Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Peptides composed of two amino acid units.
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A collection of cloned peptides, or chemically synthesized peptides, frequently consisting of all possible combinations of amino acids making up an n-amino acid peptide.
Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.
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.
Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.
Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
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.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
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.
Peptides composed of between two and twelve amino acids.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A PEPTIDE that is secreted by the BRAIN and the HEART ATRIA, stored mainly in cardiac ventricular MYOCARDIUM. It can cause NATRIURESIS; DIURESIS; VASODILATION; and inhibits secretion of RENIN and ALDOSTERONE. It improves heart function. It contains 32 AMINO ACIDS.
The rate dynamics in chemical or physical systems.
The process of cleaving a chemical compound by the addition of a molecule of water.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
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).
Phosphoric acid esters of mannose.
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.
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.
A highly basic, 28 amino acid neuropeptide released from intestinal mucosa. It has a wide range of biological actions affecting the cardiovascular, gastrointestinal, and respiratory systems and is neuroprotective. It binds special receptors (RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE).
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
Calcitonin gene-related peptide. A 37-amino acid peptide derived from the calcitonin gene. It occurs as a result of alternative processing of mRNA from the calcitonin gene. The neuropeptide is widely distributed in neural tissue of the brain, gut, perivascular nerves, and other tissue. The peptide produces multiple biological effects and has both circulatory and neurotransmitter modes of action. In particular, it is a potent endogenous vasodilator.
Peptides that have the ability to enter cells by crossing the plasma membrane directly, or through uptake by the endocytotic pathway.
A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)
The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
Proteins prepared by recombinant DNA technology.
A 36-amino acid peptide produced by the L cells of the distal small intestine and colon. Peptide YY inhibits gastric and pancreatic secretion.
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
DNA analogs containing neutral amide backbone linkages composed of aminoethyl glycine units instead of the usual phosphodiester linkage of deoxyribose groups. Peptide nucleic acids have high biological stability and higher affinity for complementary DNA or RNA sequences than analogous DNA oligomers.
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.
A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.
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 PEPTIDE of 22 amino acids, derived mainly from cells of VASCULAR ENDOTHELIUM. It is also found in the BRAIN, major endocrine glands, and other tissues. It shares structural homology with ATRIAL NATRIURETIC FACTOR. It has vasorelaxant activity thus is important in the regulation of vascular tone and blood flow. Several high molecular weight forms containing the 22 amino acids have been identified.
Proteins found in any species of bacterium.
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.
Peptides that regulate the WATER-ELECTROLYTE BALANCE in the body, also known as natriuretic peptide hormones. Several have been sequenced (ATRIAL NATRIURETIC FACTOR; BRAIN NATRIURETIC PEPTIDE; C-TYPE NATRIURETIC PEPTIDE).
An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
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)
Neuropeptide and gut hormone that helps regulate GASTRIC ACID secretion and motor function. Once released from nerves in the antrum of the STOMACH, the neuropeptide stimulates release of GASTRIN from the GASTRIN-SECRETING CELLS.
A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.
A family of G-protein-coupled receptors that was originally identified by its ability to bind N-formyl peptides such as N-FORMYLMETHIONINE LEUCYL-PHENYLALANINE. Since N-formyl peptides are found in MITOCHONDRIA and BACTERIA, this class of receptors is believed to play a role in mediating cellular responses to cellular damage and bacterial invasion. However, non-formylated peptide ligands have also been found for this receptor class.
A 27-amino acid peptide with histidine at the N-terminal and isoleucine amide at the C-terminal. The exact amino acid composition of the peptide is species dependent. The peptide is secreted in the intestine, but is found in the nervous system, many organs, and in the majority of peripheral tissues. It has a wide range of biological actions, affecting the cardiovascular, gastrointestinal, respiratory, and central nervous systems.
An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.
Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.
An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.
Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behavior of cells.
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.
Sites on an antigen that interact with specific antibodies.
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.
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.
Established cell cultures that have the potential to propagate indefinitely.
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A genus of aerobic, gram-negative, motile, slightly curved, rod-shaped bacteria. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.
An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.
The sum of the weight of all the atoms in a molecule.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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.
Polysaccharides consisting of xylose units.
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 group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.
A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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 group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.
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.
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.
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 3.4.23.5. (Formerly EC 3.4.4.23).
A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
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.

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptides from digestion with a staphylococcal proteinase. (1/6114)

The extracellular proteinase of Staphylococcus aureus strain V8 was used to digest the NADP-specific glutamate dehydrogenase of Neurospora crassa. Of 35 non-overlapping peptides expected from the glutamate content of the polypeptide chain, 29 were isolated and substantially sequenced. The sequences obtained were valuable in providing overlaps for the alignment of about two-thirds of the sequences found in tryptic peptides [Wootton, J. C., Taylor, J, G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 739-748]. The blocked N-terminal peptide of the protein was isolated. This peptide was sequenced by mass spectrometry, and found to have N-terminal N-acetylserine by Howard R. Morris and Anne Dell, whose results are presented as an Appendix to the main paper. The staphylococcal proteinase showed very high specificity for glutamyl bonds in the NH4HCO3 buffer used. Partial splits of two aspartyl bonds, both Asp-Ile, were probably attributable to the proteinase. No cleavage of glutaminyl or S-carboxymethylcysteinyl bonds was found. Additional experimental detail has been deposited as Supplementary Publication SUP 50053 (5 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K, from whom copies may be obtained under the terms given in Biochem. J. (1975) 1458 5.  (+info)

Purification of gibberellic acid-induced lysosomes from wheat aleurone cells. (2/6114)

Using isopycnic density gradient centrifugation, lysosomes were concentrated in a single region of a sucrose-Ficoll gradient (p = 1-10 g cm-3), well separated from most other cell organelles. Gibberellic acid-induced lysosomes were found to be rich in alpha-amylase and protease but not ribonuclease. The lysosomal band also contained a majority of the NADH2-cytochrome c reductase, a marker enzyme for endoplasmic reticulum, found in the gradient. Examination of electron micrographs revealed that a purified band of lyosomes contained at least 3 vesicle types, ranging in size from 0-1 to 0-5 mum. The significance of these findings to proposed mechanisms of action of gibberellic acid is discussed.  (+info)

5'-Nucleotidase activity of mouse peritoneal macrophages. I. Synthesis and degradation in resident and inflammatory populations. (3/6114)

Mouse resident peritoneal macrophages display sufficient 5'-nucleotidase activity to hydrolyze 58 nm AMP/min per cell protein. This activity increases approximately 163 nm AMP/min per mg after 72 h in culture. The enzyme is renewed in unstimulated cells with a half-time of 13.9 h. The activity is not reduced by treatment of intact cells with a variety of proteolytic enzymes, including trypsin, pronase, urokinase, and plasmin. Cells obtained from an inflammatory exudate have diminished or absent levels of enzyme activity. Endotoxin-elicited cells display enzyme activitiy of 20.9 nm AMP/min per mg, while thioglycollate-stimulated macrophages have no detectable activity. The reduced level of activity in endotoxin-stimulated cells is due to their elevated rate of enzyme degradation, with a half-time of 6.9 h. Their rate of enzyme synthesis is essentially normal. No evidence for latent enzyme activity could be obtained in thioglycollate-stimulated cells, nor do these cells produce any inhibition of normal cell enzyme activity. Serum deprivation reduces the enzyme activity of resident cells to about 45% of control activity. These conditions do not significantly affect the rate of enzyme synthesis, but again are explainable by an increase in the rate of enzyme degradation. Pinocytic rate is elevated in endotoxin-stimulated cells which show a more rapid rate of enzyme degradation than unstimulated cells do. However, in serum-free conditions, the rate of enzyme degradation is doubled with no change in the pinocytic rate of the cells.  (+info)

Genome-linked protein associated with the 5' termini of bacteriophage phi29 DNA. (4/6114)

A DNA-protein complex was isolated from Bacillus subtilis bacteriophage phi29 by sucrose gradient sedimentation or gel filtration in the presence of agents known to break noncovalent bonds. A 28,000-dalton protein was released from this complex by subsequent hydrolysis of the DNA. The DNA-protein complex was examined for its susceptibility to enzymes which act upon the 5' and 3' termini of DNA molecules. It was susceptible to exonucleolytic degradation from the 3' termini by exonuclease III but not from the 5' termini by lambda exonuclease. Attempts to label radioactively the 5' termini by phosphorylation with T4 polynucleotide kinase were unsuccessful despite prior treatment with alkaline phosphatase or phosphatase treatment of denatured DNA. Removal of the majority of the bound protein by proteolytic digestion did not increase susceptibility. These results suggest that the linked protein is covalently attached to the 5' termini of phi29 DNA.  (+info)

Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori. Purification, characterization, and cDNA cloning. (5/6114)

Prophenoloxidase-activating enzyme (PPAE) was purified to homogeneity as judged by SDS-polyacrylamide gel electrophoresis from larval cuticles of the silkworm, Bombyx mori. The purified PPAE preparation was shown to be a mixture of the isozymes of PPAE (PPAE-I and PPAE-II), which were eluted at different retention times in reversed-phase high performance liquid chromatography. PPAE-I and PPAE-II seemed to be post translationally modified isozymes and/or allelic variants. Both PPAE isozymes were proteins composed of two polypeptides (heavy and light chains) that are linked by disulfide linkage(s) and glycosylated serine proteases. The results of cDNA cloning, peptide mapping, and amino acid sequencing of PPAE revealed that PPAE is synthesized as prepro-PPAE with 441 amino acid residues and is activated from pro-PPAE by cleavage of a peptide bond between Lys152 and Ile153. The homology search showed 36.9% identity of PPAE to easter, which is a serine protease involved in dorso-ventral pattern formation in the Drosophila embryo, and indicated the presence of two consecutive clip-like domains in the light chain. A single copy of the PPAE gene was suggested to be present in the silkworm genome. In the fifth instar larvae, PPAE transcripts were detected in the integument, hemocytes, and salivary glands but not in the fat body or mid gut. A polypeptide cross-reactive to mono-specific anti-PPAE/IgG was transiently detected in the extract of eggs between 1 and 3 h after they were laid.  (+info)

Direct evidence of Na+/Ca2+ exchange in squid rhabdomeric membranes. (6/6114)

Na+/Ca2+ exchange has been investigated in squid (Loligo pealei) rhabdomeric membranes. Ca2+-containing vesicles have been prepared from purified rhabdomeric membranes by extrusion through polycarbonate filters of 1-micrometer pore size. After removal of external Ca2+, up to 90% of the entrapped Ca2+ could be specifically released by the addition of Na+; this finding indicates that most of the vesicles contained Na+/Ca2+ exchanger. The Na+-induced Ca2+ efflux had a half-maximum value (K1/2) of approximately 44 mM and a Hill coefficient of approximately 1.7. The maximal Na+-induced Ca2+ efflux was approximately 0.6 nmol Ca2+. s-1. mg protein-1. Similar Na+-induced Ca2+ effluxes were measured if K+ was replaced with Li+ or Cs+. Vesicles loaded with Ca2+ by Na+/Ca2+ exchange also released this Ca2+ by Na+/Ca2+ exchange, suggesting that Na+/Ca2+ exchange operated in both forward and reverse modes. Limited proteolysis by trypsin resulted in a rate of Ca2+ efflux enhanced by approximately fivefold when efflux was activated with 95 mM NaCl. For vesicles subjected to limited proteolysis by trypsin, Na+/Ca2+ exchange was characterized by a K1/2 of approximately 25 mM and a Hill coefficient of 1.6. For these vesicles, the maximal Na+-induced Ca2+ efflux was about twice as great as in control vesicles. We conclude that Na+/Ca2+ exchange proteins localized in rhabdomeric membranes mediate Ca2+ extrusion in squid photoreceptors.  (+info)

A study of the genetical structure of the Cuban population: red cell and serum biochemical markers. (7/6114)

Gene frequencies of several red cell and serum gentic markers were determined in the three main racial groups--whites, mulattoes and Negroes--of the Cuban population. The results were used to estimate the relative contribution of Caucasian and Negro genes to the genetic makeup of these three groups and to calculate the frequencies of these genes in the general Cuban population.  (+info)

Identification of kallidin degrading enzymes in the isolated perfused rat heart. (8/6114)

Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found.  (+info)

The term "mucolipidoses" was coined by the American pediatrician and medical geneticist Dr. Victor A. McKusick in the 1960s to describe this group of diseases. The term is derived from the Greek words "muco-," meaning mucus, and "-lipido-," meaning fat, and "-osis," meaning condition or disease.

There are several types of mucolipidoses, including:

1. Mucolipidosis type I (MLI): This is the most common form of the disorder and is caused by a deficiency of the enzyme galactocerebrosidase (GALC).
2. Mucolipidosis type II (MLII): This form of the disorder is caused by a deficiency of the enzyme sulfatases, which are necessary for the breakdown of sulfated glycosaminoglycans (sGAGs).
3. Mucolipidosis type III (MLIII): This form of the disorder is caused by a deficiency of the enzyme acetyl-CoA:beta-glucoside ceramide beta-glucosidase (CERBGL), which is necessary for the breakdown of glycosphingolipids.
4. Mucolipidosis type IV (MLIV): This form of the disorder is caused by a deficiency of the enzyme glucocerebrosidase (GUCB), which is necessary for the breakdown of glucocerebroside, a type of glycosphingolipid.

Mucolipidoses are usually diagnosed by measuring the activity of the enzymes involved in glycosphingolipid metabolism in white blood cells or fibroblasts, and by molecular genetic analysis to identify mutations in the genes that code for these enzymes. Treatment is typically focused on managing the symptoms and may include physical therapy, speech therapy, and other supportive care measures. Bone marrow transplantation has been tried in some cases as a potential treatment for mucolipidosis, but the outcome has been variable.

Prognosis: The prognosis for mucolipidoses is generally poor, with most individuals with the disorder dying before the age of 10 years due to severe neurological and other complications. However, with appropriate management and supportive care, some individuals with milder forms of the disorder may survive into adulthood.

Epidemiology: Mucolipidoses are rare disorders, with an estimated prevalence of 1 in 100,000 to 1 in 200,000 births. They affect both males and females equally, and there is no known geographic or ethnic predilection.

Clinical features: The clinical features of mucolipidoses vary depending on the specific type of disorder and the severity of the mutation. Common features include:

* Delayed development and intellectual disability
* Seizures
* Vision loss or blindness
* Hearing loss or deafness
* Poor muscle tone and coordination
* Increased risk of infections
* Coarsening of facial features
* Enlarged liver and spleen
* Abnormalities of the heart, including ventricular septal defect and atrial septal defect

Diagnosis: Diagnosis of mucolipidoses is based on a combination of clinical features, laboratory tests, and genetic analysis. Laboratory tests may include measurement of enzyme activity in white blood cells, urine testing, and molecular genetic analysis.

Treatment and management: There is no cure for mucolipidoses, but treatment and management strategies can help manage the symptoms and improve quality of life. These may include:

* Physical therapy to improve muscle tone and coordination
* Speech therapy to improve communication skills
* Occupational therapy to improve daily living skills
* Anticonvulsant medications to control seizures
* Supportive care to manage infections and other complications
* Genetic counseling to discuss the risk of inheritance and options for family planning.

Prognosis: The prognosis for mucolipidoses varies depending on the specific type and severity of the condition. In general, the prognosis is poor for children with more severe forms of the disorder, while those with milder forms may have a better outlook. With appropriate management and supportive care, some individuals with mucolipidoses can lead relatively normal lives, while others may require ongoing medical care and assistance throughout their lives.

Dev IK, Ray PH (June 1990). "Signal peptidases and signal peptide hydrolases". Journal of Bioenergetics and Biomembranes. 22 (3 ... It releases signal peptides from murein prolipoprotein and other bacterial membrane prolipoproteins. It also hydrolyses -Xaa- ...
Kobayashi K, Smith JA (August 1987). "Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction". The Journal ... Acylaminoacyl-peptidase (EC 3.4.19.1, acylamino-acid-releasing enzyme, N-acylpeptide hydrolase, N-formylmethionine (fMet) ... aminopeptidase, alpha-N-acylpeptide hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of ...
"Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase". Human APEH genome location and APEH gene details page in the UCSC Genome ... 2000). "Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase". Biochim. Biophys. Acta. ... The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It ... 1992). "Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme". J. Biol. Chem. 267 (6): 3811-8. ...
Meprin A subunit alpha also known as endopeptidase-2 or PABA peptide hydrolase is the alpha subunit of the meprin A enzyme that ... "Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)". Banerjee S, Oneda B, Yap LM, Jewell DP, Matters GL, Fitzpatrick ... 1994). "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 ... 1999). "Composition of the peptide fraction in human blood plasma: database of circulating human peptides". J. Chromatogr. B. ...
Proteases -Glycosidases Antimicrobial peptides Cathelicidin Hydrolase Molecular Cell Biology 6ed, Lodish et al. "Safety ... An acid hydrolase is an enzyme that works best at acidic pHs. It is commonly located in lysosomes, which are acidic on the ... types of Acid Hydrolase: -Nucleases (P1 from Penicillium citrinum, used in the food industry for taste enhancement or present ... Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the ...
There is also evidence that it can serve as a peptide hydrolase in the production of cat pheromone precursors. Cauxin has a ...
... a homologue of the yeast PRE4-subunit essential for peptidylglutamyl-peptide hydrolase activity". FEBS Lett. 346 (2-3): 151-5. ... An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene ... Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin- ...
Harris RB, Wilson IB (1985). "Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase". Peptides. ... Importance of Ser in the P1 position". International Journal of Peptide and Protein Research. 32 (1): 35-40. PMID 3146555. ... atrial peptide convertase) is an enzyme. It catalyses the following chemical reaction Release of a C-terminal dipeptide or ... Peptides. 10 (1): 63-8. doi:10.1016/0196-9781(89)90077-6. PMID 2501770. Peptidyl-dipeptidase+B at the US National Library of ...
1994). "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 ... Substrates include bioactive peptides and extracellular matrix proteins. See MIM 600388 for further information on meprins.[ ... 1997). "Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and ... 2001). "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity". J. Biol. Chem. ...
Park H, Suzuki T, Lennarz WJ (Sep 2001). "Identification of proteins that interact with mammalian peptide:N-glycanase and ... implicate this hydrolase in the proteasome-dependent pathway for protein degradation". Proceedings of the National Academy of ...
... peptides, and proteins, including many hydrolases. The alkaline venom is quite different from bee venom, which is acidic. The ...
Cellular proteins with the double jelly roll fold include glycoside hydrolases of the DUF2961 family, peptide:N-glycosidase F ( ...
... that are specific for this genus in the proteins such as non-ribosomal peptide synthetase, nucleoside hydrolase, TetR family ... alpha/beta hydrolase, potassium transporter Kef, a membrane protein, DUF222 domain-containing protein, MFS transporter, ...
EC 3.4 are hydrolases that act on peptide bonds EC 3.4.11 are those hydrolases that cleave off the amino-terminal amino acid ... EC 3 enzymes are hydrolases enzymes (enzymes that use water to break up some other molecule) ...
Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein and Peptide Letters. 16 (10): 1137-48. doi:10.2174/ ... Microsomal epoxide hydrolase belongs to the superfamily α/β-hydrolase fold enzymes. The center of all α/β-hydrolase fold ... ether hydrolases). The systematic name of this enzyme class is cis-stilbene-oxide hydrolase. Other names in common use include ... cis-epoxide hydrolase, and mEH. Microsomal epoxide hydrolase is a single polypeptide chain composed of 455 amino acids with a ...
... and peptide ligase". Cell. 93 (1): 103-9. doi:10.1016/S0092-8674(00)81150-2. PMID 9546396. Koldamova RP, Lefterov IM, DiSabella ... Bleomycin hydrolase is an enzyme that in humans is encoded by the BLMH gene. Bleomycin hydrolase (BMH) is a cytoplasmic ... Koldamova, R P; Lefterov I M; DiSabella M T; Almonte C; Watkins S C; Lazo J S (June 1999). "Human bleomycin hydrolase binds ... 1998). "Bleomycin hydrolase is associated with risk of sporadic Alzheimer's disease". Nat. Genet. 18 (3): 211-2. doi:10.1038/ ...
... signal peptide hydrolase, signal peptide peptidase, signalase, bacterial leader peptidase 1) is an enzyme. This enzyme ... leader peptide hydrolase, leader proteinase, signal peptidase, pilin leader peptidase, SPC, prokaryotic signal peptidase, ...
PABA-peptide hydrolase, PPH) is an enzyme that cleaves protein and peptide substrates preferentially on carboxyl side of ... Meprin A (EC 3.4.24.18, endopeptidase-2, meprin-a, meprin, N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, ...
L-pyroglutamyl peptide hydrolase, pyrrolidone-carboxyl peptidase, pyrrolidone-carboxylate peptidase, pyrrolidonyl peptidase, L- ... from pGlu-peptides and pGlu-proteins". Proteins. 20 (1): 34-51. doi:10.1002/prot.340200106. PMID 7824521. Patti JM, Schneider A ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H (1992). "A thiocyanate hydrolase of Thiobacillus thioparus. A ... In enzymology, a thiocyanate hydrolase (EC 3.5.5.8) is an enzyme that catalyzes the chemical reaction thiocyanate + 2 H2O ⇌ {\ ... "Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... This enzyme is also called 4-aminoimidazole hydrolase. This enzyme participates in purine metabolism. It employs one cofactor, ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction (R)-pantetheine + H2O ...
Amino acids are made into proteins by being joined in a chain of peptide bonds. Each different protein has a unique sequence of ... These digestive enzymes include proteases that digest proteins into amino acids, as well as glycoside hydrolases that digest ... Proteins are made of amino acids arranged in a linear chain joined by peptide bonds. Many proteins are enzymes that catalyze ...
These design rules are being exploited for making specific peptides to act as tight inhibitors of target enzymes and potent ... "Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows ... He had developed the rules of peptide design with alpha, beta - dehydro - amino acids through extensive studies using syntheses ... "Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure- ...
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in ... A peptide with similar functionality was discovered in 2014 by group at Fudan University in Shanghai, China. This peptide also ... In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical ... Allen MD, Buchberger A, Bycroft M (Sep 2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". ...
The outbreak had been predicted a year earlier by noticing the increasing number of replikins, a type of peptide, found in the ... Neuraminidase is a type of glycoside hydrolase enzyme which helps to move the virus particles through the infected cell and ...
These non-peptide inhibitors can be more stable than inhibitors containing peptide bonds, because they will not be substrates ... Hydrolase 2.76, NPTase 2.09, Transferase 1.92, Lyase 1.59, Isomerase 1.51, Phosphodiesterase 1.50, Cytochrome p450 0.84, ... This will produce a set of peptides that can be analysed using a mass spectrometer. The peptide that changes in mass after ... The structure of ritonavir, a peptidomimetic (peptide mimic) protease inhibitor containing three peptide bonds, as shown in the ...
Examples of molecules taken up by enterocytes are: ions, water, simple sugars, vitamins, lipids, peptides and amino acids. ... which is a loose network composed of the oligosaccharide side chains of integral membrane hydrolases and other enzymes ... Paneth cells produce antimicrobial peptides such as human alpha-defensin. Microfold cells (commonly referred to as M cells) ... Näslund, Erik; Hellström, Per M. (10 September 2007). "Appetite signaling: from gut peptides and enteric nerves to brain". ...
Fumarylacetoacetate hydrolase domain-containing protein 1 FAM57B: Family with sequence similarity 57 member B FBRS: Probably ... encoding enzyme Peptide deformylase, mitochondrial PDPR: encoding protein Pyruvate dehydrogenase phosphatase regulatory subunit ...
A coordinate covalent bond is formed between the terminal peptide and a C=O group attached to zinc, which gives the carbon a ... such as hydrolases, ligases, transferases, oxidoreductases, and isomerases (42,43). Bitanihirwe BK, Cunningham MG (November ... Carboxypeptidase cleaves peptide linkages during digestion of proteins. ... "Molecular dynamics study of zinc binding to cysteines in a peptide mimic of the alcohol dehydrogenase structural zinc site". ...
They target the glycosidic bonds as well as the cross-linked peptides of the peptidoglycan matrix. The peptidoglycan matrix ... Kuroda A, Asami Y, Sekiguchi J (October 1993). "Molecular cloning of a sporulation-specific cell wall hydrolase gene of ... The amide linkages between stem peptide and lactyl moiety of muramoyl residue are cleaved by N-acetylmuramoyl-l-alanine ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
"Glycoside hydrolases". CAZypedia. Retrieved 2021-04-30. Frandsen TP, Svensson B (May 1998). "Plant alpha-glucosidases of the ... Otto B, Wright N (September 1994). "Trefoil peptides. Coming up clover". Current Biology. 4 (9): 835-8. doi:10.1016/S0960-9822( ... glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Other names in common use include creatinine hydrolase, and creatinine desiminase. This enzyme participates in arginine and ...
... disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene, Vps29, is a component of a large ... Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... In enzymology, a N-carbamoyl-D-amino acid hydrolase (EC 3.5.1.77) is an enzyme that catalyzes the chemical reaction N-carbamoyl ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
NaGly is an endogenous inhibitor of fatty acid amide hydrolase (FAAH) and thereby increases the ethanolamide endocannabinoids ... assigned to Peptide Technology Pty Ltd. and Women's and Children's Hospital Adelaide Prusakiewicz JJ, Kingsley PJ, Kozak KR, ...
Penicillin-binding proteins (DD-transpeptidases), in short PBPs, recognize the PG peptides and catalyze the cross-linking ... Turnover in Wild-Type and PG Hydrolase and Cell Division Mutants of Streptococcus pneumoniae D39 Growing Planktonically and in ... of PG peptide chains are labeled with FDAA. Published studies utilizing FDAAs as tools include: Visualizing bacterial cell wall ... resulting in their incorporation into the PG peptide chains. At proper concentration, e.g. 1-2 mM, FDAAs labeling does not ...
Glycoside hydrolases (or glycosidases), are enzymes that break glycosidic bonds. Glycoside hydrolases typically can act either ... Recent examples notably include high permeability of met-enkephalin analogs amongst other peptides. The full mOR agonist ... "glycoside hydrolases" are among the most common catalysis. The former often needs expensive materials and the later often shows ... and improve PK/PD thereof the active peptide beyond increasing CNS penetration. The innate utilization of sugars as ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Other names in common use include gamma-glutamyl-GABA hydrolase, PuuD, and YcjL. This enzyme participates in urea cycle and ... In enzymology, a gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) is an enzyme that catalyzes the chemical reaction 4 ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ... Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005). "Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP ... In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction allophanate + 3 H2O + ... Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast ...
Here we report the further characterization of acyl peptide hydrolase activity using mass spectrometry. Acyl peptide hydrolase ... In addition, by real-time PCR we found elevated acyl peptide hydrolase expression in brain areas rich in amyloid plaques ... These data suggest that acyl peptide hydrolase is involved in the degradation of oligomeric amyloid-beta, an activity that, if ... We previously reported the isolation of a novel amyloid-beta-degrading enzyme, acyl peptide hydrolase, a serine protease that ...
Peptide Fragments / analysis * Peptide Hydrolases / analysis * Proteoglycans / physiology * Prothrombin / analysis * Skin / ...
Peptide Hydrolases--metabolism. Publication Types: Lecture. Webcast Rights: This is a work of the United States Government. ... Information on the peptide recognition specificity is combined with filters to exclude potential cut sites that are buried in ... This method makes use of substrate phage display, in which a highly diverse peptide library is exposed to a protease. The ... substrate recognition specificity of a protease is derived from sequences of the cleaved peptides. ...
Peptide Hydrolases / metabolism Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Categories: Peptide Hydrolases Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, CopyrightRestricted ...
Peptide Hydrolases Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Peptide Hydrolases/genetics. *Peptide Hydrolases/metabolism. *Receptor, PAR-1/genetics. *Receptor, PAR-1/metabolism ...
MeSH Terms: Alkaline Phosphatase/analysis; Animals; Hyperplasia; Hypertrophy; Male; Peptide Hydrolases/metabolism; Pneumonia/ ...
Hydrolases [D08.811.277]. *Peptide Hydrolases [D08.811.277.656]. *Exopeptidases [D08.811.277.656.350]. *Carboxypeptidases [ ... "gamma-Glutamyl Hydrolase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "gamma-Glutamyl Hydrolase" by people in Harvard Catalyst ... Below are the most recent publications written about "gamma-Glutamyl Hydrolase" by people in Profiles. ...
Hydrolases: 639*Peptide Hydrolases: 7577*Serine Proteases: 3067*Serine Endopeptidases*Myeloblastin: 496 ... 06/15/2013 - "Generation of a metabolically stable form of this peptide (CR-AnxA1(2-50)), engineered by substituting a cleavage ... only high-avidity T cells underwent apoptosis when stimulated with high PR1 peptide concentration or when exposed to leukemia ...
The nanoparticles and peptide-ION complexes are analyzed with dynamic light scattering, zeta potential, and infrared ... This contribution focuses on the binding patterns of the peptide lasioglossin III from bee venom on bare IONs. Lasioglossin has ... Therefore, bare IONs are an interesting platform material for the development of drug-delivery carriers for cationic peptides. ... experiments performed on Escherichia coli show higher antimicrobial activity of bound lasioglossin than of the free peptide. ...
keywords = "Animals, Bacteria, Bacterial Infections, Host-Pathogen Interactions, Humans, Immunity, Innate, Peptide Hydrolases, ...
Peptide Hydrolases (1973-1974). Peptide Peptidohydrolases (1993). Public MeSH Note. 94; GELATINASE was indexed under PEPTIDE ... Hydrolases [D08.811.277] * Peptide Hydrolases [D08.811.277.656] * Endopeptidases [D08.811.277.656.300] * Metalloendopeptidases ... Hydrolases [D08.811.277] * Peptide Hydrolases [D08.811.277.656] * Metalloproteases [D08.811.277.656.675] * ... PEPTIDE HYDROLASES 1973-74. Online Note. use GELATINASES (NM) to search GELATINASE 1973-93. History Note. 94; was GELATINASE ( ...
3. 3CL hydrolase-based multiepitope peptide vaccine against SARS-CoV-2 using immunoinformatics.. Jakhar R; Kaushik S; Gakhar SK ... Immunoinformatics and Molecular Docking Studies Predicted Potential Multiepitope-Based Peptide Vaccine and Novel Compounds ...
Peptide Hydrolases Preferred Concept UI. M0016225. Registry Number. EC 3.4.-. Scope Note. Hydrolases that specifically cleave ... Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group ... Peptide Hydrolases [D08.811.277.656] * Aspartic Acid Proteases [D08.811.277.656.074] * ATP-Dependent Proteases [D08.811.277.656 ... Peptide Hydrolases Preferred Term Term UI T030870. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1966). ...
GSK1322322 (34) targets bacterial peptide deformylase, a metallo-hydrolase enzyme that catalyzes the removal of the formyl ... Leeds, J. A. & Dean, C. R. Peptide deformylase as an antibacterial target: a critical assessment. Curr. Opin. Pharmacol. 6, 445 ... In vivo characterization of the peptide deformylase inhibitor LBM415 in murine infection models. Antimicrob. Agents Chemother. ... Waites, K. B., Reddy, N. B., Crabb, D. M. & Duffy, L. B. Comparative in vitro activities of investigational peptide deformylase ...
Peptide Hydrolases,N0000005793, daclizumab,N0000005792, paramethasone acetate,N0000005791, xanthan gum,N0000005790, Benactyzine ... Peptides, Cyclic,N0000007875, Peptides,N0000007874, Cefamandole,N0000007873, Azepines,N0000007872, Nucleoproteins,N0000007871, ... Peptide Fragments,N0000011457, Viral Fusion Proteins,N0000011456, HIV Antigens,N0000011455, Viral Structural Proteins, ... Carboxylic Ester Hydrolases,N0000007513, Membrane Glycoproteins,N0000011432, ATP-Binding Cassette Transporters,N0000011431, P- ...
Peptide Hydrolases Entry term(s). Enzyme, Proteolytic Esteroproteases Hydrolase, Peptide Peptidase Peptidases Peptide Hydrolase ... Peptide hydrolases Entry term(s):. Enzyme, Proteolytic. Esteroproteases. Hydrolase, Peptide. Peptidase. Peptidases. Peptide ... Peptide Hydrolases - Preferred Concept UI. M0016225. Scope note. Hydrolases that specifically cleave the peptide bonds found in ... Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group ...
Peptide Hydrolases Preferred Concept UI. M0016225. Registry Number. EC 3.4.-. Scope Note. Hydrolases that specifically cleave ... Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group ... Peptide Hydrolases [D08.811.277.656] * Aspartic Acid Proteases [D08.811.277.656.074] * ATP-Dependent Proteases [D08.811.277.656 ... Peptide Hydrolases Preferred Term Term UI T030870. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1966). ...
Peptide Hydrolases 58% * Necrosis 53% * tert-Butylhydroperoxide 28% * Protease Inhibitors 20% * Liver Mitochondrion 12% ...
Peptide Hydrolases 29% * Epithelium 27% * Transcription Factors 26% * Stem Cells 26% * Insulin 24% ...
Peptide Hydrolase Inhibitor. Peptide Hydrolase Inhibitors. Peptide Peptidohydrolase Inhibitor. Peptide Peptidohydrolase ... Hydrolase Inhibitor, Peptide. Hydrolase Inhibitors, Peptide. Inhibitor, Endopeptidase. Inhibitor, Peptidase. Inhibitor, Peptide ... Inhibitors, Peptide Hydrolase. Inhibitors, Peptide Peptidohydrolase. Inhibitors, Protease. Peptidase Inhibitor. Peptidase ... Peptides sécrétoires inhibiteurs de peptidases. Peptides sécrétoires inhibiteurs de protéases. Peptides sécrétoires inhibiteurs ...
Peptide Hydrolases Medicine & Life Sciences 16% View full fingerprint Cite this. * APA ...
Peptide Hydrolases Proteomics Swine Substances Capsid Proteins Peptide Hydrolases PMID: 35891530. View Full Text ...
Furthermore, the lamellar bodies also contain enzymes such as acid hydrolases, including glucocerebrosidase, sphingomyelinase, ... and phospholipase A, as well as proteases and antimicrobial peptides [16].. In this study, we present a large cohort of 64 ...
Peptide Hydrolases 9% * Neoplasm Metastasis 7% * Polymerase Chain Reaction 6% * DNA 6% ...
Collagen-like antimicrobial peptides. Masuda, R., Kudo, M., Dazai, Y., Mima, T. & Koide, T., 2016 11月 4, In: Biopolymers. p. ... Cyclic Peptides for Efficient Detection of Collagen. Takita, K. K., Fujii, K. K., Kadonosono, T., Masuda, R. & Koide, T., 2018 ... Collagen-like cell-penetrating peptides. Yamazaki, C. M., Nakase, I., Endo, H., Kishimoto, S., Mashiyama, Y., Masuda, R., ... Cellular uptake of IgG using collagen-like cell-penetrating peptides. Masuda, R., Yamamoto, K. & Koide, T., 2016 1月 1, In: ...
  • We previously reported the isolation of a novel amyloid-beta-degrading enzyme, acyl peptide hydrolase, a serine protease that degrades amyloid-beta, and is different in structure and activity from other amyloid-beta-degrading enzymes. (biomedcentral.com)
  • A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. (nih.gov)
  • Enzymes that catalyze the degradation of collagen by acting on the peptide bonds. (nih.gov)
  • Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES . (nih.gov)
  • Several proteases were reported as capable of degrading the Aβ peptide. (biomedcentral.com)
  • PMID- 214395 TI - Chemical modification of peptide antibiotics : Part VII--Biological activity of derivatives of polymyxin B. PMID- 214396 TI - Temporal relations in phosphohydrolases of mouse testes. (nih.gov)
  • Here we report the further characterization of acyl peptide hydrolase activity using mass spectrometry. (biomedcentral.com)
  • These data suggest that acyl peptide hydrolase is involved in the degradation of oligomeric amyloid-beta, an activity that, if induced, might present a new tool for therapy aimed at reducing neurodegeneration in the Alzheimer's brain. (biomedcentral.com)
  • ACE is identical to "bradykininase", and captopril may also interfere with the degradation of the vasodepressor peptide, bradykinin. (nih.gov)
  • The abnormal accumulation of amyloid-beta peptide is believed to cause malfunctioning of neurons in the Alzheimer's disease brain. (biomedcentral.com)
  • Acyl peptide hydrolase cleaves the amyloid-beta peptide at amino acids 13, 14 and 19. (biomedcentral.com)
  • In addition, by real-time PCR we found elevated acyl peptide hydrolase expression in brain areas rich in amyloid plaques suggesting that this enzyme's levels are responsive to increases in amyloid-beta levels. (biomedcentral.com)
  • Lastly, tissue culture experiments using transfected CHO cells expressing APP751 bearing the V717F mutation indicate that acyl peptide hydrolase preferentially degrades dimeric and trimeric forms of amyloid-beta. (biomedcentral.com)
  • Alzheimer's disease (AD) is a neurodegenerative disorder resulting from the pathological processing of APP that leads to the accumulation of amyloid-beta (Aβ) peptide, neuronal loss, synaptic dysfunction, inappropriate levels of neurotransmitters, and finally, to irreversible and progressive memory loss. (biomedcentral.com)
  • This contribution focuses on the binding patterns of the peptide lasioglossin III from bee venom on bare IONs. (mdpi.com)
  • The substrate recognition specificity of a protease is derived from sequences of the cleaved peptides. (nih.gov)
  • A brief review considered selected genetic variants and associated diseases such as red blood cell traits and predisposure to acute hemolytic anemia for persons with glucose-6-dehydrogenase deficiency, the occurrence of sickle cell anemia in individuals having a specific change in the amino acid structure of the peptide chains of hemoglobin, and the occurrence of thalassemia major due to a genetic defect in the rate of hemoglobin synthesis. (cdc.gov)
  • This method makes use of substrate phage display, in which a highly diverse peptide library is exposed to a protease. (nih.gov)
  • gamma-Glutamyl Hydrolase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • Genetic traits associated with lung diseases include increased aryl- hydrocarbon-hydrolase activity associated with bronchogenic carcinoma, and alpha-1-antitrypsin deficiency associated with obstructive pulmonary disease, particularly emphysema. (cdc.gov)
  • This method makes use of substrate phage display, in which a highly diverse peptide library is exposed to a protease. (nih.gov)
  • The substrate recognition specificity of a protease is derived from sequences of the cleaved peptides. (nih.gov)
  • Information on the peptide recognition specificity is combined with filters to exclude potential cut sites that are buried in the interior of the protein, or that are not expressed in the same tissue or sub-cellular location as the protease, to predict the putative physiologic and pathophysiologic substrates. (nih.gov)
  • Food processing can also generate N-alpha-acetylated proteins and peptides. (nih.gov)
  • Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES . (bvsalud.org)
  • A brief review considered selected genetic variants and associated diseases such as red blood cell traits and predisposure to acute hemolytic anemia for persons with glucose-6-dehydrogenase deficiency, the occurrence of sickle cell anemia in individuals having a specific change in the amino acid structure of the peptide chains of hemoglobin, and the occurrence of thalassemia major due to a genetic defect in the rate of hemoglobin synthesis. (cdc.gov)
  • Migraine is a complex and highly disabling neurological disease whose treatment remains challenging in many patients, even after the recent advent of the first specific-preventive drugs, namely monoclonal antibodies that target calcitonin gene-related peptide. (medscape.com)
  • Genetic traits associated with lung diseases include increased aryl- hydrocarbon-hydrolase activity associated with bronchogenic carcinoma, and alpha-1-antitrypsin deficiency associated with obstructive pulmonary disease, particularly emphysema. (cdc.gov)
  • The surgical procedures include Billroth-I, Billroth-II, and Roux-en-Y gastric bypass. (medscape.com)

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