analysis to search for expression of transcripts that might encode guidance molecules. They found specific expression of mRNA encoding endothelin-converting enzyme (which converts precursors of endothelin into the active form). ...
This entry represents the N-terminal domain of the aspartic peptidases. Aspartic peptidase, also known as aspartyl proteases ([intenz:3.4.23.-]) are a widely distributed family of proteolytic enzymes [ (PUBMED:6795036) (PUBMED:2194475) (PUBMED:1851433) ] known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses. Aspartate proteases of eukaryotes are monomeric enzymes which consist of two domains. Each domain contains an active site centred on a catalytic aspartyl residue. The two domains most probably evolved from the duplication of an ancestral gene encoding a primordial domain. Currently known eukaryotic aspartyl proteases are: ...
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The most important allergen associated with IgE responses, Bla g 2, belongs to a subgroup of the aspartic proteinase family of enzymes that is enzymatically inactive (Arruda et al. 2001; Pomes et al. 2002 ...
Rabbit polyclonal antibody raised against synthetic peptide of BACE1. A synthetic peptide corresponding to C-terminus of human BACE1. (PAB9981) - Products - Abnova
Hong, L., Turner, R.T., Koelsch, G., Shin, D., Ghosh, A.K. and Tang, J. (2002). „Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3. Biochemistry. 41: 10963-10967. PMID 12206667 ...
Liu et al. describe a previously unrecognized cellular complex (∼5 MD) containing β- and γ-secretases that generates a full array of Aβ peptides with physiological Aβ42/40 ratios by sequential cleavages of holo-APP. Such coordinated substrate processing also occurs with the α- and γ-secretases in the RIP mechanism.. ...
Supplementary MaterialsFigure S1: Kinetic parameter distribution of SNs before evolution. pone.0050905.s003.tif (81K) GUID:?270C2747-8D2C-40C2-A1ED-52BFDFB4C35A Abstract Transmission transduction is the process of routing information inside cells when receiving stimuli from their environment that modulate the behavior and function. In such natural procedures, the receptors, after getting the corresponding indicators, switch on several biomolecules which transduce the sign […]. ...
Supplementary MaterialsVideo 1 Time-lapse imaging cells expressing both mt-roGFP and Smac mCherry treated with cisplatin stably. with an indicated medication with 10?nm of TMRM. Live cell imaging was TMP 269 biological activity completed as defined. mmc6.mp4 (20M) GUID:?20E6FE9E-0743-40DF-9A25-5E8A9CEF2F51 TMP 269 biological activity Video 7 EGCG: U2Operating-system cells stably expressing mt-roGFP were stained with TMRM to […]. ...
View Notes - ece302hw8 from ECE ECE 302 at Cal Poly Pomona. 3:32 we g (a) Find H in rectangular components at P(2, 3, 4) if there is a current filament on the z axis carrying 8rnA in the aZ
Buy our BACE2 peptide. Ab5869 is a blocking peptide and has been validated in BL. Abcam provides free protocols, tips and expert support for WB and a 12 month…
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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 ...
... (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 ...
Candida albicans secretory acid proteinase, Candida olea acid proteinase, Candida aspartic proteinase, Candida olea aspartic ... Activates trypsinogen, and degrades keratin This endopeptidase js 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, ...
"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) Biology portal. ... Johnson JE, Schneemann A (1998). "Nodavirus endopeptidase". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... The MEROPS online database for peptidases and their inhibitors: Aspartic Peptidases. *Aspartic+Endopeptidases at the US ... Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised.[1] More recently, ... Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The animal ...
... 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 ...
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 ...
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 acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... Proteasome endopeptidase complex (EC, ingensin, macropain, multicatalytic endopeptidase complex, prosome, ... Proteasome+endopeptidase+complex at the US National Library of Medicine Medical Subject Headings (MeSH) ... Retrieved from "https://en.wikipedia.org/w/index.php?title=Proteasome_endopeptidase_complex&oldid=826116286" ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... serine-type endopeptidase activity. Cellular component. • lamellipodium membrane. • extracellular exosome. • lysosomal membrane ... 1x70: HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH A BETA AMINO ACID INHIBITOR ... 2oph: Human dipeptidyl peptidase IV in complex with an alpha amino acid inhibitor ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... aspartic acid, metallo- and acid proteases) nucleophilic so that it can attack the peptide carboxyl group. One way to make a ... aspartic, and metallo proteases.[2] The threonine and glutamic-acid proteases were not described until 1995 and 2004 ... depending on the amino acid sequence of a protein, or completely break down a peptide to amino acids (unlimited proteolysis). ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... 1990). "Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... aspartic-type endopeptidase activity. Cellular component. • multivesicular body. • late endosome. • endoplasmic reticulum lumen ... BACE1 is an aspartic-acid protease important in the formation of myelin sheaths in peripheral nerve cells: in mice the ... BACE1 is distantly related to the pathogenic aspartic-acid protease plasmepsin, which is a potential target for future anti- ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ...
... 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 ...
Aspartic Acid -OOC-CH2- Oxaloacetate → Aspartic Acid (aminotransferase) Glutamic Acid -OOC-(CH2)2- α-ketoglutarate → Glutamic ... EndopeptidasesEdit. Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that ... Amino Acid SynthesisEdit. Pathways that form each amino acid[4]. Amino Acid R-group‡ Pathway* ... The main amino acids involved are serine, histidine, and aspartic acid. They all play a role in cleaving the peptide bond. ...
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 gene with homologies to endopeptidases on the X chromosome) is one such enzyme, which extensively ... 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 Res ...
... aspartic acid, metallo- and acid proteases) nucleophilic so that it can attack the peptide carboxyl 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 ...
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 ...
Ste24 endopeptidase EC S2P endopeptidase EC ADAM 17 endopeptidase EC ADAMTS13 endopeptidase EC ... Lotus aspartic proteinase EC Deleted entry: sorghum aspartic proteinase EC renin EC HIV-1 ... Rhizopus acid proteinase. Now EC, rhizopuspepsin EC Endothia acid proteinase. Now EC, ... ADAM10 endopeptidase EC ADAMTS-4 endopeptidase EC anthrax lethal factor endopeptidase EC ...
"Acid and non-acid reflux in patients with persistent symptoms despite acid suppressive therapy: a multicentre study using ... Pepsin is an aspartic protease, using a catalytic aspartate in its active site. It is one of three principal proteases in the ... Pepsin is an endopeptidase that breaks down proteins into smaller peptides. It is produced in the gastric chief cells of the ... Weak or non-acid reflux is correlated with reflux symptoms and mucosal injury. Under non-acid conditions (neutral pH), pepsin ...
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". J. Biochem. 95 (2): 465-473. doi:10.1093/ ...
... aspartic acid, metallo- and acid proteases) nucleophilic so that it can attack the peptide carboxyl group. One way to make a ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). ... aspartic, and metallo proteases.[5] The threonine and glutamic-acid proteases were not described until 1995 and 2004 ... depending on the amino acid sequence of a protein, or completely break down a peptide to amino acids (unlimited proteolysis). ...
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 ...
"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., ...
Amino acid-derived. *Major excitatory/inhibitory systems: Glutamate system: Agmatine. *Aspartic acid (aspartate) ... role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119-25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950.. ... response to retinoic acid. • positive regulation of renal sodium excretion. • regulation of receptor activity. • G-protein ... Hornig D (September 1975). "Distribution of ascorbic acid, metabolites and analogues in man and animals". Annals of the New ...
serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and ... Similar to other aspartic protainases, cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active ... "Nucleic Acids Research. 15 (9): 3773-86. doi:10.1093/nar/15.9.3773. PMC 340781 . PMID 3588310.. ...
The CASP8 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases ... cysteine-type endopeptidase activity involved in execution phase of apoptosis. Cellular component. • cell body. • cytosol. • ... cysteine-type endopeptidase activity. • hydrolase activity. • ubiquitin protein ligase binding. • peptidase activity. • ... cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • protein complex binding. • scaffold protein ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The thioester bond is subsequently hydrolyzed to generate a carboxylic acid moiety on the remaining substrate fragment, while ... and the aspartic protease precursor pepsinogen. The protease is activated by removal of an inhibitory segment or protein. ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and nucleic acids.[9] ...
Acid/base catalysisEdit. In some reactions, protons and hydroxide may directly act as acid and base in term of specific acid ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide.[1] ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... The active site usually contains non-polar amino acids, although sometimes polar amino acids may also occur.[2] The binding of ...
Amino acid-derived. *Major excitatory/inhibitory systems: Glutamate system: Agmatine. *Aspartic acid (aspartate) ... cysteine-type endopeptidase inhibitor activity involved in apoptotic process. • neurohypophyseal hormone activity. • receptor ... the value in the table above of 164 amino acids is that obtained before the hormone is activated by cleavage.) The amino acid ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • regulation of blood vessel size. • ...
... one histidine residue and one aspartic acid residue) and two from carbonate or bicarbonate ions. ... serine-type endopeptidase activity. • hydrolase activity. • lipopolysaccharide binding. • cysteine-type endopeptidase inhibitor ... Interaction with nucleic acidsEdit. One of the important properties of lactoferrin is its ability to bind with nucleic acids. ... There are differences in amino acid sequences: 8 in Homo sapiens, 6 in Mus musculus, 6 in Capra hircus, 10 in Bos taurus and 20 ...
Energy-dependent acid transport was verified and the postulated proton pump purified.[13][14] 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 ...
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". ...
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 ...
... 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/ ...
But more often groups in substrate and active site act as Brønsted-Lowry acid and base. This is called general acid and general ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. It ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... In some reactions, protons and hydroxide may directly act as acid and base in term of specific acid and specific base catalysis ...
Polyclonal Antibody Flow Cytometry Amino Acid Transport, Polyclonal Antibody Flow Cytometry Adherens Junction Dynamics ... Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity, Polyclonal Antibody Flow Cytometry Apoptosis, ... Category listing: Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity to Polyclonal Antibody Fatty Acid ... Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity Polyclonal Antibody Flow Cytometry Aspartic-Type ...
Find out information about Aspartic endopeptidases. organic compound, one of the 20 amino acids amino acid , any one of a class ... of simple organic compounds containing carbon, hydrogen, oxygen, nitrogen, and... Explanation of Aspartic endopeptidases ... aspartic acid. (redirected from Aspartic endopeptidases). Also found in: Dictionary, Thesaurus, Medical. aspartic acid. (əspär` ... Aspartic acid is not essential to the human diet. It was discovered in protein in 1868.. aspartic acid. [ə′spärd·ik ′as·əd] ( ...
Aspartic Acid Endopeptidases/genetics. *Aspartic Acid Endopeptidases/metabolism. *Aspartic Acid Endopeptidases/physiology* ... The secreted aspartic proteinase of C. albicans was first described in 1965 and has proved to be a major factor in virulence. ... The role of Candida albicans secreted aspartic proteinase in the development of candidoses.. Hoegl L1, Ollert M, Korting HC. ... This enzyme belongs to the class of aspartic proteinases which includes pepsin and renin in humans. Although found in some ...
Aspartic Acid Endopeptidases * Brain / metabolism * CCAAT-Enhancer-Binding Proteins* * Cells, Cultured * Cytoplasm / metabolism ...
... polyunsaturated fatty acid (PUFA) docosahexaenoic acid (DHA) is associated with reduced risk of Alzheimers disease (AD). DHA ... Aspartic Acid Endopeptidases * Blotting, Western / methods * Central Nervous System / drug effects * Central Nervous System / ... A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model J ... Image analysis of brain sections with an antibody against Abeta (amino acids 1-13) revealed that overall plaque burden was ...
Aspartic Acid Endopeptidases / drug effects, metabolism, secretion. Candida albicans / drug effects*. Clusiaceae*. Magnetic ... Aspartic Acid Endopeptidases; EC A ... 15247137 - Effect of folic acid supplementation on the folate ... 4-dihydroxybenzoic acid (14). Compounds 2, 3, 12 and 13 showed inhibitory effects against Candida albicans secreted aspartic ... 17830317 - Abscisic acid induces formation of floating leaves in the heterophyllous aquatic angios.... 20183257 - Two new ...
Aspartic Acid Endopeptidases); EC (BACE1 protein, human). ... cido Asp rtico Endopeptidases/antagonistas & inibidores. xidos S-C clicos. Tiadiazinas. [Mh] Termos MeSH secund rio:. Doen a de ...
Aspartic Acid Proteases [D08.811.277.656.074]. *Aspartic Acid Endopeptidases [D08.811.277.656.074.500] ... Endopeptidases [D08.811.277.656.300]. *Aspartic Acid Endopeptidases [D08.811.277.656.300.048]. *Cathepsin D [D08.811.277.656. ...
... serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in ... Endopeptidase 3.4.21-24. Serine proteases - Cysteine protease - Aspartic acid protease - Metalloendopeptidases. ... and aspartic acid (Asp 102). Located very near one another near the heart of the enzyme, these three key amino acids each play ... Instead of having the hydrophobic pocket of the chymotrypsin, there exists an aspartic acid residue at the base of the pocket. ...
Endopeptidase 3.4.21-24. Serine proteases - Cysteine protease - Aspartic acid protease - Metalloendopeptidases. ...
In particular, serine endopeptidases, cysteine endopeptidases, aspartic acid endopeptidases and/or metalloendopeptidases may be ... The amino acid sequence and/or the amino acid sequence that is at least 80% homologous with it, preferably at least 90%, refers ... This amino acid sequence may also include other amino acids of the hinge-loop region, as explained above. ... In a preferred embodiment, the amino acid sequences ID No. 1 or ID No. 2 or amino acid sequences that are at least 80% ...
Aspartic Acid Endopeptidases. *Axin Protein. *Cyclin D1. *Cytosol. *Endopeptidases/metabolism. *Fibroblasts/cytology ...
Aspartic Acid Endopeptidases. Papers overview. Semantic Scholar uses AI to extract papers important to this topic. ... The cDNA encoding the precursor of an aspartic proteinase from the flowers of the cardoon, Cynara cardunculus, was expressed in ... Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its ... Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. ...
MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR ... are a family of zinc endopeptidases, which have been implicated ... MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR. *DOI: 10.2210/pdb1A86/pdb ... Among the hydroxamic acids, malonic acid derivatives have been used as MMP inhibitors, although optimization of their ... Various classes of MMP inhibitors, including hydroxamic acids, phosphinic acids, and thiols, have been previously described ... ...
Aspartic endopeptidases / viral capsid / nucleic acid binding / aspartic-type endopeptidase activity / zinc ion binding ... Aspartic peptidase, active site / Retroviral nucleocapsid protein Gag, p24 fragment / Retrovirus capsid, N-terminal / ... Aspartic peptidase, active site / Retroviral nucleocapsid protein Gag, p24 fragment / Retrovirus capsid, N-terminal / ... Buffer solution: 0.1M citric acid, 5mM MOPS/KOH, 725mM NaCl, 0.25mM Na azide, 0.125mM TCEP-HCl. pH: 5 Support film. Holey ...
secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, inclu ... Nepenthes aspartic proteinase; Nepenthes acid proteinase; nepenthacin; nepenthasin; aspartyl endopeptidase. Reaction. Similar ... secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, ...
"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) Biology portal. ... 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 ...
Aspartic Acid Endopeptidases/metabolism. *Biological Transport. *Carrier Proteins/genetics/metabolism. *Cell Membrane/ ...
Aspartic acid proteases, commonly known as acidic proteases, are the endopeptidases that depend on aspartic acid residues for ... Acid protease. Wheat bran. (Merheb-Dini et al., 2010). Thermomyces lanuginosus. SmF. 6.0. 50 °C. 0.71. -. Glucose, citric acid ... Acid protease. Czapek-Dox, peptone. (Larsen et al., 1998). Phanerochaete chrysosporium. SSF. 4.5. 25 °C. 35. Acid and ... based on the nature of the amino acid residues at the active site of the enzymes. Endopeptidases are characterized by their ...
... usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. In only one family of cysteine peptidases ... Structural basis of murein peptide specificity of a gamma-D-glutamyl-l-diamino acid endopeptidase.. Structure 17 303-13 2009 ... Endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme contains two major domains: a bacterial SH3-like ... They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N-ethylmaleimide or p-chloromercuribenzoate. ...
Other names: Rhizopus aspartic proteinase; neurase; Rhizopus acid protease; Rhizopus acid proteinase. Comments: From the ... A similar endopeptidase is found in R. niveus [2]. In peptidase family A1 (pepsin A family). Formerly EC, and included ... Substrate specificity of acid protease of Rhizopus chinensis. Agric. Biol. Chem. 33 (1969) 1419-1426. 2. Kurono, Y., Chidimatsu ... 4. Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. Binding of a reduced peptide inhibitor to the aspartic ...
DNA binding, RNA binding, RNA-directed DNA polymerase activity, aspartic-type endopeptidase activity, nucleic acid binding, ... crystallization of nucleic acid complexes. Protein Sci, 7:1575-82 [Medline info for 9684890] ... structures of an N-terminal fragment from Moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: ...
Aspartic Acid Endopeptidases, cerebrospinal fluid, Female, Humans, Lupus Erythematosus, Systemic, metabolism, Male, Middle Aged ...
Aspartic Acid Endopeptidases. 1. + +. 252. Receptors, Endothelin. 1. + +. 253. Calcitonin Gene-Related Peptide. 1. + +. ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid. 1. + +. ...
Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests ... Adrenal medulla; Adrenal Medulla/enzymology; Amino acid sequence; Animals; Aspartic acid; Aspartic Acid Endopeptidases/ ... Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests ... Endopeptidases; Enkephalins; Enkephalins/metabolism; Enzymology; Furin; Humans; Men; Models; Biological; Molecular Sequence ...
Endopeptidases; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC / BACE1 protein, human; EC / Bace1 protein, ... Aspartic Acid Endopeptidases. Bile Ducts / cytology. Cell Line, Transformed. Cholangitis, Sclerosing / metabolism. Cholangitis ... Nucleic Acid, Nucleoside, or Nucleotide. A1. Organophosphorus Compound. A1. Amino Acid, Peptide, or Protein ... A2. Amino Acid Sequence. A2. Carbohydrate Sequence. A2.1.5.4. Geographic Area. A2.2. Finding. A2.2.1. ...
Keywords: Aspartic Acid Endopeptidases - genetics, Amyloid beta-Peptides - metabolism, Amyloid Precursor Protein Secretases, ... Alzheimer Disease - prevention & control, Cell Line, Tumor, Endopeptidases - genetics, Gene Expression Regulation, Enzymologic ...
... allowing for cleavage N-terminal to proline and between aspartic acid and proline (18). Carbamidomethylcysteine was set as a ... Achromobacter lyticus lysyl endopeptidase, and human keratins; a total of 52,355 forward entries) and concatenated with ... For the SILAC technology, cells are grown in the presence of light or heavy forms of amino acids, such as arginine and lysine. ... Rogers, M. B., Hosler, B. A., and Gudas, L. J. (1991) Specific expression of a retinoic acid-regulated, zinc-finger gene, Rex-1 ...
Primarily on the N-terminal side of aspartic acid residues. Cleavage on the N-terminal side of glutamic acid residues can occur ... Arg-C, Sequencing Grade (Cat.# V1881), also known as clostripain, is an endopeptidase that cleaves at the C-terminus of ... In phosphate buffers, cleavage also occurs at aspartic acid residues. Glu-C activity is optimal at pH 4.0-9.0. ... is an endoproteinase that hydrolyzes peptide bonds at the N-terminal side of aspartic acid residues. Asp-N activity is optimal ...
  • Natural products inhibiting Candida albicans secreted aspartic proteases from Tovomita krukovii. (biomedsearch.com)
  • Compounds 2, 3, 12 and 13 showed inhibitory effects against Candida albicans secreted aspartic proteases (SAP) with IC50 values of 15 microg/ml, 25 microg/ml, 40 microg/ml, and 6.5 microg/ml, respectively, while the other compounds were inactive. (biomedsearch.com)
  • In biochemistry , serine proteases or serine endopeptidases (newer name) are a class of peptidases ( enzymes that cleave peptide bonds in proteins ) that are characterised by the presence of a serine residue in the active site of the enzyme . (bionity.com)
  • Located very near one another near the heart of the enzyme, these three key amino acids each play an essential role in the cleaving ability of the proteases. (bionity.com)
  • Proteases hydrolyze the peptide bonds of proteins into peptides and amino acids, being found in all living organisms, and are essential for cell growth and differentiation. (scielo.br)
  • Proteases are classified as peptide hydrolases or peptidases (EC 3.4) and constitute a large family of enzymes, divided into endopeptidases (EC 3.4.21-99) and exopeptidases (EC 3.4.11-19), classified according to the position of the peptide bond to be cleaved. (scielo.br)
  • Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. (wikipedia.org)
  • Eukaryotic aspartic proteases include pepsins , cathepsins , and renins . (wikipedia.org)
  • While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid-base mechanism involving coordination of a water molecule between the two highly conserved aspartate residues. (wikipedia.org)
  • Five superfamilies (clans) of aspartic proteases are known, each representing an independent evolution of the same active site and mechanisms . (wikipedia.org)
  • Therefore, PepA-P can be used in studying the role of intracellular aspartic proteases in the MHC class II antigen processing pathway. (edu.kz)
  • Positive and negative contributions have been described for other enzymes, including the aspartyl proteases cathepsins D and E and asparagine endopeptidase (AEP). (jimmunol.org)
  • Evolutionarily conserved functional mechanics across pepsin-like and retroviral aspartic proteases. (ebi.ac.uk)
  • The threonine and glutamic acid proteases were not described until 1995 and 2004 , respectively. (wikidoc.org)
  • Proteases are involved in digesting long protein chains into short fragments, splitting the peptide bonds that link amino acid residues. (wikidoc.org)
  • Proteases are divided into four major groups according to the character of their catalytic active site and conditions of action: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases, and metalloproteinases . (wikidoc.org)
  • One of the strategies used by pathogens to succeed in causing infection is the production of proteases, which are enzymes that cleave peptide bonds between the amino acids in a protein. (bvsalud.org)
  • The two main groups of proteases are exopeptidases and endopeptidases. (pediaa.com)
  • histidine (His 57), serine (Ser 195) (hence the name "serine protease") and aspartic acid (Asp 102). (bionity.com)
  • Structure of the dimeric aspartic protease HIV protease in white and grey, with peptide substrate in black and active site aspartate side chains in red. (wikipedia.org)
  • However, the aspartic protease inhibitors, including the highly potent pepstatin A (PepA), are inefficiently transported across the cell membrane and thus have limited access to antigen processing compartments. (edu.kz)
  • The aim of the present study was to synthesize new cell-permeable aspartic protease inhibitors by conjugating pepstatin A with well-known cell penetrating peptides (CPPs). (edu.kz)
  • We found that the bioconjugate PepA-penetratin (PepA-P) was the most efficient cell-permeable aspartic protease inhibitor tested, and was more efficient than unconjugated PepA. (edu.kz)
  • Fingerprint Dive into the research topics of 'A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin A'. Together they form a unique fingerprint. (edu.kz)
  • An Arabidopsis aspartic protease functions as an anti-cell-death component in reproduction and embryogenesis. (ebi.ac.uk)
  • N-terminal amino acid sequencing of the fragment indicated that the protease cleaves LAPP at the Abeta-N-terminus. (arctichealth.org)
  • A protease is any enzyme that conducts proteolysis , that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain. (wikidoc.org)
  • Attachment of a protease to a certain group depends on the structure of catalytic site and the amino acid (as one of the constituents) essential for its activity. (wikidoc.org)
  • The protease functions in the lysosome to cleave N-terminal tripeptides from substrates and has weaker endopeptidase activity. (wikidoc.org)
  • This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. (genecards.org)
  • HLA-E presents closely related nonameric peptide epitopes derived from the highly conserved signal sequences of classical major histocompatibility complex class I molecules as well as HLA-G. Their generation requires cleavage of the signal sequence by signal peptidase followed by the intramembrane-cleaving aspartic protease, signal peptide peptidase. (ox.ac.uk)
  • A protease is an enzyme which breaks down proteins into small peptides and eventually into amino acids. (pediaa.com)
  • Furthermore, pepsin is an endopeptidase while a protease can be either endopeptidase or exopeptidase. (pediaa.com)
  • Also, pepsin is an acid protease while a protease can either act in the acidic, neutral or basic medium. (pediaa.com)
  • In pepsin, it is aspartic acid while the active site residue of a protease can be either serine, cysteine, threonine, aspartic acid, glutamic acid, asparagine or a metal group. (pediaa.com)
  • Another difference between pepsin and protease is that pepsin breaks down proteins into small peptides while a protease may break down a protein either into small peptides or amino acids. (pediaa.com)
  • This enzyme belongs to the class of aspartic proteinases which includes pepsin and renin in humans. (nih.gov)
  • Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. (semanticscholar.org)
  • Aspartic proteinases from human immunodeficiency virus type 1 (HIV-1) and avian myeloblastosis virus (AMV) were found to interfere with microtubule assembly. (nih.gov)
  • Moreover, inhibition of tetanus toxoid C-fragment processing by PepA-P clearly implicates the role of aspartic proteinases in antigen processing. (edu.kz)
  • The structure and function of the aspartic proteinases. (ebi.ac.uk)
  • Rao JK, Erickson JW, Wlodawer A. Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases. (ebi.ac.uk)
  • Revuelta MV, van Kan JA, Kay J, Ten Have A. Extensive expansion of A1 family aspartic proteinases in fungi revealed by evolutionary analyses of 107 complete eukaryotic proteomes. (ebi.ac.uk)
  • Lysosomal proteinases or endopeptidases that function optimally at an acidic pH to catalyze the hydrolysis of peptidic bonds. (semanticscholar.org)
  • Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. (wikipedia.org)
  • The role of Candida albicans secreted aspartic proteinase in the development of candidoses. (nih.gov)
  • The secreted aspartic proteinase of C. albicans was first described in 1965 and has proved to be a major factor in virulence. (nih.gov)
  • Although found in some fungi, secreted aspartic proteinase is rare in these organisms. (nih.gov)
  • While the existence of several isoenzymes may not be fully established, it is now obvious that at least seven different genes encode for secreted aspartic proteinase. (nih.gov)
  • In future secreted aspartic proteinase may prove a prime target for new types of antimycotics. (nih.gov)
  • Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon (Cynara cardunculus). (semanticscholar.org)
  • Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests that investigation of inhibitors of peripheral PTP in blood pressure regulation should be initiated. (unlv.edu)
  • Characterization of recombinant CDR1, an Arabidopsis aspartic proteinase involved in disease resistance. (ebi.ac.uk)
  • This proteinase was shown to possess a strong preference for cleavage after glutamic acid residues, but not after aspartic acid. (blogspot.in)
  • In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. (ebi.ac.uk)
  • Peptidases are proteolytic enzymes that can be subdivided into endopeptidases and exopeptidases [ 18 ]. (biomedcentral.com)
  • Serine peptidases are a class of endopeptidases that are characterized by the presence of three invariant residues at the active site: serine, aspartic acid and histidine [ 19 , 20 ]. (biomedcentral.com)
  • The presence and position of disulfide bridges are other conserved features of aspartic peptidases. (wikipedia.org)
  • The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine (peptidases) or a water molecule (aspartic acid, metallo- and glutamic acid peptidases) nucleophilic so that it can attack the peptide carbonyl group. (wikidoc.org)
  • Peptidases can either break specific peptide bonds ( limited proteolysis ), depending on the amino acid sequence of a protein, or break down a complete peptide to amino acids ( unlimited proteolysis ). (wikidoc.org)
  • Sedolisins are acid-acting endopeptidases or tripeptidyl peptidases. (expasy.org)
  • Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastrointestinal tract. (wikipedia.org)
  • Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. (wikipedia.org)
  • Protein anabolism is the process by which proteins are formed from amino acids. (wikipedia.org)
  • Proteins are made from amino acids. (wikipedia.org)
  • Proteins containing this domain belong to the aspartic peptidase A1 family (peptidase family A1, subfamily A1B). (ebi.ac.uk)
  • Enzyme that cleaves amino acid residues from a protein chain commencing at the N-terminal Antibodies: Proteins involved in recognising bacteria, viruses, toxins, etc. as part of the immune defence system. (docplayer.net)
  • Background Folding nucleus of globular proteins formation starts by the mutual interaction of a group of hydrophobic amino acids whose close contacts allow subsequent formation and stability of the 3D structure. (capecodmushroom.org)
  • They hydrolyze peptide bonds between amino acids in both proteins and peptides. (pediaa.com)
  • Cleavage of peptide bonds lead to degradation of protein substrates into their constituent amino acids, or it can be specific, leading to selective protein cleavage for post-translational modification and processing. (scielo.br)
  • The Yps3 protein of strain G217B is 137 amino acids in length and is characterized principally by an N-terminal secretion signal sequence and a C-terminal epidermal growth factor-like domain ( 3 ). (asm.org)
  • Five point mutations within the amyloid beta-protein (Abeta) sequence of the APP gene are associated with hereditary diseases which are similar or identical to Alzheimer's disease and encode: the A21G (Flemish), E22G (Arctic), E22K (Italian), E22Q (Dutch) and the D23N (Iowa) amino acid substitutions. (arctichealth.org)
  • Amino acid: Monomer containing an amino group and a carboxyl group that is polymerised to form peptide and protein chains. (docplayer.net)
  • Typically, peptide/protein-forming amino acids have the amino and carboxyl groups attached to the same carbon atom (the alpha carbon) and are designated alpha amino acids. (docplayer.net)
  • Automated machine that determines amino acid composition of a protein. (docplayer.net)
  • Amino acid sequencer: Automated machine that determines linear order of amino acids in protein chain (i.e. the protein s primary structure). (docplayer.net)
  • Carboxypeptidase: Enzyme that cleaves amino acids from a protein chain commencing at the C-terminal Chromatography: General term for related techniques to purify the components of peptide/protein mixtures according to molecular size, polarity, charge, recognition properties, etc. (docplayer.net)
  • GO annotations related to this gene include cysteine-type endopeptidase activity and scaffold protein binding . (genecards.org)
  • If the actual local density of hydrophobicity TAK-715 around a given amino acid is as high as the ideal one, then this amino acid is assigned to the core of the globular protein, and it is assumed to follow the FOD model. (capecodmushroom.org)
  • Under conditions of induction for this protein and cefoxitin treatment, the reduction in M5 is not fully efficient, implying that LMM-PBP4 of Pseudomonas aeruginosa presents better behaviour as a D,D-endopeptidase. (biomedcentral.com)
  • These amino acid residues form much of the connective tissues in meat). (bionity.com)
  • The pocket that is in "trypsin" and "chymotrypsin" is now partially filled with valine and threonine , rendering it a mere depression, which can accommodate these smaller amino acid residues. (bionity.com)
  • The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long. (wikipedia.org)
  • Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. (genecards.org)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (ebi.ac.uk)
  • Asparagine endopeptidase (AEP) or legumain is a potentially important Ag-processing enzyme that introduces limited cleavages that trigger unfolding and class II MHC binding of different Ag substrates. (jimmunol.org)
  • Amino acid CV, % Alanine 5.0 Arginine 6.8 Asparagine 8.6 Aspartic acid 7.4 Citrulline 8.8 Cystine 8.1 Glutamic acid 8.8 Glutamine 4.1 Glycine 5.2 Histidine 6.6 Isoleucine 9.0 Leucine 5.0 Lysine 4.0 Methionine 5.5 Ornithine 4.0 Phenylalanine 9.2 Proline 12.1 Serine 4.8 Taurine 7.3 Threonine 4.5 Tryptophan 9.8 Tyrosine 5.9 Valine 8.8 Table 3. (thefreedictionary.com)
  • Chymotrypsin is responsible for cleaving peptide bonds following a bulky hydrophobic amino acid residue. (bionity.com)
  • Trypsin is responsible for cleaving peptide bonds following a positively-charged amino acid residue. (bionity.com)
  • Instead of having the hydrophobic pocket of the chymotrypsin , there exists an aspartic acid residue at the base of the pocket. (bionity.com)
  • Elastase is responsible for cleaving peptide bonds following a small neutral amino acid residue, such as Alanine , glycine and valine. (bionity.com)
  • Aminopeptidases (EC 3.4.14) act at a free N terminus of the polypeptide chain and liberate a single amino acid residue, a dipeptide, or a tripeptide. (scielo.br)
  • Amino acid residue: the portion of the amino acid that remains after incorporation into a polypeptide chain. (docplayer.net)
  • Insulin human is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. (drugbank.ca)
  • Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. (umassmed.edu)
  • The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. (expasy.org)
  • Moreover, the active site residue of pepsin is aspartic acid . (pediaa.com)
  • Exopeptidases breakdown terminal peptide bonds, resulting in peptides and amino acids. (pediaa.com)
  • The proteolytic enzymes are subdivided into two major groups, exopeptidases and endopeptidases, depending on their site of action. (scielo.br)
  • In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. (wikipedia.org)
  • Lombard V. et al "The carbohydrate-active enzymes database (CAZy) in 2013" Nucleic Acids Res. (wellnessadvocate.com)
  • 4 . The process according to claim 1 , wherein the one or more proteolytic enzymes comprise both endopeptidase and exopeptidase activity. (google.ch)
  • Daechon Kamakmen Bay Aspartic acid 16.5 (2.5) 18.5 (2.1) Glutamic acid 28.3 (7.7) 34.2 (6.8) Serine 13.2 (1.5) 10.1 (1.7) Glycine 69.0 (20.6) 42.8 (8.7) [beta]-Alanine 15.9 (3.3) 5.2 (0.1) Taurine 200.7 (48.3) 324.4 (45.1) L-Alanine 37.3 (11.0) 29.7 (7.2) T/G ratio 2.9 7.6 TOTAL 380.8 (91.9) 464.8 (60.6) TABLE 2. (thefreedictionary.com)
  • Equal amount of aspartic acid and glutamic acid by weight were substituted for the graded amounts of methionine in the basal diet to maintain the isonitrogenous of the seven experimental diets. (thefreedictionary.com)
  • Typically aspartic acid, glutamic acid. (docplayer.net)
  • Endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme contains two major domains: a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. (ebi.ac.uk)
  • endopeptidases, when they cleave the internal peptide bonds, which differ from the exopeptidases that cleave the terminal bonds. (bvsalud.org)
  • Especially, pepsin is an endopeptidase that hydrolyzes internal peptide bonds. (pediaa.com)
  • On the other hand, endopeptidases breakdown internal peptide bonds, resulting in small peptides. (pediaa.com)
  • Cloning, expression, and purification of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase: crystallization of nucleic acid complexes. (molmovdb.org)
  • however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. (expasy.org)
  • The second reaction cleaves the aminoacyl-AMP producing the energy to join the amino acid to the tRNA molecule. (wikipedia.org)
  • For example, a nuclease is a hydrolase that cleaves nucleic acids. (wikidoc.org)
  • [5] [6] One aspartate activates the water by abstracting a proton, enabling the water to perform a nucleophilic attack on the carbonyl carbon of the substrate scissile bond , generating a tetrahedral oxyanion intermediate stabilized by hydrogen-bonding with the second aspartic acid. (wikipedia.org)
  • Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides . (wikipedia.org)
  • Pepsin has a three-dimensional structure, of which one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. (wikidoc.org)
  • Furthermore, pepsin is responsible for the hydrolysis of peptide bonds between large hydrophobic amino acids. (pediaa.com)
  • Cathepsin D (CatD, EC is a member belonging to the subfamily of aspartic endopeptidases, which are classified into the MEROPS clan AA, family A1. (bvsalud.org)
  • In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle. (wikipedia.org)
  • In humans, some amino acids can be synthesized using already existing intermediates. (wikipedia.org)
  • The results showed a decrease in the relative quantity of dimeric, trimeric and anhydrous units, and a smaller reduction in monomer disaccharide pentapeptide (M5) levels, validating the occurrence of D,D-carboxypeptidase and D,D-endopeptidase activities. (biomedcentral.com)
  • Nodavirus endopeptidase (EC, Black Beetle virus endopeptidase, Flock House virus endopeptidase) is an enzyme. (wikipedia.org)
  • In enzyme science, Acid Anhydride Hydrolases are a class of hydrolase enzyme reactions that catalyze the hydrolysis of a acid anhydride bond. (wellnessadvocate.com)
  • Matrix metalloproteinases (MMPs) are a family of zinc endopeptidases, which have been implicated in various disease processes. (rcsb.org)
  • They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N -ethylmaleimide or p -chloromercuribenzoate. (ebi.ac.uk)
  • Here we report the design of malonic acid-based inhibitors using the X-ray structure of a collagenase/inhibitor complex, which revealed a nonsubstrate-like binding mode. (rcsb.org)
  • The amino acids are joined by peptide bonds making a polypeptide chain. (wikipedia.org)
  • Acidic amino acids: Those whose side chains can carry a negative charge at certain ph values. (docplayer.net)