3.4.13.9: Xaa-Pro dipeptidase
This is an abbreviated version!
For detailed information about Xaa-Pro dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.9
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3.4.13.9
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collagen
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dipeptides
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ulcer
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hydroxyproline
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gly-pro
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opaas
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soman
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exopeptidase
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proline-containing
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prolinase
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map-kinases
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paraoxonase
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dfp
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igf-ir
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alteromonas
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erk1
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splenomegaly
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sarin
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medicine
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beta1-integrin
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analysis
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diagnostics
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drug development
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degradation
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biotechnology
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food industry
- 3.4.13.9
- collagen
- dipeptides
- ulcer
- hydroxyproline
- gly-pro
-
opaas
- soman
-
exopeptidase
-
proline-containing
- prolinase
-
map-kinases
- paraoxonase
- dfp
- igf-ir
- alteromonas
- erk1
-
splenomegaly
- sarin
- medicine
- beta1-integrin
- analysis
- diagnostics
- drug development
- degradation
- biotechnology
- food industry
Reaction
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro =
Synonyms
clan MG aminopeptidase P-like metallopeptidase, dipeptidase, proline, DPP8, EC 3.4.3.7, gamma-peptidase, imidodipeptidase, LGAS_0712, M24B peptidase, More, MP50, OPAA, OPAA-2, organophosphate acid anhydrolase, organophosphate anhydrolase/prolidase, organophosphorus acid anhydrolase, PepD, PepE, PepI, PepQ, peptidase D, peptidase-Q, PepX, Pf-peptidase, Pfprol, PH0974, PH1149, Ph1prol, Phprol, PLD, post-proline-cleaving aminopeptidase, prolidase, prolidase homolog 1, prolidase homolog 2, prolidase I, prolidase II, Proline dipeptidase, proline iminopeptidase, proline-specific amino dipeptidase, prolyl dipeptidase, PRS, QPP, quiescent cell proline dipeptidase, serum prolidase, X-Pro dipeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro dipeptidase, XPD, XPD43, XPP
ECTree
3.4.13.9 Xaa-Pro dipeptidaseAdvanced search results
results (
results (Organism
Organism on EC 3.4.13.9 - Xaa-Pro dipeptidase
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ORGANISM 
COMMENTARY 
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Oenococcus oeni is the principal microorganism responsible for the malolactic fermentation, which decreases total acidity and improves the quality and stability of wine, strain IOEB 8413, gene pepQ
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Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 / 700860D-5
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36083, 36086, 36088, 36089, 36092, 36097, 36098, 36101, 36104, 36105, 36111, 683964, 698356, 698650, 700612
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36084, 36085, 36087, 36090, 36106, 36107, 36112, 36113, 36115, 651190, 651194, 651779, 652035, 652676, 653207, 667127, 667803, 668109, 670953, 679283, 680724, 683061, 683216, 683227, 683405, 683457, 683557, 683569, 683612, 683868, 683919, 683964, 695528, 695908, 695969, 697476, 697568, 697758, 699153, 699184, 700612, 707010, 707038, 707288
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comparison of isoforms prolidase I and prolidase II and isoform from patient with enzyme deficiency
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expression in Saccharomyces cerevisiae, bifunctional enzyme with both dipeptidase and organophosphorus acid anhydrolase activity
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healthy pregnant women and pregnant women with intrauterine growth restricted infants
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regulation of enzyme activity and collagen biosynthesis may involve beta1-integrin-dependent signaling
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Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 / 700860D-5
PH0974 or PepQ; gene pepQ, isozyme PH0974 or PepQ
UniProt
Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 / 700860D-5
PH1149 or PepQ; isozyme PH1149
UniProt
