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(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
(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
-
-
-
?
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
?
-
-
-
?
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
Ala-Pro-4-nitroanilide + H2O
Ala + Pro-4-nitroanilide
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
Ala-Pro-p-nitroanilide + H2O
Ala + Pro-p-nitroanilide
-
-
-
-
?
Ala-Pro-Tyr-Ala + H2O
Ala + Pro-Tyr-Ala
allostatin 1 + H2O
Ala + ?
-
-
cleavage of the Ala1-Pro2 bond
?
APKPKFIRF-amide + H2O
?
-
-
-
-
?
Arg-homoPro-Pro-Ala-NH2 + H2O
?
-
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
Arg-Pro-Lys-Pro + H2O
?
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Leu-Gly-Met-NH2 + H2O
?
-
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
Arg-Pro-Pro-benzylamide + H2O
Arg + Pro-Pro-benzylamide
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
Arg-Pro-Pro-Gly-Phe-Ser + H2O
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Asp-Pro-Gly-Phe-Tyr + H2O
?
-
-
-
-
?
beta-casomorphin + H2O
?
-
-
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
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
-
-
?
bradykinin + H2O
des-Arg-bradykinin + L-Arg
-
-
-
-
?
bradykinin + H2O
L-Arg + des-Arg-bradykinin
-
-
-
-
?
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
-
-
?
des-Arg9-bradykinin + H2O
?
-
-
-
-
?
FLRF-amide + H2O
?
-
-
-
-
?
FMRF-amide + H2O
?
-
-
-
-
?
FPHFD + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
FPHFD + H2O
L-Phe + PHFD
-
a hemoglobin peptide
-
-
?
Glu-Pro-p-nitroanilide + H2O
Glu + Pro-p-nitroanilide
-
-
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly + Pro-2-naphthylamide
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Gly + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
Gly-Pro-Arg-Pro + H2O
?
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
Gly + Pro-Gly-Gly
-
-
-
?
Gly-Pro-hydroxyPro + H2O
Gly + Pro-hydroxyPro
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
Gly-Pro-p-nitroanilide + H2O
Gly + Pro-p-nitroanilide
-
-
-
-
?
Gly-Pro-Pro-p-nitroanilide + H2O
Gly + Pro-Pro-p-nitroanilide
-
-
-
-
?
His-Pro-p-nitroanilide + H2O
His + Pro-p-nitroanilide
-
-
-
-
?
K(Dnp)PPGFSPK(Abz)NH2 + H2O
?
-
-
-
-
?
K(Dnp)PPGK(Abz)NH2 + H2O
?
-
-
-
-
?
K(Dnp)PPK(Abz)NH2 + H2O
?
-
-
-
-
?
KHEYLRF-amide + H2O
?
-
-
-
-
?
KNEFIRF-amide + H2O
?
-
-
-
-
?
KPNFLRF-amide + H2O
?
-
-
-
-
?
KPSFVRF-amide + H2O
?
-
-
-
-
?
KPSFVRFamide + H2O
Lys + PSFVRFamide
-
a neuropeptide
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
L-Ala-L-Pro-L-Ala
L-Ala + L-Pro-L-Ala
-
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
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-L-Pro-L-Pro + H2O
L-Arg + L-Pro-L-Pro
-
-
-
-
?
L-Arg-L-Pro-L-Pro-Gly + H2O
L-Arg + L-Pro-L-Pro-Gly
-
-
-
-
?
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-L-Pro-L-Pro + H2O
L-Ile + L-Pro-L-Pro
-
-
-
-
?
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-Leu-L-Pro-L-Pro + H2O
L-Leu + L-Pro-L-Pro
-
-
-
-
?
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Met-L-Ala-L-Ser + H2O
L-Met + L-Ala-L-Ser
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
L-Met-L-Ser-Gly + H2O
L-Met + L-Ser-Gly
-
-
-
-
?
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-L-Pro-Gly + H2O
L-Phe + L-Pro-Gly
L-Phe-L-Pro-L-Ala + H2O
L-Phe + L-Pro-L-Ala
L-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Phe + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Pro + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides
-
-
?
L-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ser + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Trp + Pro-7-amido-4-carbamoylmethylcoumarin
-
best substrate
-
-
?
L-Tyr-L-Pro-L-Phe-NH2 + H2O
L-Tyr + L-Pro-L-Phe-NH2
-
-
-
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Val-L-Pro-L-Leu + H2O
L-Val + L-Pro-L-Leu
-
-
-
?
L-Val-L-Pro-L-Pro + H2O
L-Val + L-Pro-L-Pro
-
-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
LemTRP-1 + H2O
Ala + PSGFLGVRamide
-
i.e. APSGFLGVRamide
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-Ala-Pro + H2O
Leu + Ala-Pro
-
-
-
-
?
Leu-Pro-Gly-Gly + H2O
Leu + Pro-Gly-Gly
-
-
-
?
Leu-Pro-Pro + H2O
Leu + Pro-Pro
-
-
-
-
?
leucine rich repeat containing 50 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
Lys-Pro-Arg + H2O
Lys + Pro-Arg
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys + Pro-p-nitroanilide
-
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
Met-Pro-Ala + H2O
Met + Pro-Ala
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
-
-
?
Nepsilon-(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
-
-
-
-
?
neuropeptide Y + H2O
Tyr + ?
-
-
cleavage of the Try1-Pro2 bond
?
papain + H2O
?
-
reduced and carboxymethylated, with the N-terminal sequence Ile-Pro-Glu-Tyr-Val
-
-
?
PPGFSPFR + H2O
Pro + PGFSPFR
low activity
-
?
Pro-Pro-Gly-(Pro-Pro-Gly)4 + H2O
?
-
-
-
-
?
RNKFEFIRF-amide + H2O
?
-
-
-
-
?
RPPGFSPFR + H2O
L-Arg + PPGFSPFR
-
i.e. bradykinin
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser + Pro-p-nitroanilide
-
-
-
-
?
Substance P + H2O
?
-
-
-
-
?
substance P + H2O
Arg + des-Arg-substance P
substance P + H2O
Arg + PKPQQFFGLM
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
substance P + H2O
L-Arg + PKPQQFFGLM
-
-
-
?
Tyr-Ala-Ala + H2O
Tyr + Ala-Ala
Tyr-Pro-Ala + H2O
Tyr + Pro-Ala
Tyr-Pro-Leu-Gly-NH2 + H2O
?
-
-
-
-
?
Tyr-Pro-Phe + H2O
?
-
-
-
-
?
Tyr-Pro-Phe-Pro + H2O
?
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly + H2O
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
?
YPWTQ + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
YPWTQ + H2O
L-Tyr + PWTQ
-
a hemoglobin peptide
-
-
?
additional information
?
-
(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
-
-
-
-
?
(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
-
-
-
-
?
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
-
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
-
-
-
?
Ala-Pro-Tyr-Ala + H2O
Ala + Pro-Tyr-Ala
-
-
-
?
Ala-Pro-Tyr-Ala + H2O
Ala + Pro-Tyr-Ala
-
-
-
?
Ala-Pro-Tyr-Ala + H2O
Ala + Pro-Tyr-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg + Pro-Ala
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
-
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
-
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
-
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
?
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
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
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
-
-
-
?
Gly-Pro-Gly-Gly + H2O
?
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
?
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
?
-
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
-
best substrate
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
best substrate
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
best substrate
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
-
-
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
?
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
-
-
-
-
?
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
-
-
-
?
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
-
-
-
?
L-Phe-L-Pro-Gly + H2O
L-Phe + L-Pro-Gly
-
-
-
?
L-Phe-L-Pro-Gly + H2O
L-Phe + L-Pro-Gly
-
-
-
?
L-Phe-L-Pro-L-Ala + H2O
L-Phe + L-Pro-L-Ala
-
-
-
?
L-Phe-L-Pro-L-Ala + H2O
L-Phe + L-Pro-L-Ala
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
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
-
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
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
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Pro-Pro + H2O
Pro
-
-
-
-
?
Pro-Pro + H2O
Pro
-
-
-
-
?
Pro-Pro + H2O
Pro
-
-
-
?
Pro-Pro-Ala + H2O
?
-
-
-
-
?
Pro-Pro-Ala + H2O
?
-
-
-
-
?
substance P + H2O
Arg + des-Arg-substance P
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PKPQQFFGLM
?
substance P + H2O
Arg + des-Arg-substance P
-
-
?
Tyr-Ala-Ala + H2O
Tyr + Ala-Ala
-
-
-
?
Tyr-Ala-Ala + H2O
Tyr + Ala-Ala
-
-
-
?
Tyr-Pro-Ala + H2O
Tyr + Pro-Ala
-
-
-
?
Tyr-Pro-Ala + H2O
Tyr + Pro-Ala
-
-
-
?
Tyr-Pro-Phe-Pro-Gly + H2O
?
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly + H2O
?
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
?
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
?
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
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
?
-
-
no activity with Gly-Pro-hydroxyPro
-
?
additional information
?
-
a proline-specific APaseP
-
-
?
additional information
?
-
-
a proline-specific APaseP
-
-
?
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
?
-
-
no cleavage of human erythropoietin
-
-
?
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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Sn2+
-
10 mM, strong inhibitory effect
Ca2+
slight activation at 10 mM
Ca2+
-
0.5-1.0 mM, slight activation
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+
strong activation at 0.01-1.0 mM, inhibitory at 10 mM
Co2+
-
stimulatory at 0.01 mM, inhibitory above 0.1 mM
Co2+
-
0.03 mM, activates
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+
-
10 mM, moderate inhibitory effect
Co2+
-
metal ion required, Co2+ is the best activator
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Co2+
or Mn2+, Zn2+, required. Maximal activity at 3 mM
Cu2+
-
0.1 mM, moderate inhibitory effect
Cu2+
-
10 mM, strong inhibitory effect
Fe2+
slight activation at 0.05 mM, complete inhibition at 1 mM
Fe2+
in a metal:protein ratio of 0.07:1
Mg2+
activates
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mg2+
stimulation of the enzyme
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+
-
0.25-1 mM activates
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, sharp optimum at 0.37 mM
Mn2+
-
0.05 mM, 3-4fold activatiion
Mn2+
-
0.005 mM, 3fold activation
Mn2+
-
2 ions per enzyme molecule, ligand binding structure determination
Mn2+
-
may substitute for Co2+
Mn2+
-
wild-type and mutat R404A, binding of Mn2+ with a stoichiometry of 2 per monomer
Mn2+
2 mol of Mn2+ ions per mol of enzyme
Mn2+
required for activity
Mn2+
-
required, maximal activity at 0.05 mM
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+
-
the enzyme is double Mn2+-dependent for its activity
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+
-
1 mM, 6.8fold stimulates
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+
-
0.3-0.4 mM, 4fold stimulation with Gly-Pro-Hyp as substrate
Mn2+
-
required, maximal activity at 0.05 mM
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+
stimulation of the enzyme, most effective at 4 mM
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+
-
stimulates, optimal activity at 4 mM
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
Mn2+
or Co2+, Zn2+, required. Maximal activity at 20 mM
Mn2+
-
required, activates
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
Ni2+
-
may substitute for Co2+
Ni2+
-
1 mM, 26% increase in activity
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+
in a metal:protein ratio of 0.11:1
Zn2+
-
1 mM, 2fold increase in activity
Zn2+
-
0.01 mM, moderate inhibitory effect
Zn2+
-
10 mM, strong inhibitory effect
Zn2+
-
mono-zinc-containing enzyme, lacks any of the typical metal binding motifs found in other zinc metalloproteases
Zn2+
or Mn2+, Co2+, required. Maximal activity at 0.4 mM
additional information
rXpmA is a metalloprotease
additional information
-
rXpmA is a metalloprotease
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
metalloprotease
additional information
-
metalloprotease
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
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
-
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
a metalloprotease
additional information
-
a metalloprotease
additional information
XPNPEP1 is a metallopeptidase
additional information
XPNPEP1 is a metallopeptidase
additional information
-
XPNPEP1 is a metallopeptidase
additional information
XPNPEP2 is a metallopeptidase
additional information
XPNPEP2 is a metallopeptidase
additional information
-
XPNPEP2 is a metallopeptidase
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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(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
4-chloromercuriphenyl sulfonic acid
4-hydroxymercuribenzenesulfonate
-
-
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
Arg-Pro
substrate inhibition at concentrations above 3 mM
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
diethyldicarbonate
50% inhibition at 0.011 mM
diisopropylphosphofluoridate
-
-
enalapril
-
significant inhibition after repeated oral dosage
enalaprilat
-
inhibition only in presence of Mn2+
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
Fe2+
slight activation at 0.05 mM, complete inhibition at 1 mM
glutathione
10% inhibition at 1 mM in absence of cations
hydrazine
inactivates wild-type hcAMPP and R535A mutant enzymes
L-Ala-(N-methyl)L-Ala-L-Ala
competitive
L-Ala-L-Ala-L-Ala
competitive
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
Leu-Pro
substrate inhibition at concentrations above 4 mM
N-benzyloxycarbonyl-Pro-prolinal
-
-
N-[1-(R,S)-carboxy-(2-phenylethyl)]-thiopropanoic acid
-
-
nitrilotriacetic acid
-
-
pepstatin A
complete inhibition at 0.1-5.0 mM
Peptides with N-terminal Pro
-
product inhibition
phenylmethylsulfonyl fluoride
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
Ser-Pro
substrate inhibition at concentrations above 10 mM
(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
-
-
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
-
-
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
-
-
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
-
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
-
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
-
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
complete inhibition at 0.1 mM
1,10-phenanthroline
-
50% inhibition at 0.01 mM
1,10-phenanthroline
50% inhibition at 0.036 mM
1,10-phenanthroline
complete inhibition at 5.0 mM
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
slow-binding inhibitors
-
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
slow-binding inhibitors
-
2-mercaptoethanol
-
2-mercaptoethanol
50% inhibition at 0.043 mM
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
inhibits cleavage of Arg-Pro-Pro
4-chloromercuriphenyl sulfonic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
inhibits hydrolysis of Gly-Pro-Hyp, activates hydrolysis of bradykinin
4-hydroxymercuribenzoate
-
partial
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
amastatin
-
-
Aprotinin
-
slight
apstatin
-
-
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
apstatin
complete inhibition at 0.1 mM
apstatin
-
specific inhibitor, in vivo
apstatin
-
50% inhibition at 0.0023 mM
apstatin
-
a APP inhibitor
apstatin
-
selective for aminopeptidase P
Ba2+
-
-
Ba2+
slight inhibition at 1-5 mM
bestatin
-
-
bestatin
50% inhibition at 0.1 mM
bradykinin
-
-
bradykinin
-
hydrolysis of Gly-Pro-Hyp
Ca2+
-
only inhibits Mn2+-activated enzyme
Ca2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Ca2+
83.1% inhibition at 1 mM
Ca2+
-
1 mM CaCl2, 27% inhibition
Ca2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Ca2+
slight inhibition at 1-5 mM
captopril
-
-
Cd2+
-
-
Cd2+
complete inhibition at 0.01-5.0 mM
Co2+
strong activation at 0.01-1.0 mM, inhibitory at 10 mM
Co2+
-
only inhibits Mn2+-activated enzyme
Co2+
-
stimulatory at 0.01 mM, inhibitory above 0.1 mM
Co2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Co2+
-
1.5 mM CoCl2, complete inhibition
Co2+
-
1 mM CoCl2, 90% inhibition
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Cu2+
-
-
Cu2+
56% inhibition at 0.1 mM
Cu2+
complete inhibition at 1 mM
Cu2+
-
inhibitory effect at 1 mM
Cu2+
complete inhibition at 4 mM
Cu2+
-
0.04-4.0 mM 4CuCl2
dithiothreitol
-
DTT
-
EDTA
10 mM EDTA inhibits enzyme activity to 0.26 times of the control level
EDTA
80% inhibition at 0.1 mM
EDTA
-
reactivation by Mn2+, Co2+, Cd2+, or Ni2+
EDTA
-
0.1-1 mM, completely
EDTA
49% inhibition at 1 mM
EDTA
-
the activity of the enzyme drops to 10% after treatment with 50 mM EDTA
EDTA
50% inhibition at 0.34 m
EDTA
90% inhibition at 0.1 mM
EGTA
-
-
Hg2+
-
-
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mg2+
38.2% inhibition at 1 mM
Mg2+
slight inhibition at 1-5 mM
Mn2+
-
-
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
Mn2+
-
above, 0.01 mM, hydrolysis of bradykinin and Arg-Pro-Pro
NaCl
-
above 0.25 M
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
NaCl
-
2 M, complete inhibition
NEM
-
-
NEM
50% inhibition at 0.079 mM
Ni2+
-
Ni2+
complete inhibition at 0.001 mM
Ni2+
93.5% inhibition at 1 mM
Ni2+
-
inhibitory effect at 1 mM
Pb2+
-
-
PCMB
-
inhibits cleavage of Arg-Pro-Pro
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
PMSF
-
-
PMSF
60% inhibition at 5.0 mM
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
-
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
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
-
ramiprilat
-
inhibition only in presence of Mn2+
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+
complete inhibition at 1 mM
Zn2+
complete inhibition at 0.001 mM
Zn2+
complete inhibition at 0.1 mM
Zn2+
-
inhibitory effect at 1 mM
Zn2+
the Zn2+ ion has high affinity for APPro and inhibits the hydrolysis reaction by occupying a third metal binding site
Zn2+
-
10 mM, complete inhibition
Zn2+
-
1 mM ZnSO4, 96% inhibition
Zn2+
complete inhibition at 4 mM
Zn2+
complete inhibition at 0.01-5.0 mM
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
-
not inhibitory: bestatin, phosphoamidon
-
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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3
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
0.22
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
0.087 - 0.14
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
0.087 - 0.14
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
0.15
Arg-homoPro-Pro-Ala-NH2
-
-
0.0007
Arg-Pro-Pro-benzylamide
-
-
0.048 - 0.34
Arg-Pro-Pro-Gly-Phe
0.032 - 0.15
Arg-Pro-Pro-Gly-Phe-Ser
0.051 - 0.25
Arg-Pro-Pro-Gly-Phe-Ser-Pro
0.039 - 0.15
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe
0.076
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
0.056
des-Arg9-bradykinin
-
pH 7.4, 37°C
0.4697
Gly-Pro-4-nitroanilide
-
pH 8, 37°C
13.82
Gly-Pro-Pro-p-nitroanilide
-
-
0.018
K(Dnp)PPGFSPK(Abz)NH2
-
-
0.02
K(Dnp)PPGK(Abz)NH2
-
-
0.019
K(Dnp)PPK(Abz)NH2
-
-
0.51 - 16.9
L-Ala-L-Pro-4-nitroanilide
0.77
L-Ala-L-Pro-L-Ala
wild-type, pH 8.1, 37°C
0.308 - 0.837
L-Arg-L-Pro-L-Pro
0.03
L-Arg-L-Pro-L-Pro-Gly
-
-
-
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
0.96
L-Met-L-Pro
pH 5.0, 80°C
1.33
L-Tyr-L-Pro-L-Phe-NH2
-
-
-
13.6
L-Val-L-Pro-L-Pro
-
pH 7, temperature not specified in the publication
0.038 - 0.1
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
0.00883
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide
recombinant enzyme, pH 7.5, 30°C
0.077
Substance P
pH 8.2, 37°C, recombinant wild-type enzyme
0.72
Tyr-Ala-Ala
pH 7.5, 40°C
1.8
Tyr-Pro-Ala
pH 7.5, 40°C
0.72
Tyr-Pro-Leu-Gly-NH2
-
-
1.02 - 1.6
Tyr-Pro-Phe-Pro-Gly
0.6 - 1.4
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
additional information
additional information
-
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
0.087
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
wild-type, pH 8.1, 37°C
0.14
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
mutant H350, pH 8.1, 37°C
2.1
Arg-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
3.5
Arg-Pro-Ala
pH 8.0, 55°C, recombinant mutant R55A
6
Arg-Pro-Ala
pH 8.0, 55°C, recombinant mutant D53A
8.4
Arg-Pro-Ala
pH 8.0, 55°C, recombinant mutant Y56A
0.16
Arg-Pro-Pro
-
-
0.35
Arg-Pro-Pro
-
without Mn2+
0.36
Arg-Pro-Pro
-
in presence of 4 mM Mn2+
0.048
Arg-Pro-Pro-Gly-Phe
-
-
0.34
Arg-Pro-Pro-Gly-Phe
-
-
0.032
Arg-Pro-Pro-Gly-Phe-Ser
-
-
0.15
Arg-Pro-Pro-Gly-Phe-Ser
-
-
0.051
Arg-Pro-Pro-Gly-Phe-Ser-Pro
-
-
0.25
Arg-Pro-Pro-Gly-Phe-Ser-Pro
-
-
0.039
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe
-
-
0.15
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe
-
-
0.021
bradykinin
-
-
0.045
bradykinin
-
pH 8.0, 35°C
0.047
bradykinin
-
mutant R404A, pH 7.5, 37°C
0.058
bradykinin
-
37°C, wild-type enzyme
0.075
bradykinin
-
pH 7.4, 37°C
0.078
bradykinin
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
0.101
bradykinin
pH 8.2, 37°C, recombinant wild-type enzyme
0.14
bradykinin
-
pH 7.5, 37°C
0.144
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
0.16
bradykinin
-
mutant R153W/R370L, pH 7.5, 37°C
0.163
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
0.17
bradykinin
pH 7.5, 37°C, recombinant wild-type enzyme
0.18
bradykinin
-
mutant R153L/R370L, pH 7.5, 37°C
0.2
bradykinin
pH 7.5, 37°C, recombinant mutant Y527F
0.21
bradykinin
-
mutant R370L, pH 7.5, 37°C
0.327
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
0.35
bradykinin
pH 7.5, 37°C, recombinant mutant R535A
0.391
bradykinin
-
37°C, mutant H519L
0.41
bradykinin
-
mutant R404K, pH 7.5, 37°C
0.42
bradykinin
-
mutant R153A, pH 7.5, 37°C
0.43
bradykinin
-
mutant R153W, pH 7.5, 37°C
0.5
bradykinin
-
37°C, mutant H519K
0.51
bradykinin
-
mutant R153L, pH 7.5, 37°C
0.6396
bradykinin
-
pH 8, 37°C
0.78
bradykinin
-
wild-type, pH 7.5, 37°C
0.84
bradykinin
-
mutant Y387F, pH 7.5, 37°C
0.97
bradykinin
-
pH 6.5, 37°C
1.02
bradykinin
-
mutant W88L, pH 7.5, 37°C
6.7
bradykinin
-
pH 5.5, 37°C
0.51
FPHFD
-
pH 7.5, 37°C
0.86
FPHFD
-
pH 5.5, 37°C
0.32
Gly-Pro-Hyp
-
without Mn2+
2
Gly-Pro-Hyp
-
in presence of 4 mM Mn2+
0.51
L-Ala-L-Pro-4-nitroanilide
-
chimera th-sl cAPP, pH 7.0, 30°C
0.51
L-Ala-L-Pro-4-nitroanilide
chimera th-sl cAPP, pH 7.0, 30°C
1.4
L-Ala-L-Pro-4-nitroanilide
-
recombinant enzyme, pH 7.4, 30°C
1.5
L-Ala-L-Pro-4-nitroanilide
native enzyme, pH 7.4, 30°C
1.7
L-Ala-L-Pro-4-nitroanilide
recombinant enzyme, pH 7.4, 30°C
16.9
L-Ala-L-Pro-4-nitroanilide
-
chimera sl-th cAPP, pH 8.2, 30°C
16.9
L-Ala-L-Pro-4-nitroanilide
chimera sl-th cAPP, pH 8.2, 30°C
0.308
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
0.837
L-Arg-L-Pro-L-Pro
-
pH 7.4, 37°C
0.038
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
0.1
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
0.15
Met-Ala-Ala
pH 8.0, 55°C, recombinant wild-type
0.23
Met-Ala-Ala
pH 8.0, 55°C, recombinant wild-type
0.46
Met-Ala-Ala
pH 8.0, 55°C, recombinant wild-type
6.3
Met-Pro
pH 8.0, 55°C, recombinant wild-type
7.9
Met-Pro
pH 8.0, 55°C, recombinant wild-type
11.9
Met-Pro
pH 8.0, 55°C, recombinant wild-type
1.9
Met-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
2
Met-Pro-Ala
pH 7.5, 40°C
3
Met-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
3.9
Met-Pro-Ala
pH 8.0, 55°C, recombinant mutant Y56A
4
Met-Pro-Ala
pH 8.0, 55°C, recombinant mutant D53A
6.1
Met-Pro-Ala
pH 8.0, 55°C, recombinant mutant R55A
9
Met-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
1.02
Tyr-Pro-Phe-Pro-Gly
-
-
1.6
Tyr-Pro-Phe-Pro-Gly
-
-
0.6
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
-
-
1.4
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
-
-
1.4
YPWTQ
-
pH 7.5, 37°C
additional information
additional information
-
-
-
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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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 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
-
enzyme TgAPP is a member of the M24 prolyl aminopeptidase family
-
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
-
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
-
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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
?
-
x * 71000, recombinant His-tagged fusion protein, SDS-PAGE, x * 68000, W03G9.4 protein, SDS-PAGE
?
-
x * 81500 + x * 89000, SDS-PAGE
?
x * 71000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 72000, recombinant enzyme, SDS-PAGE
?
x * 105000, recombinant GST-fusion protein, SDS-PAGE
?
-
x * 91000, reducing conditions, SDS-PAGE
?
-
non-reducing conditions, SDS-PAGE
?
-
x * 91000, wild-type enzyme, SDS-PAGE
dimer
2 * 71000, recombinant enzyme, 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 * 69000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 69000, recombinant His-tagged enzyme, SDS-PAGE
-
homodimer
-
2 * 69000, recombinant His-tagged enzyme, SDS-PAGE
-
homodimer
2 * 71977, recombinant His-tagged enzyme without the start Met, mass spectrometry
homodimer
2 * 37100, SDS-PAGE
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
-
2 * 37100, SDS-PAGE
-
homodimer
2 * 39600, SDS-PAGE
homodimer
-
2 * 70000, X-ray crystallography
homodimer
2 * 38700, SDS-PAGE
homodimer
-
2 * 38700, SDS-PAGE
-
homodimer
-
2 * 38700, SDS-PAGE
-
homodimer
-
2 * 73000, SDS-PAGE
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
homodimer
-
2 * 86000, SDS-PAGE
homodimer
-
2 * 86000, SDS-PAGE
-
homodimer
-
2 * 86000, SDS-PAGE
-
monomer
-
1 * 40000, SDS-PAGE
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
-
monomer
1 * 50000, about, mass spectrometry
tetramer
-
x * 95000, reducing conditions, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
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
tetramer
-
SDS-PAGE, 4* 60000
tetramer
4 * 55000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
-
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
-
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
-
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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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
R298A
site-directed mutagenesis
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R298A
-
site-directed mutagenesis
-
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
-
R153A
-
enzymic activity similar to wild-type
R153L
-
enzymic activity similar to wild-type
R153L/R370L
-
decrease in Km-value
R153W
-
enzymic activity similar to wild-type
R153W/R370L
-
decrease in Km-value
R370L
-
enzymic activity similar to wild-type
R404A
-
decrease both in KM- and kcat-value
R404K
-
decrease in kcat-value
W88L
-
enzymic activity similar to wild-type
Y387F
-
decrease in kcat-value
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
D449A
-
site-directed mutagenesis, inactive mutant
D449N
-
site-directed mutagenesis, inactive mutant
D460A
-
site-directed mutagenesis, inactive mutant
D460N
-
site-directed mutagenesis, inactive mutant
E554A
-
site-directed mutagenesis, inactive mutant
E554Q
-
site-directed mutagenesis, inactive mutant
E568A
-
site-directed mutagenesis, inactive mutant
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
H429K
-
site-directed mutagenesis, inactive mutant
H429L
-
site-directed mutagenesis, inactive mutant
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
H523K
-
site-directed mutagenesis, inactive mutant
H523L
-
site-directed mutagenesis, inactive mutant
H532K
-
site-directed mutagenesis, inactive mutant
H532L
-
site-directed mutagenesis, very low expression level in COS-1 cells, protein degradation, inactive mutant
D260A
no enzymic activity
D260A
MnA is bound at the active site, but the MnB site is empty. Loss of catalytic activity
D271A
no enzymic activity
D271A
no atoms of Mn(II) are bound at the active site. Loss of catalytic activity
E383A
no enzymic 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
no enzymic activity
H243A
crystallization data. Mutant is capable of binding the substrate L-Val-L-Pro-L-Leu
H243A
loss of catalytic acitivity. H243 stabilizes substrate binding
H350A
reduced enzymic activity
H350A
loss of catalytic activity. H350 forms part of a hydrophobic binding pocket that gives the enzym its proline specificity
H354A
no enzymic activity
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
H361A
no enzymic activity
H361A
loss of catalytic activity
H361A
crystallization data. Mutant has residual 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
-
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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Chen, K.C.S.; Buchanan, T.M.
Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase
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255
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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
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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
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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
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1988
Rattus norvegicus
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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
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226
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1983
Saccharomyces cerevisiae
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Miller, C.G.; Green, L.
Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium
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153
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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
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1980
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Yaron, A.; Berger, A.
Aminopeptidase-P
Methods Enzymol.
19
521-534
1970
Escherichia coli
-
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Yaron, A.; Mlynar, D.
Aminopeptidase-P
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32
658-663
1968
Escherichia coli, Escherichia coli B / ATCC 11303
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Fleminger, G.; Carmel, A.; Goldenberg, D.; Yaron, A.
Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung
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125
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1982
Bos taurus, Escherichia coli, Homo sapiens
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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
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34
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1995
Rattus norvegicus
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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
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267
4897-4903
1992
Bos taurus
brenda
Harbeck, H.T.; Mentlein, R.
Aminopeptidase P from rat brain. Purification and action on bioactive peptides
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198
451-458
1991
Rattus norvegicus
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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
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52
229-236
1996
Sus scrofa
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Orawski, A.T.; Susz, J.P.; Simmons, W.H.
Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation
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75
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Bos taurus
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Lloyd, G.S.; Habgood, N.T.; Hooper, N.M.; Turner, A.J.
Aminopeptidase P: immunoaffinity purification and molecular characterisation
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236S
21
1993
Sus scrofa
-
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Vanhoof, G.; de Block, J.; de Meester, I.; Scharpe, S.; de Potter, W.P.
Localization and characterization of aminopeptidase P in bovine adrenal medulla
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21
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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
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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
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Kulkarni, G.V.; Deobagkar, D.D.
A cytosolic form of aminopeptidase P from Drosophila melanogaster: molecular cloning and characterization
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2002
Drosophila melanogaster (O96794), Drosophila melanogaster
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Hauser, F.; Strassner, J.; Schaller, A.
Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P
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2001
Solanum lycopersicum (Q93X45), Solanum lycopersicum (Q93X46), Solanum lycopersicum
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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.
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2000
Homo sapiens
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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
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2002
Homo sapiens
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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
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2004
Escherichia coli
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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
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2006
Thermococcus onnurineus NA1 (Q2QC92)
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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.
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2005
Homo sapiens
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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
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2005
Escherichia coli (P15034), Escherichia coli
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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
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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
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2006
Escherichia coli (P15034), Escherichia coli
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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.
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2005
Escherichia coli, Rattus norvegicus
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Sakamoto, K.; Sugimoto, K.; Sudoh, T.; Fujimura, A.
Different effects of imidapril and enalapril on aminopeptidase P activity in the mouse trachea
Hypertens. Res.
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Mus musculus
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Zheng, Y.; Roberts, R.J.; Kasif, S.; Guan, C.
Characterization of two new aminopeptidases in Escherichia coli
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Escherichia coli
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Graham, S.C.; Guss, J.M.
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu
Arch. Biochem. Biophys.
469
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2008
Escherichia coli (P15034), Escherichia coli
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Dalal, S.; Klemba, M.
Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum
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Plasmodium falciparum (A0A144A2H0)
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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)
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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.
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2009
Homo sapiens
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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
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Homo sapiens
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Masler, E.P.
Digestion of invertebrate neuropeptides by preparations from the free-living nematode Panagrellus redivivus
J. Helminthol.
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2008
Panagrellus redivivus
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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.
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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.
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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
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2008
Streptomyces murinus (A9E3K0)
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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
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Homo sapiens, Plasmodium falciparum
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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.
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Danio rerio, Escherichia coli, Homo sapiens (Q9NQH7), Homo sapiens
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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
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Rattus norvegicus
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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
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2014
Xanthomonas campestris
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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
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Lactococcus lactis subsp. lactis
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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
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Ustilago maydis
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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.
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2012
Mus musculus
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Nandan, A.S.; Nampoothiri, K.M.
Unveiling aminopeptidase P from Streptomyces lavendulae: molecular cloning, expression and biochemical characterization
Enzyme Microb. Technol.
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2014
Streptomyces lavendulae
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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.
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2012
Homo sapiens
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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.
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2016
Plasmodium falciparum
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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
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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.
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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)
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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
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2019
Saccharomyces cerevisiae (P40051), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P40051)
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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
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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.
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2018
Streptococcus thermophilus, Streptococcus thermophilus ACA DC 0022
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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.
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Pseudomonas aeruginosa (A0A069Q0X9)
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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)
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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
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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
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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
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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
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e0190816
2018
Homo sapiens (Q9NQW7), Homo sapiens
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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)
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