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  • procollagen peptidase
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  • peptidase
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  • metal peptidase
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  • peptidase
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  • peptidase
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  • thyroidal protease and peptidase
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  • thyroidal protease peptidase
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  • cysteine peptidase
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  • peptidase
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ACE Angiotensin Converting Enzyme
  = Kininase II
  = Dipeptidyl Carboxypepti...
LAP   1) Leukocyte Alkaline Phosphatase
  2) Leucine Amino-Peptidase
PEP peptidase; phospho(enol)pyruvate; peer evaluation program; phosphoenolpyruvate; pigmentation, edema,...
Pep peptidase
PEPA peptidase A
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DP IV Dipeptidyl Peptidase IV
DPP IV Dipeptidyl Peptidase IV
DPP Dipeptidyl peptidase
DPPI Dipeptidyl peptidase I
DPP II Dipeptidyl peptidase II
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
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)
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)
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 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)
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)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Dipeptidyl Peptidase I - »õâ A cysteine-type peptidase that is CHLORINE dependent and functions maximally at acidic pHs. At neutral pH, it polymerizes esters, aryl- and dipeptide amides. EC 3.4.14.1.
    Synonyms : Dipeptidyl Transferase, Aminopeptidase I, Dipeptidyl, C, Cathepsin, I, Dipeptidyl Aminopeptidase, I, Dipeptidyl Peptidase, Peptidase I, Dipeptidyl, Transferase, Dipeptidyl
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