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
-
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
- 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 (Natural Substrates Products
Natural Substrates Products on EC 3.4.13.9 - Xaa-Pro dipeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
melphalan + H2O
?
-
prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
prophalan-D + H2O
?
-
the D-proline prodrug of melphalan, bioactivation and uptake of prolidase-targeted proline prodrugs, prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
prophalan-L + H2O
?
-
the L-proline prodrug of melphalan, bioactivation and uptake of prolidase-targeted proline prodrugs, prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism, enzyme activity is regulated through the beta1 integrin receptor
-
?
additional information
?
-
-
the enzyme plays an important role in recycling of proline for collagen synthesis and cell growth, regulation by phosphorylation and dephosphorylation
-
?
additional information
?
-
-
alpha-ketoglutarate increases activities of prolidase, which is known to play an important role in collagen metabolism, in fibroblasts, N-benzyloxycarbonyl-L-proline, a prolidase inhibitor, inhibits procollagen synthesis by alpha-ketoglutarate in fibroblasts, alpha-ketoglutarate diminishes UVB-induced wrinkle formation by increasing collagen production, through a pathway that involves prolidase activation, regulation, overview
-
-
?
additional information
?
-
-
interleukin-1beta action and inhibition, resulting in increase in beta1-integrin receptor, NF-kappaB expressions, and increase in phosphorylation of FAK, does deregulate the collagen metabolism, but does not influence the prolidase activity, while metalloproteinase MMP-2 and MMP-9 activities are activated, overview
-
-
?
additional information
?
-
-
prolidase deficiency causes a rare autosomal recessive disease, characterized by a wide range of clinical outcomes, including severe skin lesions, mental retardation, and infections of the respiratory tract
-
-
?
additional information
?
-
-
prolidase is involved in the final stage of degradation in collagen catabolism
-
-
?
additional information
?
-
-
prolidase plays an important role in enhancement of collagen biosynthesis at post-translational level
-
-
?
additional information
?
-
-
prolidase, a specific iminopeptidase involved in collagen turnover, is especially active in growing tissues, the final step of collagen degradation is mediated by prolidase, the cytosolic enzyme specifically splits iminopeptides with C-terminal proline or hydroxyproline, which together contribute 21% of collagen
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step of collagen degradation and plays an important role in collagen biosynthesis
-
-
?
additional information
?
-
-
the enzyme is relevant in the latest stage of protein catabolism, particularly of those molecules rich in imino acids such as collagens, thus being involved in matrix remodelling, overview, prolidase has an antitoxic effect against some organophosphorus molecules, can be used in dietary industry as bitterness reducing agent and is used as target enzyme for specific melanoma prodrug activation, prolidase deficiency is a rare recessive disorder caused by mutations in the prolidase gene and characterized by severe skin lesions, overview
-
-
?
additional information
?
-
-
the enzyme plays an important role in the recycling of proline from imidodipeptides, mostly derived from degradation products of collagen, for resynthesis of collagen and other proline-containing proteins, prolidase-dependent regulation of collagen biosynthesis, pathogenic mechanisms in enzyme deficiency, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
PepQ is a cytoplasmic prolidase that specifically liberated proline from dipeptides with increased activity under high salt conditions, PepX, a X-prolyl-dipeptidyl aminopeptidase, and PepI, a iminopeptidase, are unaffected, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
lack of prolidase I leads to prolidase deficiency, a disease characterized by intractable skin lesions, recurrent respiratory infections, and mental retardation, physiologic roles of prolidase isoenzymes, PD I functions by way of an intestinal peptide carrier, which may be regulated by the uptake of various iminodipeptides, intestinal PD II also participates in absorption of proline and other amino acids early in life, overview
-
-
?
additional information
?
-
-
prolidase plays an important role in collagen biosynthesis
-
-
?
