| dipeptidyl peptidase | A hydrolase occurring in two forms: Dipeptidyl peptidase I, dipeptidyl transferase, cleaving dipeptides from the amino end of polypeptides, dipeptidyl peptidase II, with properties similar to those of I, has a different specificity. (05 Mar 2000) |
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| dipeptidyl peptidases | <enzyme> Dipeptidylpeptide hydrolases. Enzymes which cleave dipeptides from the amino terminal of a polypeptide. Dipeptidyl peptidase I, II, III, IV are known. They hydrolyze the beta-naphthylamides of glycine-arginine, lysine-alanine, arginine-arginine and glycine-proline, respectively. Dipeptidyl peptidase I is cathepsin c. Registry number: EC 3.4.14. (12 Dec 1998) |
| atrial dipeptidyl carboxyhydrolase | <enzyme> Removes c-terminal phe-arg from atriopeptin II to give atriopeptin i; metalloenzyme with mw 240,000; also has tripeptidyl carboxyhydrolase activity; removes phe-arg-tyr from atriopeptin III to form atriopeptin i Registry number: EC 3.4.15.- (26 Jun 1999) |
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| PepX dipeptidyl aminopeptidase | <enzyme> Isolated from lactococcus lactis Registry number: EC 3.4.14.- Synonym: x-prolyl dipeptidyl aminopeptidase pepx (26 Jun 1999) |
| dipeptidyl carboxypeptidase | <enzyme> Hydrolytically removes dipeptides from the carboxyl end of low- and high-mol wt peptides Registry number: EC 3.4.15.- Synonym: dipeptidocarboxypeptidase, peptidyl-dipeptidase dcp (26 Jun 1999) |
| dipeptidyl transferase | Cleaving dipeptides from the amino end of polypeptides. See: dipeptidyl peptidase. (05 Mar 2000) |
| alkaline D-peptidase | <enzyme> A penicillin-recognizing enzyme from bacillus cereus; has beta-lactamase activity; genbank d86380 Registry number: EC 3.4.99.- Synonym: ADP gene product, alkaline d-stereospecific endopeptidase (26 Jun 1999) |
| aspartyllysine peptidase | <enzyme> From human intestinal brush border; stabilised by zn+2 Registry number: EC 3.4.13.- Synonym: zn-stable aspartyllysine peptidase (26 Jun 1999) |
| C5a peptidase | <enzyme> Streptococcus pyogenes enzyme inactivates complement 5a by cleaving at lysine 68, removing a six-amino acid fragment Pharmacological action: complement inactivators Registry number: EC 3.4.99.- Synonym: streptococcus c5a peptidase, gbs c5a-ase, group b streptococci c5a-ase, scpa protein (26 Jun 1999) |
| matrix processing peptidase | <enzyme> From matrix fraction of rat liver mitochondria; cleaves mitochondrial protein precursors; inhibited by metal chelators and reactived by mn2+; classified as EC 3.4.24.64 Registry number: EC 3.4.24.- Synonym: mitochondrial processing peptidase, mitochondrial processing protease, alpha-mpp, beta-mpp, p-52 protein, rat, p-55 protein, rat, mas1 protein, yeast, mas2 protein, yeast (26 Jun 1999) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| peptidase P | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
| mitochondrial intermediate peptidase | <enzyme> Removes the octapeptide from the amino terminus of the intermediate protein processed from the protein precursor of certain mitochondrial proteins by the mitochondrial processing peptidase; smip from schizophyllum commune; rmip from rat; ymip from saccharomyces cerevisiae Registry number: EC 3.4.24.59 Synonym: mip peptidase, smip peptidase, rmip peptidase, ymip peptidase (26 Jun 1999) |
| procollagen peptidase | <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome. (18 Nov 1997) |
| pyroglutamyl-peptidase I | <enzyme> An enzyme that catalyses the release of a n-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. Registry number: EC 3.4.19.3 (12 Dec 1998) |
| PZ-PLGPA peptidase | <enzyme> Endopeptidase from treponema denticola Registry number: EC 3.4.21.- (26 Jun 1999) |