Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Adenosine Triphosphatases: A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.Kinetics: The rate dynamics in chemical or physical systems.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Neprilysin: 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.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Thiorphan: A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.PHEX Phosphate Regulating Neutral Endopeptidase: 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.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cysteine Endopeptidases: 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.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Glycopeptides: 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.Neurotensin: 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.Lysostaphin: 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 3.4.24.75.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Dipeptides: Peptides composed of two amino acid units.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Atrial Natriuretic Factor: 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.Oligopeptides: Peptides composed of between two and twelve amino acids.Cells, Cultured: 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.ThiazepinesCell Line: Established cell cultures that have the potential to propagate indefinitely.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Cathepsin B: 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.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Bradykinin: 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.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Substance P: 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.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Enzyme Activation: 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.Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Kidney: Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.Exopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Enkephalin, Leucine: 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.ATP Synthetase Complexes: Multisubunit enzyme complexes that synthesize ADENOSINE TRIPHOSPHATE from energy sources such as ions traveling through channels.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Aminopeptidases: 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.Botulinum Toxins, Type A: A serotype of botulinum toxins that has specificity for cleavage of SYNAPTOSOMAL-ASSOCIATED PROTEIN 25.Indans: Aryl CYCLOPENTANES that are a reduced (protonated) form of INDENES.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Hypophosphatemia: A condition of an abnormally low level of PHOSPHATES in the blood.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Flavobacterium: 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.RNA, Messenger: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Bacterial Proteins: Proteins found in any species of bacterium.Thermolysin: A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.PeptidoglycanEnzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Propionates: Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.Protein Processing, Post-Translational: 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.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.ATP-Dependent Endopeptidases: Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Membrane Proteins: 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.Mice, Inbred C57BLRats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Carboxypeptidases A: 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 3.4.2.1 and EC 3.4.12.2.Protein PrecursorsMice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.Transfection: 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.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Angiotensin-Converting Enzyme Inhibitors: 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.Familial Hypophosphatemic Rickets: 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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Peptidyl-Dipeptidase A: 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 3.4.15.1.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Isoflurophate: A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.Rats, Wistar: A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.Magnesium: A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Leucyl Aminopeptidase: 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.Kinins: 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)Receptors, Purinergic P2: A class of cell surface receptors for PURINES that prefer ATP or ADP over ADENOSINE. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system.Mitochondrial Proton-Translocating ATPases: Proton-translocating ATPases responsible for ADENOSINE TRIPHOSPHATE synthesis in the MITOCHONDRIA. They derive energy from the respiratory chain-driven reactions that develop high concentrations of protons within the intermembranous space of the mitochondria.Cathepsin C: 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.Aminocaproates: 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.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Blotting, Western: 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.DNA, Complementary: 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.Enzyme Stability: 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.DNA Primers: 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.N-Acetylmuramoyl-L-alanine Amidase: An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.Phosphates: Inorganic salts of phosphoric acid.Botulinum Toxins: Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.Neuropeptides: Peptides released by NEURONS as intercellular messengers. Many neuropeptides are also hormones released by non-neuronal cells.Cations, Divalent: Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.Monoiodotyrosine: A product from the iodination of tyrosine. In the biosynthesis of thyroid hormones (THYROXINE and TRIIODOTHYRONINE), tyrosine is first iodized to monoiodotyrosine.Tachykinins: A family of biologically active peptides sharing a common conserved C-terminal sequence, -Phe-X-Gly-Leu-Met-NH2, where X is either an aromatic or a branched aliphatic amino acid. Members of this family have been found in mammals, amphibians, and mollusks. Tachykinins have diverse pharmacological actions in the central nervous system and the cardiovascular, genitourinary, respiratory, and gastrointestinal systems, as well as in glandular tissues. This diversity of activity is due to the existence of three or more subtypes of tachykinin receptors.Castor Bean: Common name for Ricinus communis, a species in the family EUPHORBIACEAE. It is the source of CASTOR OIL.Cyclohexanecarboxylic AcidsDipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Guinea Pigs: A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research.Sodium: A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.Brain: The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Heterocyclic Compounds, 3-Ring: A class of organic compounds containing three ring structures, one of which is made up of more than one kind of atom, usually carbon plus another atom. The heterocycle may be either aromatic or nonaromaticApoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Edetic Acid: A chelating agent that sequesters a variety of polyvalent cations such as CALCIUM. It is used in pharmaceutical manufacturing and as a food additive.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.PhenanthrolinesMitochondrial ADP, ATP Translocases: A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Recombinant Fusion Proteins: 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.DiazomethaneAlanine: 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.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Cathepsins: 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.Zinc: 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.Natriuresis: Sodium excretion by URINATION.Proline: 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.Antigens, CD13: Zinc-binding metalloproteases that are members of the type II integral membrane metalloproteases. They are expressed by GRANULOCYTES; MONOCYTES; and their precursors as well as by various non-hematopoietic cells. They release an N-terminal amino acid from a peptide, amide or arylamide.Saccharomyces cerevisiae: 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.Streptomyces griseus: An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Endopeptidase K: An enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Endothelins: 21-Amino-acid peptides produced by vascular endothelial cells and functioning as potent vasoconstrictors. The endothelin family consists of three members, ENDOTHELIN-1; ENDOTHELIN-2; and ENDOTHELIN-3. All three peptides contain 21 amino acids, but vary in amino acid composition. The three peptides produce vasoconstrictor and pressor responses in various parts of the body. However, the quantitative profiles of the pharmacological activities are considerably different among the three isopeptides.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.Thymopentin: Synthetic pentapeptide corresponding to the amino acids 32-36 of thymopoietin and exhibiting the full biological activity of the natural hormone. It is an immunomodulator which has been studied for possible use in the treatment of rheumatoid arthritis, AIDS, and other primary immunodeficiencies.Kell Blood-Group System: Multiple erythrocytic antigens that comprise at least three pairs of alternates and amorphs, determined by one complex gene or possibly several genes at closely linked loci. The system is important in transfusion reactions. Its expression involves the X-chromosome.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Cyclic GMP: Guanosine cyclic 3',5'-(hydrogen phosphate). A guanine nucleotide containing one phosphate group which is esterified to the sugar moiety in both the 3'- and 5'-positions. It is a cellular regulatory agent and has been described as a second messenger. Its levels increase in response to a variety of hormones, including acetylcholine, insulin, and oxytocin and it has been found to activate specific protein kinases. (From Merck Index, 11th ed)Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Cell Line, Tumor: A cell line derived from cultured tumor cells.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Plasmids: 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.
Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone. (1/1)
(+info)
Correction: Achieving equal standards in medical student education: is a national exit examination the answer? | The Medical...
Clp protease familyEndopeptidase Clp ATP-dependent Clp protease proteolytic subunit Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, ... ClpP endopeptidase family, clan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and ... Bowers B, Gottesman S (July 1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp ... It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective ...
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial is an enzyme that in humans is encoded by the CLPX gene ... Endopeptidase Clp). The knowledge of human ClpX protein are majorly based on the investigations on E. Coli protein. The monomer ... ATP binding can stabilize the association between ClpX and ClpP ring structures. ClpX is an ATP-dependent chaperone that can ... Baker TA, Sauer RT (January 2012). "ClpXP, an ATP-powered unfolding and protein-degradation machine". Biochimica et Biophysica ...
... may refer to: CLP protease family, a family of proteolytic enzymes Endopeptidase Clp, an enzyme complex ATP-dependent Clp ...
... may stand for: CLP protease family, a family of proteolytic enzymes Endopeptidase Clp, an enzyme complex ATP-dependent Clp ...
... atp-dependent proteases MeSH D08.811.277.656.149.200 --- endopeptidase clp MeSH D08.811.277.656.149.500 --- protease la MeSH ... cyclin-dependent kinase 9 MeSH D08.811.913.696.620.682.700.200.323 --- cyclin-dependent kinase 2 MeSH D08.811.913.696.620.682. ... 700.200.451 --- cyclin-dependent kinase 4 MeSH D08.811.913.696.620.682.700.200.515 --- cyclin-dependent kinase 6 MeSH D08.811. ... cyclin-dependent kinase 5 MeSH D08.811.913.696.620.682.700.646.500.750 --- cyclin-dependent kinase 2 MeSH D08.811.913.696. ...
... (EC 3.4.21.92, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp ... Endopeptidase CLP protease family ATP-dependent Clp protease proteolytic subunit Gottesman, S.; Clark, W.P.; Maurizi, M.R. ( ... Maurizi, M.R.; Thompson, M.W.; Singh, S.K.; Kim, S.-H. (1994). "Endopeptidase Clp: the ATP-dependent Clp protease from ... "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate". J. Biol. ...
ATP-dependent serine proteinase, lon proteinase, protease La, proteinase La, ATP-dependent lon proteinase, ATP-dependent ... A heat-shock gene which encodes the ATP-dependent protease La". J. Biol. Chem. 263: 11718-11728. PMID 3042779. Endopeptidase La ... Desautels, M.; Goldberg, A.L. (1982). "Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat ... Larimore, F.S.; Waxman, L.; Goldberg, A.L. (1982). "Studies of the ATP-dependent proteolytic enzyme, protease La, from ...
This protein is an essential component to form the protein complex of Clp protease (Endopeptidase Clp). Enzyme ClpP is a highly ... ATP-dependent Clp protease proteolytic subunit (ClpP) is an enzyme that in humans is encoded by the CLPP gene. ... "Entrez Gene: CLPP ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli)". Katayama-Fujimura, Y; ... 2002). "Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP". J. Biol. Chem. 277 (23): ...
Endopeptidase Clp Clp protease family Varshavsky, Alexander (2011-08-01). "The N-end rule pathway and regulation by proteolysis ... the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. In the bacterial cytosol, ATP-dependent protein ...
Later, the ATP-dependent proteolytic complex that was responsible for ubiquitin-dependent protein degradation was discovered ... Wilk S, Orlowski M (Nov 1980). "Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary ... After a protein has been ubiquitinated, it is recognized by the 19S regulatory particle in an ATP-dependent binding step. The ... Ciehanover A, Hod Y, Hershko A (Apr 1978). "A heat-stable polypeptide component of an ATP-dependent proteolytic system from ...
... encoding enzyme ATP-dependent RNA helicase DDX24 DEGS2: encoding protein Delta(4)-desaturase, sphingolipid 2 DLGAP5: Disks ... encoding enzyme Probable O-sialoglycoprotein endopeptidase PAPOLA: encoding enzyme Poly(A) polymerase alpha PCNX: encoding ...
ATP-dependent Clp protease proteolytic subunit. B. *Batroxobin. *Brachyurin. C. *C-terminal processing peptidase ... Wikimedia Commons has media related to Serine endopeptidases.. EC 3.4.21 Serine endopeptidases ...
Alongside glucose-dependent insulinotropic peptide (GIP), GLP-1 is the only known incretin describing its ability to decrease ... Firstly, the full-length GLP-1 (1-37) was found to be catalysed by endopeptidase to the biologically active GLP-1 (7-37). ... During the process, influx of glucose ensures sufficient ATP to sustain the stimulatory effect. Additionally, GLP-1 ensures the ... The most noteworthy effect of GLP-1 is its ability to promote insulin secretion in a glucose-dependent manner. As GLP-1 binds ...
ATP-binding cassette, sub-family A (ABC1), member 12 ACTR1B: encoding protein Beta-centractin AGXT: alanine-glyoxylate ... U12-dependent splicing) RPL37A: encoding protein 60S ribosomal protein L37a SATB2: Homeobox 2 SDPR: Serum deprivation-response ... Prolyl endopeptidase-like PXDN: Peroxidasin homolog QPCT: Glutaminyl-peptide cyclotransferase RETSAT: All-trans-retinol 13,14- ... ATP-binding cassette, subfamily A, members 5 and 8 C2orf18: encoding protein Transmembrane protein C2orf18 C2orf28: encoding ...
Brody, I; Ronquist, G; Gottfries, A; Stegmayr, B (1981). [PM:6120566 "Abnormal deficiency of both Mg2+ and Ca2+-dependent ... Ronquist, G (1988). [PM:2977004 "Zinc ion stimulation of ATP cleavage by prostasomes from human seminal plasma"] Check ,url= ... neutral endopeptidase, CD10); angiotensin converting enzyme (ACE, CD143); tissue factor TF (CD142, thromboplastin); decay ... ATP)"] Check ,url= value (help). Biochimica et Biophysica Acta (BBA) - General Subjects. 1830 (10): 4604-4610. doi:10.1016/j. ...
... leading to a rise in the ATP:ADP ratio within the cell. An increased intracellular ATP:ADP ratio closes the ATP-sensitive SUR1/ ... Proinsulin undergoes maturation into active insulin through the action of cellular endopeptidases known as prohormone ... and glucose-dependent insulinotropic peptide (GIP). Release of insulin is strongly inhibited by norepinephrine (noradrenaline ... high-energy ATP molecules are produced by the oxidation of acetyl CoA (the Krebs cycle substrate), ...
Then, the hexameric AAA-ATPase NSF catalyzes the ATP-dependent unfolding of the SNARE proteins and releases them into the ... The light chain has zinc-dependent endopeptidase or more specifically matrix metalloproteinase (MMP) activity through which ... The ATP hydrolysis-coupled dissociation of SNARE complexes is an energy investment that can be compared to "cocking the gun" so ... The light chain of BoNT acts as a metalloprotease on SNARE proteins that is dependent on Zn(II) ions, cleaving them and ...
Now EC 3.4.22.53, calpain-2 EC 3.4.22.18: Transferred entry: prolyl endopeptidase (thiol-dependent). Now EC 3.4.21.26, prolyl ... Now included with EC 3.5.2.6 β-lactamase EC 3.5.2.9: 5-oxoprolinase (ATP-hydrolysing) EC 3.5.2.10: creatininase EC 3.5.2.11: L- ... Ste24 endopeptidase EC 3.4.24.85: S2P endopeptidase EC 3.4.24.86: ADAM 17 endopeptidase EC 3.4.24.87: ADAMTS13 endopeptidase EC ... ADAM10 endopeptidase EC 3.4.24.82: ADAMTS-4 endopeptidase EC 3.4.24.83: anthrax lethal factor endopeptidase EC 3.4.24.84: ...
... are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process ... "Constitutive and interferon-gamma-induced expression of the human proteasome subunit multicatalytic endopeptidase complex-like ...
cellular response to ATP. • ovulation. • positive regulation of smooth muscle cell proliferation. • hair cycle. • response to ... E-cat is regulated by E-allo in a way dependent on what ligand is bound to E-allo. Substrate and non-substrate fatty acid (FAs ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • cellular response to non-ionic ...
Yaish P, Gazit A, Gilon C, Levitzki A (1988). "Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors ... TKIs operate by four different mechanisms: they can compete with adenosine triphosphate (ATP), the phosphorylating entity, the ... "ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system". Nture Chem Biol. 9 (5): 307-312. doi ...
cysteine-type endopeptidase inhibitor activity. • связывание с ионом металла. • ubiquitin-protein transferase activity. • ... Davoodi J, Lin L, Kelly J, et al. (2004). «Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP ... Structural requirements for hippocalcin binding and effects on survival of NGF-dependent sympathetic neurons.». Biochim. ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • response to amino acid. • negative ...
When ATP levels rise, ATP binds an allosteric site in PFK1 to decrease the rate of the enzyme reaction; glycolysis is inhibited ... Under these conditions, traditional Michaelis-Menten kinetics give a false value for Ki, which is time-dependent. The true ... This catabolic pathway consumes glucose and produces ATP, NADH and pyruvate. A key step for the regulation of glycolysis is an ... The activity will be decreased in a time-dependent manner, usually following exponential decay. Fitting these data to a rate ...
Gottesman MM, Fojo T, Bates SE (January 2002). "Multidrug resistance in cancer: role of ATP-dependent transporters". Nat. Rev. ... aspartic-type endopeptidase activity. • endopeptidase activity. • hydrolase activity. • aspartic endopeptidase activity, ... Notch receptor processing, ligand-dependent. • positive regulation of phosphorylation. • astrocyte activation. • synapse ... positive regulation of proteasomal ubiquitin-dependent protein catabolic process. • L-glutamate transport. • brain ...
Ferdinand KC (February 2011). "Are cardiovascular benefits in statin lipid effects dependent on baseline lipid levels?". ... in part because the risk/benefit ratio of statins in low-risk populations is highly dependent on the rate of adverse events.[57 ... "Comparison of cytochrome P-450-dependent metabolism and drug interactions of the 3-hydroxy-3-methylglutaryl-CoA reductase ...
... the ATP-dependent proteolytic complex that was responsible for ubiquitin-dependent protein degradation was discovered and was ... Wilk S, Orlowski M (November 1980). "Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary ... After a protein has been ubiquitinated, it is recognized by the 19S regulatory particle in an ATP-dependent binding step.[15][ ... Ciehanover A, Hod Y, Hershko A (April 1978). "A heat-stable polypeptide component of an ATP-dependent proteolytic system from ...
ATP-Dependent Endopeptidases | Profiles RNS"ATP-Dependent Endopeptidases" by people in this website by year, and whether "ATP-Dependent Endopeptidases" was a major or ... "ATP-Dependent Endopeptidases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... ATP-Dependent Endopeptidases*ATP-Dependent Endopeptidases. *ATP Dependent Endopeptidases. *Endopeptidases, ATP-Dependent ... Below are the most recent publications written about "ATP-Dependent Endopeptidases" by people in Profiles. ...
ATP-Dependent Proteases); EC 3.4.22.36 (Caspase 1); EC 3.4.25.1 (Proteasome Endopeptidase Complex); K848JZ4886 (Cysteine). ... Transportadores de Cassetes de Liga o de ATP/metabolismo. Proteases Dependentes de ATP/gen tica. Proteases Dependentes de ATP/ ... Complexo de Endopeptidases do Proteassoma/metabolismo. Serina Endopeptidases/gen tica. Serina Endopeptidases/metabolismo. ... ATP-Dependent Proteases); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (mitochondrial intermembrane space protease); EC 3.4 ...
GO:0004176 ATP-dependent peptidase activity GO:0004252 serine-type endopeptidase activity ... A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.. Proc. Natl. Acad. Sci. U.S.A ... Bacterial ATP-dependent proteases [PMID: 8294008, PMID: 8331083]. The prototype of those bacterial enzymes is the Escherichia ... The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of ...
GO:0004298 threonine-type endopeptidase activity Cellular Component. GO:0005839 proteasome core complex GO:0009376 HslUV ...
CLPP - ATP-dependent Clp protease proteolytic subunit, mitochondrial precursor - Bos taurus (Bovine) - CLPP gene & proteinProtease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase ... serine-type endopeptidase activity Source: UniProtKB. View the complete GO annotation on QuickGO ... ... ATP-dependent Clp protease proteolytic subunit, mitochondrial. ,p>This subsection of the PTM / Processing section describes ... ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC:3.4.21.92). Alternative name(s): ...
Atp-dependent Endopeptidases. Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains. ... Dna Ligase Atp. ATP-dependent cellular enzyme which catalyzes DNA replication, repair and recombination through formation of ... DNA ligases either require ATP or NAD. However, archaebacterial, viral, and some eubacterial DNA ligases are ATP-dependent. ... An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike ...
CDD Conserved Protein Domain Family: clpPATP-dependent Clp endopeptidase, proteolytic subunit ClpP. This model for the proteolytic subunit ClpP has been rebuilt to a ...
ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the ... ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the ... serine-type endopeptidase activity Source: InterPro. Complete GO annotation.... ,p>The ,a href="http://www.geneontology.org/"> ... ATPUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB automatic annotation system.,/ ...
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- ... ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- ... serine-type endopeptidase activity Source: UniProtKB-UniRule. Complete GO annotation on QuickGO ... ... ATP-dependent protease LaUniRule annotation. Manual assertion according to rulesi ...
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major ... Endopeptidase ClpUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB automatic ... ATP-dependent Clp protease proteolytic subunitUniRule annotation. ,p>Manual validated information which has been generated by ... sp,Q5NH47,CLPP_FRATT ATP-dependent Clp protease proteolytic subunit OS=Francisella tularensis subsp. tularensis (strain SCHU S4 ...
S14 family endopeptidase ClpAImported. Automatic assertion inferred from database entriesi ... ATP-dependent Clp protease ATP-binding subunit ClpA. Clostridium colicanis DSM 13634 ... ATP-dependent Clp protease ATP-binding subunit ClpA. Clostridium thermopalmarium DSM 5974 ... ATP-dependent Clp protease subunit A (ClpA)Imported. Automatic assertion inferred from database entriesi ...
Multi-omics Analysis Identifies ATF4 as a Key Regulator of the Mitochondrial Stress Response in MammalsProteasome Endopeptidase Complex * ATP dependent 26S protease ... Serine Endopeptidases * High-Temperature Requirement A Serine ...
... dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the ... Endopeptidase Clp / genetics * Endopeptidase Clp / metabolism* * Escherichia coli / enzymology* * Escherichia coli Proteins / ... The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic ... Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation Res ...
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB- ... DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0034605; P:cellular response to heat ... 191:347-354(2009). CC -!- FUNCTION: ATP-dependent serine protease that mediates the CC selective degradation of mutant and ... ATP-dependent protease La {ECO:0000256,HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000256,HAMAP-Rule:MF_01973, GN ECO:0000313,EMBL: ...
Proteasome Endopeptidase Complex * ATP dependent 26S protease ...
Proteasome Endopeptidase Complex * ATP dependent 26S protease * Ligases ...
Proteasome Endopeptidase Complex * ATP dependent 26S protease * Adenosine Triphosphatases * RPT4 protein, S cerevisiae ...
CLPP Gene - GeneCards | CLPP Protein | CLPP AntibodyEndopeptidase Clp 3 4 * EC 3.4.21.92 4 51 * ClpP (Caseinolytic Protease, ATP-Dependent, Proteolytic Subunit, E. Coli) Homolog 2 ... Putative ATP-Dependent Clp Protease Proteolytic Subunit, Mitochondrial 3 * ATP-Dependent Protease ClpAP (E. Coli), Proteolytic ... ClpP Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E. Coli) 2 * ClpP Caseinolytic Protease, ATP-Dependent ... Putative ATP-dependent Clp protease proteolytic subunit, mitochondrial) ELISA and Immunotag™ Putative ATP-dependent Clp ...
Dtpsy_1475 ATP-dependent metalloprotease FtsH Dtpsy_2695 Ste24 endopeptidase Dtpsy_3023 HtpX domain protein Dtpsy_1230 membrane ... Dtpsy_1128 ATP-dependent Clp protease Dtpsy_1130 ATP-dependent protease La Dtpsy_1549 SOS-response transcriptional repressor ... ATP-dependent Clp protease, protease subunit [EC:3.4.21.92] K01338 lon; ATP-dependent Lon protease [EC:3.4.21.53] K01356 lexA; ... ATP-dependent HslUV protease, peptidase subunit HslV [EC:3.4.25.2] K00681 ggt; gamma-glutamyltranspeptidase / glutathione ...
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- ... ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- ... serine-type endopeptidase activity Source: UniProtKB-UniRule. Complete GO annotation on QuickGO ... ... ATP-dependent protease LaUniRule annotation. Manual assertion according to rulesi ...
Mouse Atp-Dependent Chromatin Remodeling to Mouse Apical Part of Cell from Cell Signaling TechnologyMouse Atp-Dependent Chromatin Remodeling, Mouse Atp-Dependent 3-5 Dna Helicase Activity, Mouse Atp Metabolic Process, Mouse ... Mouse Aspartic-Type Endopeptidase Activity Mouse Aspartic-Type Endopeptidase Activity: Polyclonal Antibody - Caspase-3 Antibody ... Mouse Atp-Dependent 3-5 Dna Helicase Activity Mouse Atp-Dependent 3-5 Dna Helicase Activity: Polyclonal Antibody - Mre11 ... Mouse Atp-Dependent Chromatin Remodeling Mouse Atp-Dependent Chromatin Remodeling: Polyclonal Antibody - HDAC2 Antibody, ...
ATP-dependent peptidase activity; FT GO_function: GO:0004252 - serine-type endopeptidase FT activity; GO_function: GO:0005524 ... ATP-dependent peptidase activity; GO_function: FT GO:0004252 - serine-type endopeptidase activity; FT GO_function: GO:0004518 ... "probable ATP-dependent Clp protease ATP-binding FT subunit" FT /EC_number="3.4.21.92" FT /note="GO_function: GO:0003677 - DNA ... "possible ATP-dependent helicase" FT /note="GO_function: GO:0003677 - DNA binding; GO_function: FT GO:0005524 - ATP binding; GO_ ...
Proteasome Endopeptidase Complex * ATP dependent 26S protease Grant support * P01 AG031097/AG/NIA NIH HHS/United States ...
Endopeptidase Clp Clp protease family Varshavsky, Alexander (2011-08-01). "The N-end rule pathway and regulation by proteolysis ... the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. In the bacterial cytosol, ATP-dependent protein ...
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255,HAMAP-Rule:MF_00444}; DE EC=3.4.21.92 {ECO:0000255 ... DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR CDD; cd07017; S14_ClpP_2; 1. DR HAMAP; MF_00444; ClpP ... FT CHAIN 1 198 ATP-dependent Clp protease proteolytic FT subunit. FT /FTId=PRO_1000026144. FT ACT_SITE 103 103 Nucleophile. { ... the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides ...
- In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family, clan SK). (wikipedia.org)
- ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin. (wikipedia.org)
- ATP binding can stabilize the association between ClpX and ClpP ring structures. (wikipedia.org)
- As an essential component of ClpP protease complex, ClpX recruits degradable substrates and unfolds their tertiary structure, which requires energy provided by ATP hydrolysis. (wikipedia.org)
- GO annotations related to this gene include threonine-type endopeptidase activity . (genecards.org)
- Bacterial ATP-dependent proteases [ PMID: 8294008 , PMID: 8331083 ]. (ebi.ac.uk)
- The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the enzymes utilized, in organisms from different kingdoms. (nih.gov)
- GPP and its ortholog, the peroxisomal DEG protease from Arabidopsis thaliana (AtDEG15), belong to the Deg/HtrA family of ATP-independent serine proteases with Escherichia coli DegP as their prototype. (springer.com)
- Much of this directed protein turnover is performed by proteases that require ATP and, of those in bacteria, the Clp protease from Escherichia coli is one of the best characterized to date. (nih.gov)
- This gene encodes a mitochondrial matrix protein that belongs to the Lon family of ATP-dependent proteases. (genecards.org)
- They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. (ebi.ac.uk)
- Key events in mitosis such as sister chromatid separation and subsequent inactivation of cyclin-dependent kinase 1 are regulated by ubiquitin-dependent proteolysis. (nih.gov)
- It was then discovered that a previously identified protein associated with proteolytic degradation, known as ATP-dependent proteolysis factor 1 (APF-1), was the same protein as ubiquitin. (wikipedia.org)
- Proteolysis-dependent roles of the 26S proteasome in transcription activation. (nih.gov)
- Other folded as well as unstructured polyubiquitylated proteins required ATP hydrolysis for proteolysis and deubiquitylation. (elsevier.com)
- Most notably, we describe a mutation in the ATP dependent protease HslUV that induces rapid degradation of σ32, and a mutation leading to increased levels of the house keeping σ70 that outcompete σ32 for binding to the RNA polymerase. (bireme.br)
- ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. (uniprot.org)
- In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. (wikipedia.org)
- ClpX is an ATP-dependent chaperone that can recognize protein substrates by binding to protein degradation tags. (wikipedia.org)
- The 26S proteasome is the major eukaryotic ATP-dependent protease, responsible for regulating the proteome through degradation of ubiquitin-tagged substrates. (nih.gov)
- However, work by Alfred Goldberg in 1977 on ATP-dependent protein degradation in reticulocytes, which lack lysosomes, suggested the presence of a second intracellular degradation mechanism. (wikipedia.org)
- Activator degradation can be transcription dependent where the initiation of transcription marks the activator for destruction. (nih.gov)
- Exposure of S. cerevisiae to the alkylating agent MMS resulted in activation of genes that are involved in ubiquitin- and 26S proteasome-dependent protein degradation. (nih.gov)
- All mutations reduced the activity of the heat shock sigma factor σ32, demonstrating that the DnaK-dependent inactivation of σ32 is a growth requirement. (bireme.br)
- By pharmacological inhibition and gene silencing, we demonstrated that PI3K_PDK1_RSK2 signaling was induced in TGEV-infected ST cells, and ouabain imparted a degree of anti-TGEV activity via further augmentation of this existing PI3K_PDK1 axis signaling, in a manner dependent upon its association with the Na/K-ATPase. (bioportfolio.com)
- In this study, we utilize a panel of P. aeruginosa burn wound and cystic fibrosis (CF) lung isolates to demonstrate that P. aeruginosa alters S. aureus susceptibility to bactericidal antibiotics in a variable, strain-dependent manner and further identify 3 independent interactions responsible for antagonizing or potentiating antibiotic activity against S. aureus. (bireme.br)
- The proteasome has an ATP-dependent proteolytic activity. (genecards.org)
- Molecular function: serine-type endopeptidase activity. (expasy.org)
- IMSEAR at SEARO: Ubiquitin with a non-ATP-dependent slow intrinsic proteolytic activity: a mild and rapid purification procedure. (who.int)
- Ubiquitin showed a slow intrinsic proteolytic activity against SDS-denatured beta-galactosidase in the absence of ATP. (who.int)
- Gene Ontology (GO) annotations related to this gene include sequence-specific DNA binding and serine-type endopeptidase activity . (genecards.org)
- It has an ATP-dependent proteolytic activity (By similarity). (uniprot.org)
- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. (univ-lyon1.fr)
- PepO has significant sequence identity to mammalian metallopeptidases, including endothelin-converting enzyme, which converts a potent vasoconstrictor into its active form, and neutral endopeptidase (NEP), which is involved in terminating the activity of opioid peptides. (asm.org)
- These results indicate that FW213 pepO encodes an enzyme with activity similar to that of known mammalian endopeptidases. (asm.org)
- We identify mitochondrial trifunctional protein-α (MTPα) as a binding partner of GLP-1(28-36) and demonstrate that the ability of GLP-1(28-36) to shift substrate utilization from oxygen-consuming fatty acid metabolism toward oxygen-sparing glycolysis and glucose oxidation and to increase cAMP levels is dependent on MTPα. (jci.org)
- Here, we show in both ex vivo and in vivo models of ischemic injury that treatment with GLP-1(28-36), a neutral endopeptidase-generated (NEP-generated) metabolite of GLP-1, was as cardioprotective as GLP-1 and was abolished by scrambling its amino acid sequence. (jci.org)
- However, endogenous GLP-1 is rapidly degraded primarily by dipeptidyl peptidase-4 (DPP-4), but also neutral endopeptidase 24.11 (NEP 24.11) and renal clearance, resulting in a half-life of approximately 2 minutes. (wikipedia.org)
- In molecular biology, the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. (wikipedia.org)
- A heat-shock gene which encodes the ATP-dependent protease La". J. Biol. (wikipedia.org)
- The scaC gene encodes an ATP-binding protein (251 amino acid [aa] residues), scaB encodes a transmembrane component (278 aa residues) which presumably dimerizes ( 22 ), and scaA encodes a lipoprotein (310 aa residues) ( 27 ). (asm.org)
- fimA is part of an operon that encodes components of an ATP-binding cassette-type membrane transport system. (asm.org)
- In addition to fimA , the fim locus includes fimB (formerly orf1 ), which encodes an ATP-binding protein, and fimC (formerly orf5 ), which encodes a hydrophobic transmembrane protein ( 20 ). (asm.org)
- The cardenolide ouabain suppresses coronaviral replication via augmenting a Na/K-ATPase-dependent PI3K_PDK1 axis signaling. (bioportfolio.com)
- The transmembrane protein, FtsH, is the only known ATP-dependent protease responsible for this task. (bireme.br)
- Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. (pdbj.org)
- In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. (uniprot.org)