| peptidyl leukotrienes | Leukotrienes having amino acids present (even single amino acids) although not true peptides; e.g., LTC4 is an S-substituted glutathione, LTD4 is an S-substituted cysteinylglycine, LTE4 is an S-substituted cysteine, and LTF4 (also known as gamma-glutamyl-LTE4) is an S-substituted gamma-glutamylcysteine. (05 Mar 2000) |
|---|---|
| peptidyl prolyl cis trans isomerase | See: PPIase and immunophilin. (18 Nov 1997) |
| peptidyl-Asp metalloendopeptidase | <enzyme> Extracellular metalloproteinase secreted by a pseudomonas fragi mutant; partial amino acid sequence given in first source Registry number: EC 3.4.24.33 Synonym: endopeptidase asp-n (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) |
| peptidyl-Lys metalloendopeptidase | <enzyme> From lysobacter enzymogenes; cleaves at the carboxyl side of lysine residues; active at pH 9;endoproteinase lys-c (EC 3.4.99.30) was combined with EC 3.4.24.20 in 1992 enzyme nomenclature Registry number: EC 3.4.24.20 Synonym: endoprotease lys-c, endopeptidase lys-c, endoproteinase lys-c, lysc protease (26 Jun 1999) |
| peptidylamidoglycolate lyase | <enzyme> Second step in the production of alpha-amidated peptides from their glycine-extended precursors; first step is EC 1.14.17.3 (amide synthetase) Registry number: EC 4.3.2.5 Synonym: pahgaa lyase, peptidyl-alpha-hydroxyglycine alpha amidating lyase, peptidylhydroxyglycine n-c lyase (26 Jun 1999) |
| peptidylglycine monooxygenase | <enzyme> Forms alpha-amide from c-terminal glycine precursor of peptide hormones by oxidation of hydrogen and spontaneous hydrolysis of resulting imino linkage; may be the same as bovine somatotropin Registry number: EC 1.14.17.3 Synonym: peptide amide synthetase, alpha-amidation monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, substance p-gly12 amidating enzyme, peptidyl glycine alpha-amidase, alpha-amidating enzyme ae-ii, peptidyl alpha-amidating monooxygenase, amide synthetase, substance p alpha-amidating enzyme, peptidylglycine hydroxylase, peptidylglycine alpha-hydroxylating monooxygenase, peptidylglycine alpha-amidating monooxygenase, pam protein, pam-3 protein (26 Jun 1999) |
| peptidylprolyl isomerase | <enzyme> An enzyme that catalyses the isomerization of proline residues within proteins. Chemical name: Peptidylproline cis-trans-isomerase Registry number: EC 5.2.1.8 (12 Dec 1998) |
| peptidyltransferase | <enzyme> An enzyme that catalyses the transfer of aminoacyl-trna to formyl-methionine-trna or peptidyl-trna during peptide chain elongation. It is a part of the 50 s (bacteria) and 60 s (eukaryotes) ribosomal subunits. Integral enzymic activity of the large subunit of a ribosome, catalysing the formation of a peptide bond between the carboxy terminus of the nascent chain and the amino group of an arriving tRNA associated amino acid. Chemical name: Peptidyl-tRNA:aminoacyl-tRNA N-peptidyltransferase Registry number: EC 2.3.2.12 (12 Dec 1998) |