| proline dipeptidase | <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) |
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| gamma-glutamyl dipeptidase | <enzyme> Removes glycine from leukotriene d4 to form leukotriene e4 Registry number: EC 3.4.13.- (26 Jun 1999) |
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| glycylprolyl dipeptidase | <enzyme> From b gingivalis; cleaves gly-pro dipeptides from native, partially digested type I collagen; a serine protease Registry number: EC 3.4.14.- Synonym: glycylprolyl protease (26 Jun 1999) |
| membrane dipeptidase | <enzyme> Renal dipeptidase which metabolises thienamycin and related carbapenem antibiotic Registry number: EC 3.4.13.19 Synonym: dehydropeptidase-i, dehydropeptidase I, microsomal dipeptidase (26 Jun 1999) |
| peptidyl-dipeptidase A | <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) |
| Met-enkephalin heptapeptide dipeptidase | <enzyme> Enzyme from rabbit ear artery forms met-enkephalin from met(5)-enkephalin-arg(6)-phe(7); inhibited by captopril Registry number: EC 3.4.15.- Synonym: met-enkephalin-arg(6)-phe(7) cleavage enzyme, me-ap dipeptidase (26 Jun 1999) |
| methionyl dipeptidase | A hydrolase catalyzing the hydrolysis of an l-methionyl-amino acid to l-methionine and an amino acid. (05 Mar 2000) |
| cytosol non-specific dipeptidase | <enzyme> Also referred to as peptidase a (see synonym to penicillopepsin, EC 3.4.23.20) Registry number: EC 3.4.13.- Synonym: glycyl-l-leucine hydrolase, glycylleucine dipeptidase, gly-leu dipeptide peptidase, dipeptide hydrolase, glycyl-leucine dipeptidase (26 Jun 1999) |
| prolylglycine dipeptidase | prolyl dipeptidase |
| N-acetylated-alpha-linked acidic dipeptidase | <enzyme> Chloride-dependent membrane bound metallopeptidase, most active with the endogenous neuropeptide n-acetyl-l-aspartyl-l-glutamate Registry number: EC 3.4.13.- Synonym: naaladase, glutamate carboxypeptidase II, prostate-specific membrane antigen, psm antigen (26 Jun 1999) |
| non-stereospecific dipeptidase | <enzyme> Hydrolyzes d- or l-amino acid peptides from the brain of cephalopods Registry number: EC 3.4.13.17 Synonym: peptidyl-d-amino acid hydrolase (26 Jun 1999) |
| dipeptidase | <enzyme> Cleave preferentially hydrophobic dipeptides; from various bacterial and mammalian sources Registry number: EC 3.4.13.11 Synonym: renal dipeptidase (26 Jun 1999) |
| kyotorphin I dipeptidase | <enzyme> Responsible for the major kyotorphin-degrading activity in the soluble fraction of rat brain Registry number: EC 3.4.13.- Synonym: kyotorphin I hydrolyzing enzyme, tyrosyl-arginine dipeptidase, ktpase I, kyotorphin (l-tyr-l-arg)-hydrolyzing peptidase, ktpase (26 Jun 1999) |
| leukotriene D4 dipeptidase | <enzyme> Converts leukotriene d4 to leukotriene e4 Registry number: EC 3.4.13.- Synonym: ld4 dipeptidase (26 Jun 1999) |
| procollagen-proline dioxygenase | <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of a prolyl-glycyl-containing-peptide, usually in protocollagen, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilises molecular oxygen with a concomitant oxidative decarboxylation of 2-oxoglutarate to succinate. Chemical name: Procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase Registry number: EC 1.14.11.2 (12 Dec 1998) |
| proline | <amino acid> One of the 20 amino acids directly coded for in proteins. Structure differs from all the others, in that its side chain is bonded to the nitrogen of the _ amino group, as well as the _ carbon. This makes the amino group a secondary amine and so proline is described as an imino acid. Has strong influence on secondary structure of proteins and is much more abundant in collagens than in other proteins, occurring especially in the sequence glycine proline hydroxyproline. A proline rich region seems to characterise the binding site of SH3 domains. (18 Nov 1997) |