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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, xpnpep3, membrane-bound app, xpnpep1, appro, tgapp, tvmp50, x-prolyl-dipeptidyl aminopeptidase, aminopeptidase p1, x-prolyl aminopeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoacylproline aminopeptidase
-
-
-
-
aminopeptidase P
aminopeptidase P1
aminopeptidase, aminoacylproline
-
-
-
-
AMPP
AP-P
APP
APP1
APPro
Dr-smAPP
Icp55
M24B peptidase
mAmP
-
-
-
-
Membrane-bound AmP
-
-
-
-
Membrane-bound APP
-
-
-
-
Mt-smAPP
PEPP
PepQ
peptidase PepQ
PepX aminopeptidase
proline aminopeptidase
-
-
-
-
small aminopeptidase-P
TgAPP
X-Pro aminopeptidase
X-prolyl aminopeptidase
X-prolyl aminopeptidase 2
X-prolyl aminopeptidase 3
Xaa-Pro aminopeptidase
-
-
-
-
XpmA
XPNPEP1
XPNPEP2
XPNPEP3
YpdF
additional information
aminopeptidase P
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-
-
-
AP-P
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-
-
-
APP
-
-
-
-
X-Pro aminopeptidase
-
-
-
-
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
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
exopeptidase, N-terminus, amino acid
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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-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
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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
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-
-
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?
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
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best substrate
-
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
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-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
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-
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?
leucine rich repeat containing 50 + H2O
?
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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
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-
?
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-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
-
?
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
Streptomyces murinus TH-4
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.
Lymphatic Metastasis
XPNPEP2 is associated with lymph node metastasis in prostate cancer patients.
Lymphatic Metastasis
XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
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
Altered hippocampal gene expression, glial cell population, and neuronal excitability in aminopeptidase P1 deficiency.
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
0.308
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
7.7
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
2
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
3.2
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
3.8
bradykinin
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
8.3
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.12
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
22.22
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
50.92
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0603
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.269
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.0282
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.0789
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.027
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.0307
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
pH 7.4, 30°C
0.0198
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
pH 7.4, 30°C
0.037
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
pH 7.4, 30°C
0.00126
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
pH 7.4, 30°C
0.057
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
pH 7.4, 30°C
0.014
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
pH 7.4, 30°C
0.11
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
pH 7.4, 30°C
0.0043
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
pH 7.4, 30°C
0.0229
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
pH 7.4, 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.016
-
humans with previous angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
0.022 - 0.023
-
humans without angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
additional information
additional information
the supernatant shows a specific activity of the recombinant enzyme of 117 units/mg, the cell-free extract shows a specific activity of the recombinant enzyme of 8 units/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
7
-
hydrolysis of bradykinin(1-8), 0.5 mM, in both 0.1 M Hepes buffer or 0.1 M potassium phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
55
additional information
-
activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C, kinetic analysis, overview
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
70% of maximal activity at 15°C, 20% at 50°C, recombinant enzyme, profile overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type and mutant strain that lacks peptidase P
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
upregulation of Xaa-Pro aminopeptidase-1, XPNPEP-1, in renal cell carcinoma from von Hippel-Lindau patients, and a strong decrease of XPNPEP-2, quantitative proteomic analysis, overview
brenda
additional information
-
enriched in caveolae on the luminal surface of pulmonary vascular endothelium. Lung vascular targeting is assessed using a human/mouse chimeric monoclonal antibody (833c) against APP
brenda
the enzyme colocalizes with collagens Col3 and Col4 in fetal ovaries around the germ cells, GCN, and along the ovigerous cords
brenda
-
the enzyme colocalizes with collagens Col3 and Col4 in fetal ovaries around the germ cells, GCN, and along the ovigerous cords
-
brenda
additional information
enzyme is expressed through the asexual erythrocytic cycle
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
XPNPEP2 is glycophosphatidylinositol (GPI) anchored on the cytosolic side of the plasma membrane
brenda
additional information
-
attached to the membranes via a glycosylphosphatidylinositol anchor
brenda
-
attached to the membranes via a glycosylphosphatidylinositol anchor
brenda
additional information
isoforms of the human enzyme include the cytosolic (hcAMPP) and membrane-bound (hmAMPP) aminopeptidase P, encoded by XPNPEP1 and XPNPEP2 genes, and a third hypothetical isoform thought to be present in mitochondrial and cytosolic localizations
-
brenda
additional information
-
isoforms of the human enzyme include the cytosolic (hcAMPP) and membrane-bound (hmAMPP) aminopeptidase P, encoded by XPNPEP1 and XPNPEP2 genes, and a third hypothetical isoform thought to be present in mitochondrial and cytosolic localizations
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzyme PepP belongs to the family of proline-specific aminopeptidases
evolution
-
enzyme TgAPP is a member of the M24 prolyl aminopeptidase family
evolution
pepP encodes an enzyme belonging to the aminopeptidases P (APPro) family, a type of metalloprotease that catalyzes the removal of the N-terminal residue from a polypeptide that has proline as the second residue. Enzyme PepP is highly conserved in all Pseudomonas aeruginosa genomes sequenced to date and has high genetic similarity with enzymes from other Pseudomonas species (82.4%-100% identity)
evolution
the enzyme belongs to the M24B subfamily of aminoproteases
evolution
the enzyme TvMP50 belong to the aminopeptidase P-like metalloproteinase subfamily A/B, family M24 of clan MG, Parabasalia group. The Parabasalia group contains two protein lineages with a pita bread fold; the ancestral monomeric group 1 is probably derived from an ancestral dimeric aminopeptidase P-type enzyme, and group 2 has a probable dimeric kind of ancestral eukaryotic prolidase lineage. Phylogenetic analysis, overview
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
evolution
-
the enzyme belongs to the M24B subfamily of aminoproteases
-
malfunction
in 2 families with an nephronophthisis-like phenotype, homozygous frameshift and splice-site mutations, respectively, are detected in the X-prolyl aminopeptidase 3 gene
malfunction
-
suppression of zebrafish xpnpep3 phenocopied the developmental phenotypes of ciliopathy morphants, and this effect is rescued by human XPNPEP3 that is devoid of a mitochondrial localization signal, suggesting that the protein might also have mitochondrial-independent activity
malfunction
-
Xpnpep1 knockout mice display severe growth retardation, microcephaly, and modest lethality. Imino-oligopeptide excretion is observed in urine samples from APP1-deficient mice
malfunction
-
deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system results in inhibition of growth indicating the importance of TgAPP
malfunction
-
deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system results in inhibition of growth indicating the importance of TgAPP
-
metabolism
-
four metalloaminopeptidases (MAPs) play a role in peptide turnover in Pf parasites: leucyl aminopeptidase (PfA-M17), alanyl aminopeptidase (PfA-M1), aspartyl aminopeptidase (PfM18AAP), and aminopeptidase P (PfAPP). The substrate profile shows that PfAPP has the capacity to catalyze the removal of any N-terminal amino acid residue from peptides with a P1' proline, and that the other MAPs in Plasmodium falciparum are unable to perform this function
metabolism
the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803 contains 25 genes of aminopeptidases, among which only the sll0136 gene encodes a aminopeptidase P (PepP)
physiological function
eukaryotic aminopeptidase P1 (APP1) is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases, role for APP-1 is in the breakdown of imino-peptides generated during protein catabolism
physiological function
-
peptide recycling, the process by which cellular proteins are broken down to single amino acid residues, is critical to parasite survival. In blood-stage malaria parasites, two major processes are responsible for peptide turnover: proteasomal (within the cytosol) and vacuolar (in the specialized digestive food vacuole). The vacuolar pathway is responsible for the digestion of 60-80% of host cell hemoglobin, which is imported into the digestive vacuole and degraded into free amino acids. This process is absolutely necessary for parasite growth and development. The final step of peptide turnover, the removal of N-terminal amino acids from short polypeptide chains, is catalyzed by a panel of aminopeptidases, which work in concert according to different substrate specificities, to complete protein digestion. During the blood stage, the parasites utilise a proteolytic cascade to digest host hemoglobin, which produces free amino acids absolutely necessary for parasite growth and reproduction. The enzymes required for hemoglobin digestion are therefore attractive therapeutic targets. The final step of the cascade is catalyzed by several metalloaminopeptidases, including aminopeptidase P (APP)
physiological function
Xaa-Pro aminopeptidase-1 is an anti-proliferative and anti-migratory exoprotease. Differential expression of Xaa-Pro aminopeptidases 1 and 2 in renal cancer, overview
additional information
analysis of structure-function relationship of aminopeptidase P, structure modelling, overview. A loop extending from the active site is important for specific large-substrate binding, and this non-conserved surface loop is also critical for Pseudomonas aeruginosa virulence. The extended substrate binding site is identified to be responsible for virulence-related protein recognition.
additional information
Caenorhabditis elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases
additional information
-
Caenorhabditis elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases
additional information
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
additional information
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
additional information
-
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
additional information
the active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
additional information
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
additional information
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-123) and a C-terminal domain (residues 124-360). The C-terminal domain, adopting a typical pita-bread-fold, houses the metal binding active site. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
additional information
three-dimensional modeling of the Synechocystis sp. PCC6803 PepP protein, overview. The PepP amino acid residues Asp260, Asp271, His354, Glu385, and Glu415 are involved in the formation of the enzym's catalytic site
additional information
-
three-dimensional structure analysis and structure-function analysis, structure comparisons, overview
additional information
Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme
additional information
-
Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
additional information
-
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P
-
Show AA Sequence and Transmembrane Helices (7729 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
x * 105000, recombinant GST-fusion protein, SDS-PAGE
140000
220000
40000
68000
-
x * 71000, recombinant His-tagged fusion protein, SDS-PAGE, x * 68000, W03G9.4 protein, SDS-PAGE
71000
90000
91000
71000
-
x * 71000, recombinant His-tagged fusion protein, SDS-PAGE, x * 68000, W03G9.4 protein, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
arranged in 2 types of tetramers, one tetramer comprises 4 crystallographically independent subunits, while the other tetramer comprises 2 pairs of subunits related by a crystallographic 2fold axis
homodimer
monomer
tetramer
additional information
?
-
x * 71000, recombinant His-tagged fusion protein, SDS-PAGE, x * 68000, W03G9.4 protein, SDS-PAGE
dimer
2 * 52000, gel filtration, the enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, not monomer, is the active species of the enzyme with loop dynamics at the dimer interface playing an important role in activity. Dynamics of Icp55 protein between two conformations of dimer are found to be important for activity of the enzyme
dimer
-
2 * 52000, gel filtration, the enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, not monomer, is the active species of the enzyme with loop dynamics at the dimer interface playing an important role in activity. Dynamics of Icp55 protein between two conformations of dimer are found to be important for activity of the enzyme
-
homodimer
2 * 71977, recombinant His-tagged enzyme without the start Met, mass spectrometry
homodimer
-
the enzyme structure shows a homodimer associated by an extensive interface between the catalytic domains (domain III) of both monomers. 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
monomer
1 * 52000, the enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, not monomer, is the active species of the enzyme
monomer
-
1 * 52000, the enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, not monomer, is the active species of the enzyme
-
tetramer
the monomers are arranged as a dimer with an extended loop contributing to the active site of the adjacent subunit and an average interface area of approximately 2050.9 A2 per subunit. The dimer-of-dimers results in an 815.6 A2 buried area per subunit
additional information
APP-1 is a dimer that uses dinuclear zinc at the active site. The two protomers (MolA and MolB) are held together mainly via hydrophobic interactions. Interfacing residues run along the entire length of the dimer with each subunit contributing 54 residues to the dimer interface
additional information
-
APP-1 is a dimer that uses dinuclear zinc at the active site. The two protomers (MolA and MolB) are held together mainly via hydrophobic interactions. Interfacing residues run along the entire length of the dimer with each subunit contributing 54 residues to the dimer interface
additional information
interaction of the subunits can not be disrupted by 2-mercaptoethanol, 1 M NaCl, 1% Triton X-100, and 4 mM CHAPS
additional information
-
interaction of the subunits can not be disrupted by 2-mercaptoethanol, 1 M NaCl, 1% Triton X-100, and 4 mM CHAPS
additional information
the reported X-ray structure of hcAMPP depicts a homodimer with each subunit containing an N-terminal domain, a middle domain, and a C-terminal catalytic domain, two active site divalent metal ions. Dimerization is mediated by the N-terminal domain and Trp477, and conservation of the key active site residues including Asp415, Asp426, His489, Glu523, Glu537, His395, His485, and His498
additional information
-
the reported X-ray structure of hcAMPP depicts a homodimer with each subunit containing an N-terminal domain, a middle domain, and a C-terminal catalytic domain, two active site divalent metal ions. Dimerization is mediated by the N-terminal domain and Trp477, and conservation of the key active site residues including Asp415, Asp426, His489, Glu523, Glu537, His395, His485, and His498
additional information
the recombinant enzyme exists as a monomer in solution, tetrameric oligomerization is observed in crystal packing. The monomer structure displays a two-domain organization where the N-domain (1-175) is composed of a mainly parallel beta-sheet core (B1-B6) flanked by seven alpha helices (A-G). In contrast, the catalytic C-domain (176-444) adopts a conserved pita-bread fold wth six beta sheets (B7-B12) in antiparallel configuration. This 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
additional information
-
pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increases. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity
additional information
Streptococcus thermophilus ACA DC 0022
-
pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increases. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity
-
additional information
Streptococcus thermophilus ACA-DC 0022
-
pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increases. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity
-
additional information
three-dimensional modeling of the Synechocystis sp. PCC6803 PepP protein, overview
additional information
crystallographic coordinates show a monomer on a pseudo-homodimer array on the asymmetric unit that resembles the quaternary structure of the M24B dimeric family and suggests a homodimeric aminopeptidase P-like enzyme as a likely ancestor. TvMP50 has a modified N-terminal region compared with other Xaa-Pro aminopeptidases/prolidases with three-dimensional structures. The formation of the standard dimer is structurally unstable in aqueous solution, and a comparably reduced number of hydrogen bridges and lack of saline bridges are found between subunits A/B, which explain why TvMP50 portrays monomeric functionality
additional information
-
crystallographic coordinates show a monomer on a pseudo-homodimer array on the asymmetric unit that resembles the quaternary structure of the M24B dimeric family and suggests a homodimeric aminopeptidase P-like enzyme as a likely ancestor. TvMP50 has a modified N-terminal region compared with other Xaa-Pro aminopeptidases/prolidases with three-dimensional structures. The formation of the standard dimer is structurally unstable in aqueous solution, and a comparably reduced number of hydrogen bridges and lack of saline bridges are found between subunits A/B, which explain why TvMP50 portrays monomeric functionality
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
glycoprotein
-
secreted enzyme mutant with translational stop codon at position 658, N-glycosylated
side-chain modification
-
the enzyme is attached to the membranes via a glycosylphosphatidylinositol anchor
side-chain modification
-
the enzyme is anchored to the membrane via a covalently attached glycosyl-phosphatidylinositol moiety
side-chain modification
-
the enzyme is attached to the membranes via a glycosylphosphatidylinositol anchor
side-chain modification
-
the enzyme contains at least 17% N-linked carbohydrate
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme by sitting drop vapour diffusion method, crystallization buffer containing 17.5% PEG 3350, 0.1 M bis-tris propane, pH 8.5, and 0.2 M sodium malonate is mixed with an equal volume of 3 mg/ml protein in 10 mM Tris/HCl, pH 8.0, and 150 mM NaCl,16°C, X-ray diffraction structure determination and analysis at 1.93 A resolution
purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml crystallization solution containing 0.1 M phospho-citrate, pH 4.6, 0.2 M NaCl, and 22% PEG 8000, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template
8 mg/ml purified recombinant enzyme in Tris, pH 8.5, hanging drop vapour diffusion method, 0.003 ml mixed with 0.002 ml reservoir solution containing 25% PEG 4000, 0.1 M Tris-HCl, pH 8.0, 0.2 M sodium acetate, and 1 mM MnCl2, 1 month at 4°C, cryoprotectant is 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group
purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 1.4 M trisodium citrate, 0.1 M sodium cacodylate, pH 6.5, 10% glycerol, and 0.5 mM ZnCl2, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template
hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5)
-
purified recombinant enzyme PfAPP both unliganded and in complex with inhibitor apstatin, hanging drop vapor diffusion method, mixing of 2:1 vl/v ratio of 6 mg/ml protein solution with reservoir containing 40-50% 2-methyl-2,4-pentanediol, and 0.1 M sodium cacodylate, pH 5.6-6.2, 3-7 days, X-ray diffraction structure determination and analysis at 2.30-2.35 A resolution. Crystals of the apstatin:PfAPP complex are obtained by soaking unliganded crystals in mother liquor supplemented with 2 mM apstatin for 1 h. For the unliganded PfAPP structure, the molecular replacement search model is prepared from the structure of human APP1 (PDB ID 3CTZ)
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.78-1.85 A resolution
purified recombinant His6-tagged enzyme, microbatch crystallization method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of crstallization solution containing 30% v/v PEG400, 0.1 M sodium acetate, 0.2 M calcium acetate, pH 4.5, the pH is adjusted to pH 5.8 with acetic acid, X-ray diffraction structure determination and analysis at 3.4 A, molecular replacement based on the structure of human prolidase (PDB ID 2IW2)
XPD43 is crystallized to 1.83 A resolution using the microbatch-under-oil technique
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D53A
site-directed mutagenesis, mutant D53A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
H193A
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
H281A
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
R55A
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
Y56A
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
H193A
-
site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type
-
H281A
-
site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding
-
R55A
-
site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
Y56A
-
site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides
-
D260A
D271A
E383A
H243A
H350A
H354A
H361A
E41A
-
the mutant maintains 91% of the wild type activity and demonstrates that the acidic residue, which is considered as a stabilizing factor in the protonation of catalytic residue His498, plays only a marginal role in catalysis
R535A
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme. The respective levels of activity restoration are determined to be 86%, 31%, 16%, and 10% for guanidine hydrochloride, methylguanidine, aminoguanidine and N-ethyl-guanidine
W477E
-
the mutant, designed to block dimer formation, shows only 6% of the wild type activity
Y527F
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme
E568Q
-
site-directed mutagenesis, low expression level in COS-1 cells, inactive mutant
E588A
-
site-directed mutagenesis, 66% remaining activity compared to the wild-type enzyme with substrate bradykinin
E588Q
-
site-directed mutagenesis, 83% remaining activity compared to the wild-type enzyme with substrate bradykinin
H519K
-
site-directed mutagenesis, 2.3% remaining activity compared to the wild-type enzyme with substrate bradykinin, increased Km, reduced kcat
H519L
-
site-directed mutagenesis, 73.8% remaining activity compared to the wild-type enzyme with substrate bradykinin, increased Km
H532L
-
site-directed mutagenesis, very low expression level in COS-1 cells, protein degradation, inactive mutant
additional information
D260A
MnA is bound at the active site, but the MnB site is empty. Loss of catalytic activity
D271A
no atoms of Mn(II) are bound at the active site. Loss of catalytic activity
E383A
both Mn-(II) atoms are present in the active site, but the bridging solvent molecule is located significantly farther from the metals than in wild-type. Loss of catalytic activity
E383A
crystallization data. One of the two metal sites is only partially occupied
H243A
crystallization data. Mutant is capable of binding the substrate L-Val-L-Pro-L-Leu
H350A
loss of catalytic activity. H350 forms part of a hydrophobic binding pocket that gives the enzym its proline specificity
H354A
MnB is present at the active site at less than full occupancy, and a water molecule occupies the MnA site. Loss of catalytic activity
additional information
-
partial or complete deletion of N-terminal domain, complete loss of enzymic activity
additional information
design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
-
design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
-
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
additional information
-
kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
additional information
-
construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and sl-th cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP were almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP showed curves and pKa values that resembled those of Streptomyces lividans isoform II
additional information
construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and slth cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP are almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP shows curves and pKa values that resemble those of Streptomyces lividans isoform II
additional information
Streptomyces murinus TH-4
-
construction of chimeric enzymes th-sl cAPP, in which half of the N-terminal domain is derived from Streptomyces costaricanus and the rest is Streptomyces lividans isoform II and sl-th cAPP, in which half of the N-terminal domain is Streptomyces lividans isoform II and the rest is Streptomyces costaricanus. Both chimera are activated by Zn2+. Th-sl cAPP and slth cAPP, respectively, form a tetramer and a dimer. The pH dependence and pKa values of th-sl cAPP are almost identical to those of Streptomyces costaricanus. In contrast, sl-th cAPP shows curves and pKa values that resemble those of Streptomyces lividans isoform II
-
additional information
-
deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system
additional information
-
deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
purified recombinant enzyme, stable at. The enzyme maintains activity after incubation at pH 3.5 -12.0, pretreatment between pH 4.0 and pH 7.5 or between pH 8.5 and pH 11.0 results in enzyme activity above 100% of control, in particular at pH 4.0-5.5 about 4-5fold
754215
4.5 - 7
-
polyethylene glycol 20000 improves stability in the pH-range 4.5-7.0
36054
5.5
-
human cytosolic APP1 is unstable and forms a high molecular weight aggregate at acidic pH
709048
8 - 9
8
-
50°C, 30 min, 50% loss of activity of enzyme form APP-I, 60°C, 50% loss of activity of enzyme form APP-II
36039
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 37
-
reasonable stability at 0°C, 20°C and 37°C over 15 days
20 - 50
purified recombinant enzyme, stable up to, inactivation at 60°C
50
60
additional information
additional information
thermal stability of wild-type and mutant hcAMPPs, overview
additional information
-
thermal stability of wild-type and mutant hcAMPPs, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C to 4°C, 0.5 mg/ml recombinant GST-fusion enzyme, several weeks without significant loss of activity
4°C, bicine buffer, pH 7.8, 1 mM dithiothreitol, 1 mM MnCl2, stable for several weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange chromatography, ultrafiltration, gel filtration, and hydroxyapatite chromatography, to homogeneity
-
Ni-NTA resin column chromatography and Hitrap Q HP affinity column chromatography
-
partial
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography, gel filtration, and dialysis
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by glutathione affinity chromatography, tag cleavage through enterokinase, followed by another step of glutathione affinity chromatography for tag removal
recombinant His-tagged enzyme from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, dialysis, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 star (DE3) by affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain strain BL21(DE3)
recombinant His-tagged wild-type and mutant cytosolic isozymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and ultrafiltration
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration
recombinant wild-type and mutant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, dialysis, and gel filtration
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
cloning, DNA and amino acid sequence determination and analysis, and functional expression of open reading frame W03H9.4 from EST yk91g4 in Caenorhabditis elegans as GFP-fusion protein and as His-tagged enzyme in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli
DNA and amino acid sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme, and in COS-1 cells
expressed in Escherichia coli as a His-tagged fusion protein
expression as a fusion with the yellow fluorescent protein allele Citrine or with hemagglutinin tag in Plasmodium falciparum
expression in Escherichia coli
expression in Escherichia coli BL21(DE3). Full-length Icp55 construct can not be expressed in the soluble fraction. Two truncated versions, Icp55t1 with 42 amino acid N-terminal truncation and Icp55t2 with 57 amino acid N-terminal truncation, are successfully expressed in soluble forms. All activity assays for Icp55 are reported for Icp55t1 construct
gene ampp, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21
gene LeAPP1, DNA and amino acid sequence determination and analysis
gene LeAPP2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli in N-terminal fusion with GST, a mutant form lacking 11 amino acids from the N-terminus is not active
gene pepP, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene sll0136, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene TgApp, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21
-
gene XPNPEP1, recombinant expression of wild-type and mutant cytosolic aminopeptidases P (hcAMPP, residues M1 to H623), with a thrombin-cleavable N-terminal His-tag in Escherichia coli strain Rosetta (DE3)
recombinant expression in Escherichia coli as a His-tagged fusion protein
-
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
recombinant expression of wild-type and mutant His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the enzyme PfAPP might be a potential target for an antimalarial therapeutic strategy
food industry
medicine
-
significant inhibition of enzyme after repeated oral dosage of angiotensin-converting enzyme inhibitor enalapril, but not of imidapril. Induction of dry cough by ACE inhibitors may be related to accumulation of bradykinin
food industry
-
PepX aminopeptidase from Streptococcus thermophilus ACA DC 0022 is used in Greek Feta cheese manufacturing
food industry
Streptococcus thermophilus ACA-DC 0022
-
PepX aminopeptidase from Streptococcus thermophilus ACA DC 0022 is used in Greek Feta cheese manufacturing
-
food industry
Streptococcus thermophilus ACA DC 0022
-
PepX aminopeptidase from Streptococcus thermophilus ACA DC 0022 is used in Greek Feta cheese manufacturing
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, K.C.S.; Buchanan, T.M.
Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase
J. Biol. Chem.
255
1704-1710
1980
Neisseria gonorrhoeae
brenda
Harada, M.; Mogi, M.; Fukasawa, K.; Fukasawa, F.M.
High-performance liquid chromatographic determination of aminopeptidase P activity in Fischer F344 rat serum and kidney
J. Chromatogr.
493
176-181
1989
Rattus norvegicus
brenda
Yoshimoto, T.; Murayama, N.; Tsuru, D.
A novel assay method for aminopeptidase P and partial purification of two types of the enzyme in Escherichia coli
Agric. Biol. Chem.
52
1957-1963
1988
Escherichia coli
-
brenda
Yoshimoto, T.; Murayama, N.; Honda, T.; Tone, H.; Tsuru, D.
Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme
J. Biochem.
104
93-97
1988
Escherichia coli
brenda
Hooper, N.M.; Turner, A.J.
Ectoenzymes of the kidney microvillar membrane. Aminopeptidase P is anchored by a glycosyl-phosphatidylinositol moiety
FEBS Lett.
229
340-344
1988
Homo sapiens, Sus scrofa
brenda
Lasch, J.; Koelsch, R.; Steinmetzer, T.; Neumann, U.; Demuth, H.U.
Enzymic properties of intestinal aminopeptidase P: a new continuous assay
FEBS Lett.
227
171-174
1988
Rattus norvegicus
brenda
Holtzman, E.J.; Pillay, G.; Rosenthal, T.; Yaron, A.
Aminopeptidase P activity in rat organs and human serum
Anal. Biochem.
162
476-481
1987
Homo sapiens, Rattus norvegicus
brenda
Ryan, J.W.; Valido, F.; Berryer, P.; Chung, A.Y.K.; Ripka, J.E.
Purification and characterization of guinea pig serum aminoacylproline hydrolase (aminopeptidase P)
Biochim. Biophys. Acta
1119
140-147
1992
Cavia porcellus
brenda
Achstetter, T.; Ehmann, C.; Wolf, D.H.
Proteolysis in eucaryotic cells: aminopeptidases and dipeptidyl aminopeptidases of yeast revisited
Arch. Biochem. Biophys.
226
292-305
1983
Saccharomyces cerevisiae
brenda
Miller, C.G.; Green, L.
Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium
J. Bacteriol.
153
350-356
1983
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Mc Donnell, M.; Fitzgerald, R.; Fhaolain, I.N.; Jennings, P.V.; O'Cuinn, G.
Purification and characterization of aminopeptidase P from Lactococcus lactis subsp. cremoris
J. Dairy Res.
64
399-407
1997
Lactococcus lactis
brenda
Lin, L.N.; Brandts, J.F.
Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease
Biochemistry
19
3055-3059
1980
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Yaron, A.; Berger, A.
Aminopeptidase-P
Methods Enzymol.
19
521-534
1970
Escherichia coli
-
brenda
Yaron, A.; Mlynar, D.
Aminopeptidase-P
Biochem. Biophys. Res. Commun.
32
658-663
1968
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Fleminger, G.; Carmel, A.; Goldenberg, D.; Yaron, A.
Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung
Eur. J. Biochem.
125
609-615
1982
Bos taurus, Escherichia coli, Homo sapiens
brenda
Lin, L.N.; Brandts, J.F.
Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline
Biochemistry
18
5037-5042
1979
Escherichia coli
brenda
Orawski, A.T.; Simmons, W.H.
Purification and properties of membrane-bound aminopeptidase P from rat lung
Biochemistry
34
11227-11236
1995
Rattus norvegicus
brenda
Hooper, N.M.; Hryszko, J.; Turner, A.J.
Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme
Biochem. J.
267
509-515
1990
Sus scrofa
brenda
Simmons, W.H.; Orawski, A.T.
Membrane-bound aminopeptidase P from bovine lung. Its purification, properties, and degradation of bradykinin
J. Biol. Chem.
267
4897-4903
1992
Bos taurus
brenda
Harbeck, H.T.; Mentlein, R.
Aminopeptidase P from rat brain. Purification and action on bioactive peptides
Eur. J. Biochem.
198
451-458
1991
Rattus norvegicus
brenda
Lloyd, G.S.; Hryszko, J.; Hooper, N.M.; Turner, A.J.
Inhibition and metal ion activation of pig kidney aminopeptidase P. Dependence on nature of substrate
Biochem. Pharmacol.
52
229-236
1996
Sus scrofa
brenda
Orawski, A.T.; Susz, J.P.; Simmons, W.H.
Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation
Mol. Cell. Biochem.
75
123-132
1987
Bos taurus
brenda
Lloyd, G.S.; Habgood, N.T.; Hooper, N.M.; Turner, A.J.
Aminopeptidase P: immunoaffinity purification and molecular characterisation
Biochem. Soc. Trans.
236S
21
1993
Sus scrofa
-
brenda
Vanhoof, G.; de Block, J.; de Meester, I.; Scharpe, S.; de Potter, W.P.
Localization and characterization of aminopeptidase P in bovine adrenal medulla
Neurochem. Int.
21
203-208
1992
Bos taurus
brenda
Matsumoto, H.; Erickson, R.H.; Kim, Y.S.
Localization and characterization of rat small intestinal aminopeptidase P and its role in prolyl peptide digestion
J. Nutr. Biochem.
6
104-110
1995
Rattus norvegicus
-
brenda
Stckel, A.; Stiebitz, B.; Neubert, K.
Specific inhibitors of aminopeptidase P. Peptides and pseudopeptides of 2-hydroxy-3-amino acids
Adv. Exp. Med. Biol.
421
31-35
1997
Escherichia coli, Rattus norvegicus
brenda
Ryan, J.W.; Berryer, P.; Chung, A.Y.K.; Sheffy, D.H.
Characterization of rat pulmonary vascular aminopeptidase P in vivo: role in the inactivation of bradykinin
J. Pharmacol. Exp. Ther.
269
941-947
1994
Rattus norvegicus
brenda
Graham, S.C.; Lee, M.; Freeman, H.C.; Guss, J.M.
An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution
Acta Crystallogr. Sect. D
59
897-902
2003
Escherichia coli
brenda
Cottrell, G.S.; Hooper, N.M.; Turner, A.J.
Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme
Biochemistry
39
15121-15128
2000
Homo sapiens (Q9NQW7), Homo sapiens
brenda
Cottrell, G.S.; Hyde, R.J.; Lim, J.; Parsons, M.R.; Hooper, N.M.; Turner, A.J.
Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P
Biochemistry
39
15129-15135
2000
Sus scrofa
brenda
Wolfrum, S.; Richardt, G.; Dominiak, P.; Katus, H.A.; Dendorfer, A.
Apstatin, a selective inhibitor of aminopeptidase P, reduces myocardial infarct size by a kinin-dependent pathway
Br. J. Pharmacol.
134
370-374
2001
Rattus norvegicus
brenda
Laurent, V.; Brooks, D.R.; Coates, D.; Isaac, R.E.
Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans
Eur. J. Biochem.
268
5430-5438
2001
Caenorhabditis elegans
brenda
Kulkarni, G.V.; Deobagkar, D.D.
A cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization
J. Biochem.
131
445-452
2002
Drosophila melanogaster (O96794), Drosophila melanogaster
brenda
Hauser, F.; Strassner, J.; Schaller, A.
Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P
J. Biol. Chem.
276
31732-31737
2001
Solanum lycopersicum (Q93X45), Solanum lycopersicum (Q93X46), Solanum lycopersicum
brenda
Kim, K.S.; Kumar, S.; Simmons, W.H.; Brown, N.J.
Inhibition of aminopeptidase P potentiates wheal response to bradykinin in angiotensin-converting enzyme inhibitor-treated humans
J. Pharmacol. Exp. Ther.
292
295-298
2000
Homo sapiens
brenda
Adam, A.; Cugno, M.; Molinaro, G.; Perez, M.; Lepage, Y.; Agostoni, A.
Aminopeptidase P in individuals with a history of angio-oedema on ACE inhibitors
Lancet
359
2088-2089
2002
Homo sapiens
brenda
Graham, S.C.; Maher, M.J.; Simmons, W.H.; Freeman, H.C.; Guss, J.M.
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin
Acta Crystallogr. Sect. D
D60
1770-1779
2004
Escherichia coli
brenda
Lee, H.S.; Kim, Y.J.; Bae, S.S.; Jeon, J.H.; Lim, J.K.; Jeong, B.C.; Kang, S.G.; Lee, J.H.
Cloning, expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1
Appl. Environ. Microbiol.
72
1886-1890
2006
Thermococcus onnurineus NA1 (Q2QC92)
brenda
Molinaro, G.; Carmona, A.K.; Juliano, M.A.; Juliano, L.; Malitskaya, E.; Yessine, M.A.; Chagnon, M.; Lepage, Y.; Simmons, W.H.; Boileau, G.; Adam, A.
Human recombinant membrane-bound aminopeptidase P: production of a soluble form and characterization using novel, internally quenched fluorescent substrates
Biochem. J.
385
389-397
2005
Homo sapiens
brenda
Graham, S.C.; Bond, C.S.; Freeman, H.C.; Guss, J.M.
Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center
Biochemistry
44
13820-13836
2005
Escherichia coli (P15034), Escherichia coli
brenda
Jao, S.C.; Huang, L.F.; Hwang, S.M.; Li, W.S.
Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P
Biochemistry
45
1547-1553
2006
Escherichia coli
brenda
Graham, S.C.; Lilley, P.E.; Lee, M.; Schaeffer, P.M.; Kralicek, A.V.; Dixon, N.E.; Guss, J.M.
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis
Biochemistry
45
964-975
2006
Escherichia coli (P15034), Escherichia coli
brenda
Stockel-Maschek, A.; Stiebitz, B.; Koelsch, R.; Neubert, K.
Novel 3-amino-2-hydroxy acids containing protease inhibitors. Part 1: Synthesis and kinetic characterization as aminopeptidase P inhibitors
Bioorg. Med. Chem.
13
4806-4820
2005
Escherichia coli, Rattus norvegicus
brenda
Sakamoto, K.; Sugimoto, K.; Sudoh, T.; Fujimura, A.
Different effects of imidapril and enalapril on aminopeptidase P activity in the mouse trachea
Hypertens. Res.
28
243-247
2005
Mus musculus
brenda
Zheng, Y.; Roberts, R.J.; Kasif, S.; Guan, C.
Characterization of two new aminopeptidases in Escherichia coli
J. Bacteriol.
187
3671-3677
2005
Escherichia coli
brenda
Graham, S.C.; Guss, J.M.
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu
Arch. Biochem. Biophys.
469
200-208
2008
Escherichia coli (P15034), Escherichia coli
brenda
Dalal, S.; Klemba, M.
Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum
J. Biol. Chem.
282
35978-35987
2007
Plasmodium falciparum (A0A144A2H0)
brenda
Arima, J.; Uesugi, Y.; Iwabuchi, M.; Hatanaka, T.
Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain
Protein Eng. Des. Sel.
21
45-53
2008
Streptomyces lividans, Streptomyces murinus (A9E3K0), Streptomyces murinus TH-4 (A9E3K0)
brenda
Duan, Q.L.; Binkley, K.; Rouleau, G.A.
Genetic analysis of Factor XII and bradykinin catabolic enzymes in a family with estrogen-dependent inherited angioedema
J. Allergy Clin. Immunol.
123
906-910
2009
Homo sapiens
brenda
Li, X.; Lou, Z.; Li, X.; Zhou, W.; Ma, M.; Cao, Y.; Geng, Y.; Bartlam, M.; Zhang, X.C.; Rao, Z.
Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit
J. Biol. Chem.
283
22858-22866
2008
Homo sapiens
brenda
Masler, E.P.
Digestion of invertebrate neuropeptides by preparations from the free-living nematode Panagrellus redivivus
J. Helminthol.
82
279-285
2008
Panagrellus redivivus
brenda
La Corte, A.L.; Carter, A.M.; Turner, A.J.; Grant, P.J.; Hooper, N.M.
The bradykinin-degrading aminopeptidase P is increased in women taking the oral contraceptive pill
J. Renin Angiotensin Aldosterone Syst.
9
221-225
2008
Homo sapiens
brenda
Doria, C.; Elia, E.S.; Kang, Y.; Adam, A.; Desormeaux, A.; Ramirez, C.; Frank, A.; di Francesco, F.; Herman, J.H.
Acute hypotensive transfusion reaction during liver transplantation in a patient on angiotensin converting enzyme inhibitors from low aminopeptidase P activity
Liver Transpl.
14
684-687
2008
Homo sapiens
brenda
Hatanaka, T.; Onaka, H.; Arima, J.; Uraji, M.; Uesugi, Y.; Usuki, H.; Nishimoto, Y.; Iwabuchi, M.
pTONA5: a hyperexpression vector in Streptomycetes
Protein Expr. Purif.
62
244-248
2008
Streptomyces murinus (A9E3K0)
brenda
Ragheb, D.; Bompiani, K.; Dalal, S.; Klemba, M.
Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol
J. Biol. Chem.
284
24806-24815
2009
Homo sapiens, Plasmodium falciparum
brenda
OToole, J.F.; Liu, Y.; Davis, E.E.; Westlake, C.J.; Attanasio, M.; Otto, E.A.; Seelow, D.; Nurnberg, G.; Becker, C.; Nuutinen, M.; Kaerppae, M.; Ignatius, J.; Uusimaa, J.; Pakanen, S.; Jaakkola, E.; van den Heuvel, L.P.; Fehrenbach, H.; Wiggins, R.; Goyal, M.; Zhou, W.; Wolf, M.T.; Wise, E.; Helou, J.; A, A.l.
Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
J. Clin. Invest.
120
791-802
2010
Danio rerio, Escherichia coli, Homo sapiens (Q9NQH7), Homo sapiens
brenda
Chrastina, A.; Valadon, P.; Massey, K.A.; Schnitzer, J.E.
Lung Vascular Targeting Using Antibody to Aminopeptidase P: CT-SPECT Imaging, Biodistribution and Pharmacokinetic Analysis
J. Vasc. Res.
47
531-543
2010
Rattus norvegicus
brenda
Kumar, A.; Are, V.; Ghosh, B.; Agrawal, U.; Jamdar, S.; Makde, R.; Sharma, S.
Crystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris
Acta Crystallogr. Sect. F
70
1268-1271
2014
Xanthomonas campestris
brenda
Stressler, T.; Eisele, T.; Schlayer, M.; Fischer, L.
Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481
AMB Express
2
39
2012
Lactococcus lactis subsp. lactis
brenda
Juarez-Montiel, M.; Ibarra, J.A.; Chavez-Camarillo, G.; Hernandez-Rodriguez, C.; Villa-Tanaca, L.
Molecular cloning and heterologous expression in Pichia pastoris of X-prolyl-dipeptidyl aminopeptidase from basidiomycete Ustilago maydis
Appl. Biochem. Biotechnol.
172
2530-2539
2014
Ustilago maydis
brenda
Yoon, S.H.; Bae, Y.S.; Mun, M.S.; Park, K.Y.; Ye, S.K.; Kim, E.; Kim, M.H.
Developmental retardation, microcephaly, and peptiduria in mice without aminopeptidase P1
Biochem. Biophys. Res. Commun.
429
204-209
2012
Mus musculus
brenda
Nandan, A.S.; Nampoothiri, K.M.
Unveiling aminopeptidase P from Streptomyces lavendulae: molecular cloning, expression and biochemical characterization
Enzyme Microb. Technol.
55
7-13
2014
Streptomyces lavendulae
brenda
Wu, S.; Liu, S.; Sim, S.; Pedersen, L.G.
Weakly antiferromagentic coupling via superexchange interaction between Mn(II)-Mn(II) atoms: A QM/MM study of the active site of human cytosolic X-propyl aminopeptidase P
J. Phys. Chem. Lett.
3
2293-2297
2012
Homo sapiens
brenda
Drinkwater, N.; Sivaraman, K.K.; Bamert, R.S.; Rut, W.; Mohamed, K.; Vinh, N.B.; Scammells, P.J.; Drag, M.; McGowan, S.
Structure and substrate fingerprint of aminopeptidase P from Plasmodium falciparum
Biochem. J.
473
3189-3204
2016
Plasmodium falciparum
brenda
Cordova, A.; Woodrick, J.; Grindrod, S.; Zhang, L.; Saygideger-Kont, Y.; Wang, K.; DeVito, S.; Daniele, S.G.; Paige, M.; Brown, M.L.
Aminopeptidase P mediated targeting for breast tissue specific conjugate delivery
Bioconjug. Chem.
27
1981-1990
2016
Homo sapiens (O43895), Homo sapiens
brenda
Banu, S.K.; Stanley, J.A.; Sivakumar, K.K.; Arosh, J.A.; Barhoumi, R.; Burghardt, R.C.
Identifying a novel role for X-prolyl aminopeptidase (Xpnpep) 2 in CrVI-induced adverse effects on germ cell nest breakdown and follicle development in rats
Biol. Reprod.
92
67
2015
Rattus norvegicus (Q99MA2), Rattus norvegicus Sprague Dawley (Q99MA2)
brenda
Baik, A.S.; Mironov, K.S.; Arkhipov, D.V.; Piotrovskii, M.S.; Pojidaeva, E.S.
Characterization of aminopeptidase P from the unicellular cyanobacterium Synechocystis sp. PCC6803
Dokl. Biochem. Biophys.
481
190-194
2018
Synechocystis sp. PCC 6803 (P74468)
brenda
Singh, R.; Goyal, V.D.; Kumar, A.; Sabharwal, N.S.; Makde, R.D.
Crystal structures and biochemical analyses of intermediate cleavage peptidase role of dynamics in enzymatic function
FEBS Lett.
593
443-454
2019
Saccharomyces cerevisiae (P40051), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P40051)
brenda
Iyer, S.; La-Borde, P.J.; Payne, K.A.; Parsons, M.R.; Turner, A.J.; Isaac, R.E.; Acharya, K.R.
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans A cytosolic enzyme with a di-nuclear active site
FEBS open bio
5
292-302
2015
Caenorhabditis elegans (O44750), Caenorhabditis elegans
brenda
Giannoglou, M.; Alexandrakis, Z.; Stavros, P.; Katsaros, G.; Katapodis, P.; Nounesis, G.; Taoukis, P.
Effect of high pressure on structural modifications and enzymatic activity of a purified X-prolyl dipeptidyl aminopeptidase from Streptococcus thermophilus
Food Chem.
248
304-311
2018
Streptococcus thermophilus, Streptococcus thermophilus ACA DC 0022
brenda
Peng, C.T.; Liu, L.; Li, C.C.; He, L.H.; Li, T.; Shen, Y.L.; Gao, C.; Wang, N.Y.; Xia, Y.; Zhu, Y.B.; Song, Y.J.; Lei, Q.; Yu, L.T.; Bao, R.
Structure-function relationship of aminopeptidase P from Pseudomonas aeruginosa
Front. Microbiol.
8
2385
2017
Pseudomonas aeruginosa (A0A069Q0X9)
brenda
Matsushita-Morita, M.; Tada, S.; Suzuki, S.; Hattori, R.; Kusumoto, K.I.
Enzymatic characterization of a novel Xaa-Pro aminopeptidase XpmA from Aspergillus oryzae expressed in Escherichia coli
J. Biosci. Bioeng.
124
534-541
2017
Aspergillus oryzae (Q2U7S5), Aspergillus oryzae, Aspergillus oryzae RIB 40 (Q2U7S5), Aspergillus oryzae ATCC 42149 (Q2U7S5)
brenda
Arreola, R.; Villalpando, J.L.; Puente-Rivera, J.; Morales-Montor, J.; Rudino-Pinera, E.; Alvarez-Sanchez, M.E.
Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme
Mol. Biotechnol.
60
563-575
2018
Trichomonas vaginalis (A2F8Y2), Trichomonas vaginalis
brenda
Drendel, V.; Heckelmann, B.; Chen, C.Y.; Weisser, J.; Espadas, G.; Schell, C.; Sabido, E.; Werner, M.; Jilg, C.A.; Schilling, O.
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
Oncotarget
8
100066-100078
2017
Homo sapiens (O43895), Homo sapiens (Q9NQW7), Homo sapiens
brenda
Yang, M.; Zheng, J.; Jia, H.; Song, M.
Functional characterization of X-prolyl aminopeptidase from Toxoplasma gondii
Parasitology
143
1443-1449
2016
Toxoplasma gondii, Toxoplasma gondii RH
brenda
Chang, H.C.; Kung, C.C.; Chang, T.T.; Jao, S.C.; Hsu, Y.T.; Li, W.S.
Investigation of the proton relay system operative in human cystosolic aminopeptidase P
PLoS ONE
13
e0190816
2018
Homo sapiens (Q9NQW7), Homo sapiens
brenda
Are, V.; Kumar, A.; Goyal, V.; Gotad, S.; Ghosh, B.; Gadre, R.; Jamdar, S.; Makde, R.
Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases
Proteins
87
212-225
2018
Deinococcus radiodurans (Q9RUY4), Deinococcus radiodurans ATCC 13939 (Q9RUY4), Deinococcus radiodurans DSM 20539 (Q9RUY4), Deinococcus radiodurans JCM 16871 (Q9RUY4), Deinococcus radiodurans LMG 4051 (Q9RUY4), Deinococcus radiodurans NBRC 15346 (Q9RUY4), Deinococcus radiodurans NCIMB 9279 (Q9RUY4), Deinococcus radiodurans R1 (Q9RUY4), Deinococcus radiodurans VKM B-1422 (Q9RUY4), Escherichia coli (P76524), Mycobacterium tuberculosis (I6YDN6), Mycobacterium tuberculosis ATCC 25618 (I6YDN6), Mycobacterium tuberculosis H37Rv (I6YDN6)
brenda
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