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  • peptidyl transferase
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  • peptidyl-tRNA
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  • peptidyldipeptide hydrolase
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  • peptidyl site
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  • peptidyl transferase
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  • peptidyl transferase center
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  • peptidyl-puromycin
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  • peptidyl-tRNA
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  • peptidyl-tRNA site
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PAL pathology laboratory; peptidyl-alpha-hydroxyglycine alpha-amidating lysine phase alteration plane; p...
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PPI Peptidyl prolyl cis-trans-isomerase
PPIase Peptidyl-prolyl cisltrans isomerase
PPIases Peptidyl-prolyl isomerases
DPP IV di-peptidyl-aminopeptidase IV
PCP peptidyl carrier protein
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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)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 3 ÆäÀÌÁö: 1
  • Peptidyl Transferases - »õâ Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.
    Synonyms : Peptidyltransferases, Transferases, Peptidyl, Translocases, Peptidyl
  • Peptidyl-Dipeptidase A - »õâ 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.
    Synonyms : Angiotensin I-Converting Enzyme, Carboxycathepsin, Dipeptidyl Peptidase A, Kininase A, Angiotensin I Converting Enzyme, Peptidyl Dipeptidase A
  • Peptidylprolyl Isomerase - »õâ An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
    Synonyms : Proline Isomerase, Proline Rotamase, Isomerase, Peptidylprolyl, Isomerase, Proline, Isomerase, Prolyl, Peptidyl Prolyl cis trans Isomerase, Rotamase, Proline, cis-trans-Isomerase, Peptidyl-Prolyl
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peptidyl-dipeptidase (pep
Ãâó: www.mercksource.com/pp/us/cns/cns_hl_dorlands.jspz...
peptidyl-dipeptidase A (pep
Ãâó: www.mercksource.com/pp/us/cns/cns_hl_dorlands.jspz...
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