Any feedback?
Information on EC 3.4.11.9 - Xaa-Pro aminopeptidase
for references in articles please use BRENDA:EC3.4.11.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.11.9 Xaa-Pro aminopeptidaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
Synonyms
xpnpep2, xpnpep3, membrane-bound app, xpnpep1, appro, tgapp, tvmp50, x-prolyl-dipeptidyl aminopeptidase, aminopeptidase p1, x-prolyl aminopeptidase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoacylproline aminopeptidase
-
-
-
-
aminopeptidase P
aminopeptidase P1
aminopeptidase, aminoacylproline
-
-
-
-
AMPP
AP-P
APP
APP1
APPro
Dr-smAPP
Icp55
M24B peptidase
mAmP
-
-
-
-
Membrane-bound AmP
-
-
-
-
Membrane-bound APP
-
-
-
-
Mt-smAPP
PEPP
PepQ
peptidase PepQ
PepX aminopeptidase
proline aminopeptidase
-
-
-
-
small aminopeptidase-P
TgAPP
X-Pro aminopeptidase
X-prolyl aminopeptidase
X-prolyl aminopeptidase 2
X-prolyl aminopeptidase 3
Xaa-Pro aminopeptidase
-
-
-
-
XpmA
XPNPEP1
XPNPEP2
XPNPEP3
YpdF
additional information
aminopeptidase P
-
-
-
-
AP-P
-
-
-
-
APP
-
-
-
-
X-Pro aminopeptidase
-
-
-
-
additional information
-
the enzyme belongs to the peptidase family M24
additional information
the enzyme belongs to the peptidase family M24
additional information
the enzyme belongs to the peptidase family M24
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
-
-
-
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
acive site configuration, modeling, Asp449, Asp460, His523, Glu554, and Glu568 are in volved in metal binding in the active site, His429 and His523 are involved in shuttling protons during catalysis
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
isozyme APP-2 shows a preference for Arg-Pro-Pro-, Arg-Pro-Lys-, Pro-Pro-Gly-, -Phe-Gly- in descending order
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
H243 stabilizes substrate binding, H361 stabilizes substrate binding and the gem-diol catalytic intermediate. H350 forms part of a hydrophobic binding pocket that gives the enzyme its proline specificity
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
R404 participates in proton relay and in the hydrogen bond network
-
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
mechanism, cis-trans specificity
Escherichia coli B / ATCC 11303
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37288-66-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
?
Ala-Pro + H2O
Ala