3.4.11.9: Xaa-Pro aminopeptidase
This is an abbreviated version!
For detailed information about Xaa-Pro aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.9
-
3.4.11.9
-
aminopeptidases
-
apstatin
-
xpnpep2
-
lactococci
-
medicine
- 3.4.11.9
- aminopeptidases
- apstatin
-
xpnpep2
-
lactococci
- medicine
Reaction
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide =
Synonyms
aminoacylproline aminopeptidase, aminopeptidase P, aminopeptidase P-like enzyme, aminopeptidase P1, aminopeptidase, aminoacylproline, AMPP, AP-P, APaseP, APP, APP1, APPro, DAP-P, dapUm, Dr-smAPP, Ec-smAPP, ecAPP, hAPP1, hcAMPP, Icp55, LeAPP1, LeAPP2, M24B peptidase, mAmP, Membrane-bound AmP, Membrane-bound APP, membrane-bound proline-specific APaseP, More, Mt-smAPP, Pa-PepP, PEPP, PepQ, peptidase PepQ, PepX aminopeptidase, PfAPP, proline aminopeptidase, sll0136, small aminopeptidase-P, TgAPP, TvMP50, X-Pro aminopeptidase, X-prolyl aminopeptidase, X-prolyl aminopeptidase 2, X-prolyl aminopeptidase 3, X-prolyl peptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro aminopeptidase, Xaa-Pro aminopeptidase-1, Xaa-Pro aminopeptidase-2, Xaa-Pro dipeptidase, XPD, XpmA, XPNEP2, XPNPEP-1, XPNPEP-2, XPNPEP1, XPNPEP2, XPNPEP3, YpdF
ECTree
3.4.11.9 Xaa-Pro aminopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.11.9 - Xaa-Pro aminopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
bradykinin + H2O
Arg + PPGFSPFR
i.e. RPPGFSPFR, rapid hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
des-Arg-bradykinin + Arg
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
centrosomal protein 290 kDa/NPHP6 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
FPHFD + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Gly + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Ala-L-Pro-L-Ala-2-naphthylamide + H2O
L-Ala-L-Pro-L-Ala + 2-naphthylamine
-
-
-
?
L-Ala-L-Pro-p-nitroanilide + H2O
L-Ala-L-Pro + p-nitroaniline
-
-
-
?
L-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ala + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Arg + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Asn-L-Pro-L-Thr-L-Asn-L-Leu-L-His + H2O
L-Asn + L-Pro-L-Thr-L-Asn-L-Leu-L-His
-
-
-
-
?
L-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-ASn + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Asp + Pro-7-amido-4-carbamoylmethylcoumarin
-
low activity
-
-
?
L-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Gln + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Glu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-His + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ile + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Leu 7-amido-4-carbamoylmethylcoumarin + H2O
L-Leu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Met + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Nle-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Nle + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Phe + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Pro + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides
-
-
?
L-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ser + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Trp + Pro-7-amido-4-carbamoylmethylcoumarin
-
best substrate
-
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
-
?
leucine rich repeat containing 50 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
Nalpha-(2-aminobenzoyl)-Lys-Pro-Pro 4-nitroanilide + H2O
Nalpha-(2-aminobenzoyl)-Lys + Pro-Pro-4-nitroanilide
-
-
?
papain + H2O
?
-
reduced and carboxymethylated, with the N-terminal sequence Ile-Pro-Glu-Tyr-Val
-
-
?
substance P + H2O
Arg + PKPQQFFGLM
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
YPWTQ + H2O
?
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
-
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
i.e. bradykinin
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
i.e. bradykinin
one Arg is released per mol of bradykinin in less than 5 min, the following Pro residue is released within 1 h
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
bradykinin + H2O
?
-
potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
i.e. RPPGFSPFR, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PPGFSPFR
?
bradykinin + H2O
Arg + des-Arg-bradykinin
i.e. RPPGFSPFR, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PPGFSPFR
?
bradykinin + H2O
Arg + des-Arg-bradykinin
hydrolysis of the N-terminal Arg1-Pro bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
enzyme activity in plasma of humans with previous angio-oedema, a rare but potentially life-threatening side-effect of angiotensin-converting enzyme inhibitor treatment, is low compared to humans without this sensitivity and might be a predisposing factor for development of angio-oedema
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
the enzyme contributes to the degradation of bradykinin in human skin, especially in case of angiotensin-converting enzyme inhibition
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Streptococcus thermophilus ACA DC 0022
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Streptococcus thermophilus ACA-DC 0022
-
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
-
best substrate
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
best substrate
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
Streptomyces murinus TH-4
best substrate
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
-
?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide
-
APP cleaves the Lys-Pro peptide bond separating the fluorogenic aminobenzoyl residue and the internal quenching residue 4-nitroanilide
-
-
?
substance P + H2O
Arg + des-Arg-substance P
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
i.e. PKPQQFFGLM
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
-
?
additional information
?
-
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
-
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
-
?
additional information
?
-
the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys)
-
-
?
additional information
?
-
-
the enzyme favors peptides with 2 proline residues or proline analogs in position 2 and 3 of the substrate
-
-
?
additional information
?
-
-
enzyme may be important for the modulation of the biological activity of neuropeptides
-
-
?
additional information
?
-
-
the enzyme is involved in the pulmonary inactivation of circulating bradykinin
-
-
?
additional information
?
-
-
the enzyme may have an important role in the pulmonary degradation of the potent vasoactive peptide, bradykinin
-
-
?
additional information
?
-
-
no activity with angiotensin I, des-Arg-bradykinin, AF1, i.e. KNEFIRNRVYIHPFHL, and substance P
-
?
additional information
?
-
enzyme APP specifically cleaves the N-terminal Xaa-Pro peptide bond from oligopeptides and is distinct from prolidase, which acts only on dipeptides
-
-
?
additional information
?
-
-
enzyme APP specifically cleaves the N-terminal Xaa-Pro peptide bond from oligopeptides and is distinct from prolidase, which acts only on dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
-
the enzyme can only hydrolyze the trans form of the X-L-Pro-peptide bond, the cis form has to isomerize before it can be cleaved
-
-
?
additional information
?
-
-
enzyme hydrolyzes the Xaa-Pro peptide bond when the first amino acid is Asn, Ala, or Met
-
-
?
additional information
?
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
-
?
additional information
?
-
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
-
?
additional information
?
-
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
no activity with Gly-Pro-hydroxyPro
-
?
additional information
?
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
-
?
additional information
?
-
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
-
?
additional information
?
-
-
the enzyme removes the N-terminal amino acid from peptides only where Pro, and in one case Ala, is present in the penultimate position. No hydrolysis of dipeptides even when Pro is present in the C-terminal position or when either N-termial Pro or pyroglutamate is present preceeding a Pro residue in the penultimate position of longer peptides
-
-
?
additional information
?
-
-
aminopeptidase P appears to be an important enzyme for debittering of casein-derived peptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
additional information
?
-
-
the enzyme releases only amino acid X from the NH2-termini of peptides with the general structure X-Pro-Y-Z
-
-
?
additional information
?
-
specific role in the catabolism of proline-containing peptides in both the vacuole and the cytosol, enzyme is required for efficient parasite proliferation
-
-
?
additional information
?
-
-
substrate specificity, overview. Design and synthesis of a library composed of 20 fluorogenic substrates, which is used to determine the substrate fingerprint of mature PfAPP (PfAPP, residues 121-777). The enzyme from Plasmodium falciparum can catalyze the removal of any residue immediately prior to a proline. The coupled assay uses a prolyl iminopeptidase (EC 3.4.11.5) to release the free 7-amino-4-carbamoylmethylcoumarin for fluorogenic detection
-
-
?
additional information
?
-
modeling of the Val-Pro-Leu bound Pa-PepP complex by superposing Pa-PepP structure with the substrate-bound Escherichia coli PepP structure (PDB ID 2BN7)
-
-
?
additional information
?
-
-
the enzyme liberates all unblocked preferentially basic or hydrophobic ultimate amino acids from dipeptides, tripeptides and oligopeptides with N-terminal Xaa-Pro- sequences, overview
-
-
?
additional information
?
-
-
the enzyme accounts for virtually all of the pulmonary inactivation of bradykinin injected in vitro
-
-
?
additional information
?
-
-
the enzyme probably plays an important role in conjunction with other intestinal prolyl peptidases in the digestion of proline containing peptides and proteins
-
-
?
additional information
?
-
-
the enzyme plays an important role in hydrolysis of Xaa-Pro-Yaa peptides
-
-
?
additional information
?
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is involved in degradation of peptide intermediates
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systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
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additional information
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systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
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additional information
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systemin, a peptide hormone-like signaling molecule from tomato plants, is no substrate
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additional information
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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
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additional information
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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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additional information
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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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