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Information on EC 3.4.11.9 - Xaa-Pro aminopeptidase
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3.4.11.9 Xaa-Pro aminopeptidaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
Synonyms
xpnpep2, membrane-bound app, xpnpep3, xpnpep1, appro, x-prolyl-dipeptidyl aminopeptidase, tvmp50, hcampp, x-prolyl aminopeptidase, tgapp, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase P
aminopeptidase P1
AMPP
AP-P
APP
APP1
APPro
Dr-smAPP
Icp55
M24B peptidase
Mt-smAPP
PEPP
PepQ
peptidase PepQ
PepX aminopeptidase
small aminopeptidase-P
TgAPP
X-Pro aminopeptidase
X-prolyl aminopeptidase
X-prolyl aminopeptidase 2
X-prolyl aminopeptidase 3
XpmA
XPNPEP1
XPNPEP2
XPNPEP3
YpdF
additional information
additional information
-
the enzyme belongs to the peptidase family M24
additional information
the enzyme belongs to the peptidase family M24
additional information
the enzyme belongs to the peptidase family M24
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
-
-
-
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
acive site configuration, modeling, Asp449, Asp460, His523, Glu554, and Glu568 are in volved in metal binding in the active site, His429 and His523 are involved in shuttling protons during catalysis
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
isozyme APP-2 shows a preference for Arg-Pro-Pro-, Arg-Pro-Lys-, Pro-Pro-Gly-, -Phe-Gly- in descending order
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
H243 stabilizes substrate binding, H361 stabilizes substrate binding and the gem-diol catalytic intermediate. H350 forms part of a hydrophobic binding pocket that gives the enzyme its proline specificity
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
R404 participates in proton relay and in the hydrogen bond network
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
Escherichia coli B / ATCC 11303
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
37288-66-7
-
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SUBSTRATE
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
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
bradykinin + H2O
Arg + PPGFSPFR
i.e. RPPGFSPFR, rapid hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
des-Arg-bradykinin + Arg
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
centrosomal protein 290 kDa/NPHP6 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
?
FPHFD + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methyl-7-coumarylamide
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
?
Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Gly + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ala-L-Pro-L-Ala-2-naphthylamide + H2O
L-Ala-L-Pro-L-Ala + 2-naphthylamine
-
-
?
L-Ala-L-Pro-p-nitroanilide + H2O
L-Ala-L-Pro + p-nitroaniline
-
-
?
L-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ala + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Arg + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asn-L-Pro-L-Thr-L-Asn-L-Leu-L-His + H2O
L-Asn + L-Pro-L-Thr-L-Asn-L-Leu-L-His
-
-
-
?
L-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-ASn + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Asp + Pro-7-amido-4-carbamoylmethylcoumarin
-
low activity
-
?
L-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Gln + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Glu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-His + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ile + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Leu 7-amido-4-carbamoylmethylcoumarin + H2O
L-Leu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Met + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Nle-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Nle + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Phe + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Pro + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides
-
?
L-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ser + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Trp + Pro-7-amido-4-carbamoylmethylcoumarin
-
best substrate
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
leucine rich repeat containing 50 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
Nalpha-(2-aminobenzoyl)-Lys-Pro-Pro 4-nitroanilide + H2O
Nalpha-(2-aminobenzoyl)-Lys + Pro-Pro-4-nitroanilide
-
-
?
papain + H2O
?
-
reduced and carboxymethylated, with the N-terminal sequence Ile-Pro-Glu-Tyr-Val
-
?
substance P + H2O
Arg + PKPQQFFGLM
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
YPWTQ + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
-
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
-
-
?
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
i.e. bradykinin
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
i.e. bradykinin
one Arg is released per mol of bradykinin in less than 5 min, the following Pro residue is released within 1 h
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
bradykinin + H2O
?
-
potential natural substrate, efficiently hydrolyzed by PfAPP
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
i.e. RPPGFSPFR, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PPGFSPFR
?
bradykinin + H2O
Arg + des-Arg-bradykinin
i.e. RPPGFSPFR, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PPGFSPFR
?
bradykinin + H2O
Arg + des-Arg-bradykinin
hydrolysis of the N-terminal Arg1-Pro bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
enzyme activity in plasma of humans with previous angio-oedema, a rare but potentially life-threatening side-effect of angiotensin-converting enzyme inhibitor treatment, is low compared to humans without this sensitivity and might be a predisposing factor for development of angio-oedema
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
the enzyme contributes to the degradation of bradykinin in human skin, especially in case of angiotensin-converting enzyme inhibition
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Streptococcus thermophilus ACA DC 0022
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Streptococcus thermophilus ACA-DC 0022
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
best substrate
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
best substrate
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
-
best substrate
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
?
substance P + H2O
Arg + des-Arg-substance P
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PKPQQFFGLM
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
?
additional information
?
-
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
?
additional information
?
-
-
the enzyme favors peptides with 2 proline residues or proline analogs in position 2 and 3 of the substrate
-
?
additional information
?
-
-
enzyme may be important for the modulation of the biological activity of neuropeptides
-
?
additional information
?
-
-
the enzyme is involved in the pulmonary inactivation of circulating bradykinin
-
?
additional information
?
-
-
the enzyme may have an important role in the pulmonary degradation of the potent vasoactive peptide, bradykinin
-
?
additional information
?
-
-
no activity with angiotensin I, des-Arg-bradykinin, AF1, i.e. KNEFIRNRVYIHPFHL, and substance P
-
?
additional information
?
-
enzyme APP specifically cleaves the N-terminal Xaa-Pro peptide bond from oligopeptides and is distinct from prolidase, which acts only on dipeptides
-
?
additional information
?
-
-
enzyme APP specifically cleaves the N-terminal Xaa-Pro peptide bond from oligopeptides and is distinct from prolidase, which acts only on dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
-
the enzyme can only hydrolyze the trans form of the X-L-Pro-peptide bond, the cis form has to isomerize before it can be cleaved
-
?
additional information
?
-
-
enzyme hydrolyzes the Xaa-Pro peptide bond when the first amino acid is Asn, Ala, or Met
-
?
additional information
?
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
?
additional information
?
-
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
?
additional information
?
-
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
no activity with Gly-Pro-hydroxyPro
-
?
additional information
?
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
?
additional information
?
-
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
?
additional information
?
-
-
the enzyme removes the N-terminal amino acid from peptides only where Pro, and in one case Ala, is present in the penultimate position. No hydrolysis of dipeptides even when Pro is present in the C-terminal position or when either N-termial Pro or pyroglutamate is present preceeding a Pro residue in the penultimate position of longer peptides
-
?
additional information
?
-
-
aminopeptidase P appears to be an important enzyme for debittering of casein-derived peptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
?
additional information
?
-
-
the enzyme releases only amino acid X from the NH2-termini of peptides with the general structure X-Pro-Y-Z
-
?
additional information
?
-
specific role in the catabolism of proline-containing peptides in both the vacuole and the cytosol, enzyme is required for efficient parasite proliferation
-
?
additional information
?
-
-
substrate specificity, overview. Design and synthesis of a library composed of 20 fluorogenic substrates, which is used to determine the substrate fingerprint of mature PfAPP (PfAPP, residues 121-777). The enzyme from Plasmodium falciparum can catalyze the removal of any residue immediately prior to a proline. The coupled assay uses a prolyl iminopeptidase (EC 3.4.11.5) to release the free 7-amino-4-carbamoylmethylcoumarin for fluorogenic detection
-
?
additional information
?
-
modeling of the Val-Pro-Leu bound Pa-PepP complex by superposing Pa-PepP structure with the substrate-bound Escherichia coli PepP structure (PDB ID 2BN7)
-
?
additional information
?
-
-
the enzyme liberates all unblocked preferentially basic or hydrophobic ultimate amino acids from dipeptides, tripeptides and oligopeptides with N-terminal Xaa-Pro- sequences, overview
-
?
additional information
?
-
-
the enzyme accounts for virtually all of the pulmonary inactivation of bradykinin injected in vitro
-
?
additional information
?
-
-
the enzyme probably plays an important role in conjunction with other intestinal prolyl peptidases in the digestion of proline containing peptides and proteins
-
?
additional information
?
-
-
the enzyme plays an important role in hydrolysis of Xaa-Pro-Yaa peptides
-
?
additional information
?
-
-
the enzyme participates in the myocardial kinin metabolism to the same extent as angiotensin-converting enzyme, APP inhibition leads to a reduction in myocardial infarct size by the bradykinin-dependent pathway, synergistic with inhibition of angiotensin-converting enzyme, overview
-
?
additional information
?
-
the enzyme is active towards substrates with proline at P1' position (M-/-PA and Y-/-PA). Icp55 cleaves off bulky residues from N-termini of proteins. Active towards substrates Y-/-AA, Y-/-TA and Y-/-SA
-
?
additional information
?
-
-
the enzyme is active towards substrates with proline at P1' position (M-/-PA and Y-/-PA). Icp55 cleaves off bulky residues from N-termini of proteins. Active towards substrates Y-/-AA, Y-/-TA and Y-/-SA
-
?
additional information
?
-
the enzyme is active towards substrates with proline at P1' position (M-/-PA and Y-/-PA). Icp55 cleaves off bulky residues from N-termini of proteins. Active towards substrates Y-/-AA, Y-/-TA and Y-/-SA
-
?
additional information
?
-
-
the enzyme is involved in degradation of peptide intermediates
-
?
additional information
?
-
systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
-
?
additional information
?
-
systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
-
?
additional information
?
-
-
systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
-
?
additional information
?
-
aminopeptidase P catalyzes the cleavage of the first amino acid residue in peptides and proteins when it is followed by the proline residue. PepP is able to hydrolyze the Xaa-Pro-bond and belongs to the family of proline-specific aminopeptidases. Substrate specificity, overview
-
?
additional information
?
-
-
X-prolyl aminopeptidase (APP) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of N-terminal amino acid present adjacent to a penultimate proline residue
-
?
additional information
?
-
-
X-prolyl aminopeptidase (APP) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of N-terminal amino acid present adjacent to a penultimate proline residue
-
?
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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
bradykinin + H2O
?
-
potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
FPHFD + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
YPWTQ + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
enzyme activity in plasma of humans with previous angio-oedema, a rare but potentially life-threatening side-effect of angiotensin-converting enzyme inhibitor treatment, is low compared to humans without this sensitivity and might be a predisposing factor for development of angio-oedema
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
the enzyme contributes to the degradation of bradykinin in human skin, especially in case of angiotensin-converting enzyme inhibition
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
-
?
additional information
?
-
-
enzyme may be important for the modulation of the biological activity of neuropeptides
-
-
?
additional information
?
-
-
the enzyme is involved in the pulmonary inactivation of circulating bradykinin
-
-
?
additional information
?
-
-
the enzyme may have an important role in the pulmonary degradation of the potent vasoactive peptide, bradykinin
-
-
?
additional information
?
-
-
aminopeptidase P appears to be an important enzyme for debittering of casein-derived peptides
-
-
?
additional information
?
-
specific role in the catabolism of proline-containing peptides in both the vacuole and the cytosol, enzyme is required for efficient parasite proliferation
-
-
?
additional information
?
-
-
the enzyme accounts for virtually all of the pulmonary inactivation of bradykinin injected in vitro
-
-
?
additional information
?
-
-
the enzyme probably plays an important role in conjunction with other intestinal prolyl peptidases in the digestion of proline containing peptides and proteins
-
-
?
additional information
?
-
-
the enzyme plays an important role in hydrolysis of Xaa-Pro-Yaa peptides
-
-
?
additional information
?
-
-
the enzyme participates in the myocardial kinin metabolism to the same extent as angiotensin-converting enzyme, APP inhibition leads to a reduction in myocardial infarct size by the bradykinin-dependent pathway, synergistic with inhibition of angiotensin-converting enzyme, overview
-
?
additional information
?
-
-
the enzyme is involved in degradation of peptide intermediates
-
-
?
additional information
?
-
-
X-prolyl aminopeptidase (APP) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of N-terminal amino acid present adjacent to a penultimate proline residue
-
-
?
additional information
?
-
-
X-prolyl aminopeptidase (APP) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of N-terminal amino acid present adjacent to a penultimate proline residue
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
NaCl
Ni2+
Zn2+
additional information
Ca2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Ca2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Co2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Co2+
in a metal:protein ratio of 0.11:1, slightly activates the enzyme at 0.01-0.1 mM, 2.8fold activation at 1 mM in presence of 1 mM glutathione
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mn2+
required, best metal ion, the enzyme activity increases 27.6 times of the control level at 1 mM Mn2+, strong activation at 0.01-50 mM
Mn2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM with substrates substance P and bradykinin
Mn2+
-
wild-type and mutat R404A, binding of Mn2+ with a stoichiometry of 2 per monomer
Mn2+
in a metal:protein ratio of 1:1, activates the enzyme 2.80fold at 0.1 mM with substrate substance P, maximal at 0.3 mM, 4.6fold activation at 1 mM in presence of 1 mM glutathione
Mn2+
-
using the QM/MM method it is shown that XPNPEP1 employs two divalent manganese atoms (Mn(II)-Mn(II)) in the active site. The possibility of a single Mn(II) atom or other combination of divalent metal ions: Ca(II), Fe(II), Mg(II) is excluded
Mn2+
activates, required, Km values for Mn2+ are 0.0022 mM for the wild-type enzyme, 0.004 mM for mutant Y527F, and 0.0018 mM for mutant R535A. Kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
Mn2+
-
the active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Mn2+
activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern
Mn2+
the activity of the enzyme depends critically on the presence of Mn2+. Reducing concentration of Mn2+ in reaction buffer from 1 mM to 0.006 mM reduces the activity of the enzyme by about 60%. Other divalent metal ions (Mg2+, Ca2+, Co2+, Ni2+ and Zn2+) fail to fully restore activity of the enzyme
Mn2+
-
enhances activity, atomic absorption studies reveal the presence of Mn2+ in the protein as a co-factor
Mn2+
-
4-10 mM, activates hydrolysis of Gly-Pro-Hyp, beta-casomorphin or substance P
Mn2+
activates 5fold at 0.01 mM, 2.5fold at 5 mM. The active site of PepP is involved in the binding of two Mn2+ ions
NaCl
increases the enzyme activity in the concentration range 0.5-3.0 M, suggesting that the enzyme is halophilic
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
Zn2+
APP-1 is a dimer that uses dinuclear zinc at the active site
Zn2+
required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA of Dr-smAPP is coordinated by O3 of phosphate ion, His285 Nepsilon2, and Glu328 Oepsilon1 in the equatorial plane and Asp221 Odelta2 and Glu314 Oepsilon2 in the axial sites. Metal ZnB of Dr-smAPP is coordinated by O3 of phosphate ion, Asp210 Odelta1, Asp221 Odelta1, and Glu328 Oepsilon2. Glu328 and Asp221 act as bidentate ligands and bind to both the metals
Zn2+
required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA is coordinated by O1 of cacodylate ion, Glu335 Oepsilon2, Glu321 Oepsilon2, His292 Nepsilon2, and Asp223 Odelta2. Metal ZnB is coordinated by O1 of cacodylate ion, Glu335 Oepsilon1, Asp212 Odelta1, and Asp223 Odelta1. Glu335 and Asp223 act as bidentate ligands and bind to both the metals
Zn2+
-
mono-zinc-containing enzyme, lacks any of the typical metal binding motifs found in other zinc metalloproteases
additional information
-
metalloenzyme, enzyme which is free of metals due to EDTA-treatment cannot be reactivated by addition of Co2+, Zn2+, or Mn2+
additional information
-
the active site contains a dinuclear metal binding site, the enzyme contains 12 metal atoms per molecule, 2 of which are Mn2+ ions
additional information
the enzyme activity is dependent on metal ions and influenced by different metal ions. This enzyme's pita-bread fold is commonly found in N-terminal amido-, imido-, and amidino-scissile bond-cleaving enzymes, and serves as a structural basis for the metal-dependent catalysis. Addition of Mn2+ significantly restores the Pa-PepP activity of the apoenzyme, while the limited enhancement of activity is observed upon addition of Ca2+ or Mg2+
additional information
structure modeling reveals that residues Thr273 and Thr383 do not directly interact with metal ions but may be important for their retention in the protein active site
additional information
-
activity of rTgAPP is enhanced by the addition of divalent cations
additional information
the active site of each subunit of puified recombinant TVMP50 contains two metals Ca2+ and Ni2+. The Ni2+ is likely also dragged from the IMAC resin purification. Additional Ca2+ atoms are detected bound in the structure, one on the N-terminal and two on the C-terminal domain. The conserved residues responsible for direct interaction with metallic ions are Glu407, Glu364, Asp232, Asp243, His328, and His335
additional information
-
the active site of each subunit of puified recombinant TVMP50 contains two metals Ca2+ and Ni2+. The Ni2+ is likely also dragged from the IMAC resin purification. Additional Ca2+ atoms are detected bound in the structure, one on the N-terminal and two on the C-terminal domain. The conserved residues responsible for direct interaction with metallic ions are Glu407, Glu364, Asp232, Asp243, His328, and His335
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-Phe(NO2)-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.5 mM, 30% inhibition of hydrolysis of (4-nitr)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
cilazaprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methyl-7-coumarylamide, substance P, and beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
Cr6+
CrVI, a heavy metal endocrine-disrupting chemical industrially widely used, gestational exposure to CrVI increases germ cell/oocyte apoptosis and advance germ cell nest (GCN) breakdown. CrVI increases X-prolyl aminopeptidase (Xpnpep) 2 (a marker for premature ovarian failure in humans) during germ cell nest (GCN) breakdown, it decreases Xpnpep2 during postnatal follicle development, and increases colocalization of Xpnpep2 with collagens Col3 and Col4. Phenotype, overview
enaprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methylcoumarin 7-amide, substance P, and beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
L-Ala-L-Pro-L-Ala
competitive; competitive, 50% inhibition at 0.22 mM
L-Pro-L-Leu
product inhibition, a third metal binding site is formed by two conserved His-residues and L-Pro-L-Leu
4-chloromercuriphenyl sulfonic acid
-
inhibits hydrolysis of Gly-Pro-Hyp, activates hydrolysis of bradykinin
apstatin
92% inhibition at 0.01 mM, enzyme binding structure modeling, molecular interactions between APP-1 and the ligand, overview. Comparison between Caenorhabditis elegans APP-1-apstatin structure and Escherichia coli APP-1-apstatin structure
apstatin
-
binds to the active site with its N-terminal amino group coordinated to one of the two Mn(II) ions at the metal center
Ca2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Ca2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Co2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
EDTA
10 mM EDTA inhibits enzyme activity to 0.26 times of the control level
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mn2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM with substrates substance P and bradykinin
Mn2+
activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.01 mM, complete inhibition of hydrolysis of (4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
ramiprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methylcoumarin 7-amide, substance P or beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
Zn2+
the Zn2+ ion has high affinity for APPro and inhibits the hydrolysis reaction by occupying a third metal binding site
additional information
no inhibition by 4-(2-aminoethyl)benzensulfonylfluoride, tosyl lysyl chloromethyl ketone, and tosyl phenylalanyl chloromethyl ketone
-
additional information
-
no inhibition by 4-(2-aminoethyl)benzensulfonylfluoride, tosyl lysyl chloromethyl ketone, and tosyl phenylalanyl chloromethyl ketone
-
additional information
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
additional information
-
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
additional information
no significant inhibition by amastatin and enalaprilat
-
additional information
-
no significant inhibition by amastatin and enalaprilat
-
additional information
-
more intense processing conditions, above 100-200 MPa and 20-30°C, lead to enzyme inactivation with PepX HP-induced conformational changes, investigated by circular dichroism spectroscopy, kinetic analysis, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuriphenyl sulfonic acid
-
inhibits hydrolysis of Gly-Pro-Hyp, activates hydrolysis of bradykinin
glutathione
activates the enzyme in presence of Mn2+ or Co2+, and slightly in presence of Zn2+
guanidine hydrochloride
strongly reactivates enzyme mutant R353 at 0.1-10 mM, approximately 90% of the activity lost in theR535A hcAMPP mutant is regained in the presence of 30 mM guanidine hydrochloride. It has neither an observable rescue effect on wild-type hcAMPP nor on the Y527F mutant
progesterone
-
exposure of HepG2 cells to 0.001 mM progesterone results in a significant increase in the AP-P activity of cell lysates
additional information
-
women on the oral contraceptive pill have higher age-adjusted plasma AP-P compared to women not on the oral contraceptive pill or males
-
additional information
-
activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Generation of Alzheimer disease-associated amyloid ?42/43 peptide by ?-secretase can be inhibited directly by modulation of membrane thickness.
Alzheimer Disease
Targeting Cannabinoid Receptor Activation and BACE-1 Activity Counteracts TgAPP Mice Memory Impairment and Alzheimer's Disease Lymphoblast Alterations.
Angioedema
A functional XPNPEP2 promoter haplotype leads to reduced plasma aminopeptidase P and increased risk of ACE inhibitor-induced angioedema.
Angioedema
A variant in XPNPEP2 is associated with angioedema induced by angiotensin I-converting enzyme inhibitors.
Angioedema
Diagnosis and treatment of bradykinin-mediated angioedema: outcomes from an angioedema expert consensus meeting.
Angioedema
Sex-dependent and race-dependent association of XPNPEP2 C-2399A polymorphism with angiotensin-converting enzyme inhibitor-associated angioedema.
Asthma
Eastern Carolina Asthma Prevention Program (ECAPP): An Environmental Intervention Study Among Rural and Underserved Children with Asthma in Eastern North Carolina.
Biliary Atresia
Association of X-prolyl aminopeptidase 1 rs17095355 polymorphism with biliary atresia in Thai children.
Carcinoma
Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease.
Carcinoma, Renal Cell
Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease.
Cervical Intraepithelial Neoplasia
XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
Ciliopathies
Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy.
Cough
PNPT1 and PCGF3 variants associated with angiotensin-converting enzyme inhibitor-induced cough: a nested case-control genome-wide study.
Kidney Diseases
Mitochondrial aminopeptidase deletion increases chronological lifespan and oxidative stress resistance while decreasing respiratory metabolism in S. cerevisiae.
Kidney Diseases, Cystic
Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.
Microcephaly
Developmental retardation, microcephaly, and peptiduria in mice without aminopeptidase P1.
Neoplasm Metastasis
XPNPEP2 is associated with lymph node metastasis in prostate cancer patients.
Neoplasm Metastasis
XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
Neoplasms
Identification of DEGs and transcription factors involved in H. pylori-associated inflammation and their relevance with gastric cancer.
Neoplasms
XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
Primary Ovarian Insufficiency
Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene.
Prostatic Neoplasms
XPNPEP2 is associated with lymph node metastasis in prostate cancer patients.
Stroke
Recurrent ischemic stroke in patients with atrial fibrillation ablation and prior stroke: A study based on etiological classification.
Trichomonas Infections
The 50kDa metalloproteinase TvMP50 is a zinc-mediated Trichomonas vaginalis virulence factor.
Trichomonas Infections
TvMP50 is an immunogenic metalloproteinase during male trichomoniasis.
Uterine Cervical Neoplasms
XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
xaa-pro aminopeptidase deficiency
Deficiency of aminopeptidase P1 causes behavioral hyperactivity, cognitive deficits, and hippocampal neurodegeneration.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
L-Ile-L-Pro-L-Pro
-
pH 7, temperature not specified in the publication
4.7
L-Leu-L-Pro-L-Pro
-
pH 7, temperature not specified in the publication
13.6
L-Val-L-Pro-L-Pro
-
pH 7, temperature not specified in the publication
0.00883
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide
recombinant enzyme, pH 7.5, 30°C
0.087
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
wild-type, pH 8.1, 37°C
0.14
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
mutant H350A, pH 8.1, 37°C
0.078
bradykinin
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
0.144
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
0.163
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
0.327
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
0.51
L-Ala-L-Pro-4-nitroanilide
chimera th-sl cAPP, pH 7.0, 30°C
1.7
L-Ala-L-Pro-4-nitroanilide
recombinant enzyme, pH 7.4, 30°C
16.9
L-Ala-L-Pro-4-nitroanilide
chimera sl-th cAPP, pH 8.2, 30°C
0.308
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics. Kinetic parameters for R535A hcAMPP measured in the presence and absence of guanidine hydrochloride, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Kinetic parameters for R535A hcAMPP measured in the presence and absence of guanidine hydrochloride, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE