Information on EC 3.4.11.9 - Xaa-Pro aminopeptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.4.11.9
-
RECOMMENDED NAME
GeneOntology No.
Xaa-Pro aminopeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-66-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cytosolic isoform
SwissProt
Manually annotated by BRENDA team
Escherichia coli B / ATCC 11303
-
-
-
Manually annotated by BRENDA team
subsp. cremonis AM2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild type and mutant strain that lacks peptidase P
-
-
Manually annotated by BRENDA team
-
A9E3K0
SwissProt
Manually annotated by BRENDA team
-
A9E3K0
SwissProt
Manually annotated by BRENDA team
isoform APP II
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
show the reaction diagram
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-HN-CH2-CH2-NH-o-aminobenzoyl
show the reaction diagram
-
-
-
?
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
show the reaction diagram
-
-
-
?
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
show the reaction diagram
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
show the reaction diagram
Ala-Pro + H2O
Ala + Pro
show the reaction diagram
Ala-Pro-4-nitroanilide + H2O
Ala + Pro-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
show the reaction diagram
Ala-Pro-p-nitroanilide + H2O
Ala + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
allostatin 1 + H2O
Ala + ?
show the reaction diagram
-
-
cleavage of the Ala1-Pro2 bond
?
APKPKFIRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-homoPro-Pro-Ala-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro + H2O
Arg + Pro
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Leu-Gly-Met-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro + H2O
Arg + Pro-Pro
show the reaction diagram
Arg-Pro-Pro-benzylamide + H2O
Arg + Pro-Pro-benzylamide
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
?
show the reaction diagram
Arg-Pro-Pro-Gly-Phe-Ser + H2O
?
show the reaction diagram
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
?
show the reaction diagram
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
show the reaction diagram
Asp-Pro-Gly-Phe-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casomorphin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
bradykinin + H2O
Arg + des-Arg-bradykinin
show the reaction diagram
bradykinin + H2O
Arg + PPGFSPFR
show the reaction diagram
i.e. RPPGFSPFR, rapid hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
des-Arg-bradykinin + L-Arg
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
L-Arg + des-Arg-bradykinin
show the reaction diagram
-
-
-
-
?
centrosomal protein 290 kDa/NPHP6 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
FLRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
FMRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
FPHFD + H2O
?
show the reaction diagram
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
Glu-Pro-p-nitroanilide + H2O
Glu + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
show the reaction diagram
Gly-Pro-2-naphthylamide + H2O
Gly + Pro-2-naphthylamide
show the reaction diagram
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methyl-7-coumarylamide
show the reaction diagram
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
show the reaction diagram
Gly-Pro-Arg-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
?
show the reaction diagram
Gly-Pro-Gly-Gly + H2O
Gly + Pro-Gly-Gly
show the reaction diagram
-
-
-
?
Gly-Pro-hydroxyPro + H2O
Gly + Pro-hydroxyPro
show the reaction diagram
-
-
-
?
Gly-Pro-Hyp + H2O
Gly + Pro-Hyp
show the reaction diagram
Gly-Pro-p-nitroanilide + H2O
Gly + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Gly-Pro-Pro-p-nitroanilide + H2O
Gly + Pro-Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
His-Pro-p-nitroanilide + H2O
His + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
K(Dnp)PPGFSPK(Abz)NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
K(Dnp)PPGK(Abz)NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
K(Dnp)PPK(Abz)NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
KHEYLRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
KNEFIRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
KPNFLRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
KPSFVRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
KPSFVRFamide + H2O
Lys + PSFVRFamide
show the reaction diagram
-
a neuropeptide
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala + L-Pro-4-nitroanilide
show the reaction diagram
L-Ala-L-Pro-L-Ala
L-Ala + L-Pro-L-Ala
show the reaction diagram
-
-
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
show the reaction diagram
-
-
-
-
?
L-Ala-L-Pro-L-Ala-2-naphthylamide + H2O
L-Ala-L-Pro-L-Ala + 2-naphthylamine
show the reaction diagram
Q8IKT5;
-
-
-
?
L-Ala-L-Pro-p-nitroanilide + H2O
L-Ala-L-Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Arg-L-Pro-L-Pro + H2O
L-Arg + L-Pro-L-Pro
show the reaction diagram
-
-
-
-
?
L-Arg-L-Pro-L-Pro + H2O
L-Arg-L-Pro + L-Pro
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
L-Ile-L-Pro-L-Pro + H2O
L-Ile + L-Pro-L-Pro
show the reaction diagram
-
-
-
-
?
L-Leu-L-Pro-L-Pro + H2O
L-Leu + L-Pro-L-Pro
show the reaction diagram
-
-
-
-
?
L-Met-L-Ala-L-Ser + H2O
L-Met + L-Ala-L-Ser
show the reaction diagram
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
show the reaction diagram
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
show the reaction diagram
L-Met-L-Ser-Gly + H2O
L-Met + L-Ser-Gly
show the reaction diagram
-
-
-
-
?
L-Phe-L-Pro-Gly + H2O
L-Phe + L-Pro-Gly
show the reaction diagram
L-Phe-L-Pro-L-Ala + H2O
L-Phe + L-Pro-L-Ala
show the reaction diagram
L-prolyl-peptide + H2O
L-proline + peptide
show the reaction diagram
-
X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides
-
-
?
L-Val-L-Pro-L-Leu + H2O
L-Val + L-Pro-L-Leu
show the reaction diagram
-
-
-
-
?
L-Val-L-Pro-L-Pro + H2O
L-Val + L-Pro-L-Pro
show the reaction diagram
-
-
-
-
?
LemTRP-1 + H2O
Ala + PSGFLGVRamide
show the reaction diagram
-
i.e. APSGFLGVRamide
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
Leu-Ala-Pro + H2O
Leu + Ala-Pro
show the reaction diagram
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
show the reaction diagram
Leu-Pro-Gly-Gly + H2O
Leu + Pro-Gly-Gly
show the reaction diagram
-
-
-
?
Leu-Pro-Pro + H2O
Leu + Pro-Pro
show the reaction diagram
-
-
-
-
?
leucine rich repeat containing 50 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
Lys-Pro-Arg + H2O
Lys + Pro-Arg
show the reaction diagram
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Met-Pro + H2O
Met + Pro
show the reaction diagram
N-alpha-aminobenzyloxycarbonyl-Lys-Pro-Pro-4-nitroanilide + H2O
N-alpha-aminobenzyloxycarbonyl-Lys + Pro-Pro-4-nitroaniline
show the reaction diagram
-
-
?
Nepsilon-(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
neuropeptide Y + H2O
Tyr + ?
show the reaction diagram
-
-
cleavage of the Try1-Pro2 bond
?
papain + H2O
?
show the reaction diagram
-
reduced and carboxymethylated, with the N-terminal sequence Ile-Pro-Glu-Tyr-Val
-
-
?
Phe-Pro + H2O
Phe + Pro
show the reaction diagram
PPGFSPFR + H2O
Pro + PGFSPFR
show the reaction diagram
low activity
-
?
Pro-Pro + H2O
Pro
show the reaction diagram
Pro-Pro-Ala + H2O
?
show the reaction diagram
Pro-Pro-Gly-(Pro-Pro-Gly)4 + H2O
?
show the reaction diagram
-
-
-
-
?
RNKFEFIRF-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Ser-Pro + H2O
Ser + Pro
show the reaction diagram
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser + Pro-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
substance P + H2O
Arg + des-Arg-substance P
show the reaction diagram
substance P + H2O
Arg + PKPQQFFGLM
show the reaction diagram
i.e. RPKPQQFFGLM, hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
Tyr-Pro-Leu-Gly-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Tyr-Pro-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Tyr-Pro-Phe-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly + H2O
?
show the reaction diagram
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
?
show the reaction diagram
Val-Pro + H2O
Val + Pro
show the reaction diagram
YPWTQ + H2O
?
show the reaction diagram
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bradykinin + H2O
?
show the reaction diagram
-
potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
show the reaction diagram
FPHFD + H2O
?
show the reaction diagram
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
YPWTQ + H2O
?
show the reaction diagram
-
globin pentapeptide sequence, potential natural substrate, efficiently hydrolyzed by PfAPP
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
activates
Fe2+
in a metal:protein ratio of 0.07:1
Sn2+
-
10 mM, strong inhibitory effect
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
1,10-phenanthroline
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
2-mercaptoethanol
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
4-chloromercuriphenyl sulfonic acid
4-hydroxymercuribenzenesulfonate
-
-
4-hydroxymercuribenzoate
8-hydroxyquinoline
-
-
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
amastatin
antipain
-
-
Aprotinin
apstatin
bestatin
bradykinin
captopril
CH3HgCl
-
-
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
diethyldicarbonate
50% inhibition at 0.011 mM
diisopropylphosphofluoridate
-
-
dithioerythritol
-
-
dithiothreitol
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
glutathione
10% inhibition at 1 mM in absence of cations
iodoacetate
-
-
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
N-benzyloxycarbonyl-Pro-prolinal
-
-
N-[1-(R,S)-carboxy-(2-phenylethyl)]-thiopropanoic acid
-
-
nitrilotriacetic acid
-
-
pefabloc
-
-
Peptides with N-terminal Pro
-
product inhibition
phenylmethylsulfonyl fluoride
phosphoramidon
-
-
Pro-Gly-Pro
-
-
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
Pro-Pro-Ala
-
-
puromycin
-
-
ramiprilat
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuriphenyl sulfonic acid
-
inhibits hydrolysis of Gly-Pro-Hyp, activates hydrolysis of bradykinin
glutathione
activates the enzyme in presence of Mn2+ or Co2+, and slightly in presence of Zn2+
progesterone
-
exposure of HepG2 cells to 0.001 mM progesterone results in a significant increase in the AP-P activity of cell lysates
additional information
-
women on the oral contraceptive pill have higher age-adjusted plasma AP-P compared to women not on the oral contraceptive pill or males
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
-
1.23
Arg-Pro
-
-
0.16 - 1.4
Arg-Pro-Pro
0.0007
Arg-Pro-Pro-benzylamide
-
-
0.03
Arg-Pro-Pro-Gly
-
-
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
-
-
0.021 - 6.7
bradykinin
0.056
des-Arg9-bradykinin
-
pH 7.4, 37°C
0.51 - 0.86
FPHFD
0.4697
Gly-Pro-4-nitroanilide
-
pH 8, 37°C
0.32 - 40.4
Gly-Pro-Hyp
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
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
13.6
L-Val-L-Pro-L-Pro
-
pH 7, temperature not specified in the publication
0.9
Leu-Pro-Pro
-
-
0.038 - 0.1
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
0.077
Substance P
pH 8.2, 37°C, recombinant wild-type enzyme
0.72
Tyr-Pro-Leu-Gly-NH2
-
-
1.2
Tyr-Pro-Phe
-
-
1.33
Tyr-Pro-Phe-NH2
-
-
1.02 - 1.6
Tyr-Pro-Phe-Pro-Gly
0.6 - 1.4
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
1.4 - 1.8
YPWTQ
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
135
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
20
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
7.3 - 95
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
73
Arg-Pro
-
-
49 - 230
Arg-Pro-Pro
125
Arg-Pro-Pro-benzylamide
-
-
17
Arg-Pro-Pro-Gly
-
-
15 - 48
Arg-Pro-Pro-Gly-Phe
11 - 30
Arg-Pro-Pro-Gly-Phe-Ser
16 - 41
Arg-Pro-Pro-Gly-Phe-Ser-Pro
13 - 39
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe
12 - 26
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
0.17 - 160
bradykinin
5.4 - 8.6
FPHFD
48 - 69
Gly-Pro-Hyp
47.2
Gly-Pro-Pro-p-nitroanilide
-
-
1.5 - 487
L-Ala-L-Pro-4-nitroanilide
0.77
L-Ala-L-Pro-L-Ala
-
wild-type, pH 8.1, 37°C
7.7
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
541
L-Met-L-Pro
pH 5.0, 80°C
3.1
Substance P
pH 8.2, 37°C, recombinant wild-type enzyme
40
Tyr-Pro-Leu-Gly-NH2
-
-
58
Tyr-Pro-Phe-NH2
-
-
32
Tyr-Pro-Phe-Pro-Gly
-
-
26
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
-
-
12 - 150
YPWTQ
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0603 - 0.269
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
0.19 - 2.1
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
0.0282 - 0.0789
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
0.016 - 0.12
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
0.027 - 0.0307
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
0.0198 - 0.037
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
0.014 - 0.032
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
0.00126 - 0.057
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
0.0026 - 0.024
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
0.014 - 0.11
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
0.0043 - 0.0229
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
0.158 - 0.854
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
L-Ala-L-Pro-L-Ala
Escherichia coli;
-
wild-type, pH 8.1, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.016
-
humans with previous angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
0.022 - 0.023
-
humans without angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
0.0375
-
recombinant wild-type enzyme, substrate bradykinin
0.17
-
mutant R404A, pH 7.5, 37°C
0.95
-
mutant R404A, presence of guanidine, pH 7.5, 37°C
3534
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
substrate L-Met-L-Pro
6.5
-
hydrolysis of Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
6.5 - 7
substrate Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
6.8 - 7.5
-
hydrolysis of Arg-Pro-Pro
6.9
-
native protein
7
-
hydrolysis of Arg-Pro-Pro
7 - 8
-
with substrate bradykinin
7.6
with substrate substance P
7.6 - 8
-
hydrolysis of Arg-Pro-Pro, Ala-Pro or Tyr-Pro-Leu-Gly-NH2
8 - 8.2
-
-
8.2
recombinant enzyme expressed in Escherichia coli
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
about 40% of maximal activity at pH 6.5-10
7.9 - 9.5
-
about 30% of maximal activity at pH 7.9 and at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
recombinant protein
41
-
enzyme form APP-II
46 - 49
-
-
55
-
enzyme form APP-I
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
less than 10% of maximum activity
50
less than 10% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expression of GFP-fusion protein
Manually annotated by BRENDA team
-
low activity in patients with angio-oedema
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
plasma
-
Manually annotated by BRENDA team
-
membrane-bound
-
Manually annotated by BRENDA team
-
mutant form with translational stop codon at position 658
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Caenorhabditis elegans;
Escherichia coli (strain K12);
Homo sapiens;
Q9WXP9
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39714
x * 39714, calculated
41600
-
gel filtration
50000
-
4 * 50000, SDS-PAGE
55000
-
4 * 55000, SDS-PAGE
60000
-
SDS-PAGE
68000
-
x * 71000, recombinant His-tagged fusion protein, SDS-PAGE, x * 68000, W03G9.4 protein, SDS-PAGE
70000
-
2 * 70000, X-ray crystallography
73000
-
SDS-PAGE, mature form
81500
-
x * 81500 + x * 89000, SDS-PAGE
89000
-
x * 81500 + x * 89000, SDS-PAGE
95000
-
x * 95000, reducing conditions, SDS-PAGE
105000
x * 105000, recombinant GST-fusion protein, SDS-PAGE
125000
-
SDS-PAGE
140000
143000
-
with 0.14 M NaCl, gel filtration
157000
-
gel filtration
200000
-
gel filtration
205000
-
calculation from sedimentation and diffusion data
208000
-
gel giltration
210000
-
enzyme form APP-II, gel filtration
217000
-
gel filtration
218000
-
without NaCl, gel filtration
220000
230000
-
equilibrium sedimentation
240000
-
native PAGE
280000
-
gel filtration
350000
-
enzyme form APP-I, gel filtration
360000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 71000, recombinant enzyme, SDS-PAGE
hexamer
-
arranged in 2 types of tetramers, one tetramer comprises 4 crystallographically independent subunits, while the other tetramer comprises 2 pairs of subunits related by a crystallographic 2fold axis
homodimer
monomer
-
1 * 40000, SDS-PAGE
tetramer
additional information
interaction of the subunits can not be disrupted by 2-mercaptoethanol, 1 M NaCl, 1% Triton X-100, and 4 mM CHAPS
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
8 mg/ml purified recombinant enzyme in Tris, pH 8.5, hanging drop vapour diffusion method, 0.003 ml mixed with 0.002 ml reservoir solution containing 25% PEG 4000, 0.1 M Tris-HCl, pH 8.0, 0.2 M sodium acetate, and 1 mM MnCl2, 1 month at 4°C, cryoprotectant is 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
in complex with inhibitor apstatin
-
Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu
-
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group
-
mutants H243A, D260A, D271A, H350A, H354A, H361A, E383A
-
hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5)
-
XPD43 is crystallized to 1.83 A resolution using the microbatch-under-oil technique
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
-
polyethylene glycol 20000 improves stability in the pH-range 4.5-7.0
36054
5 - 7.5
-
high stability at 37°C
709048
5 - 9
-
-
684020
5.5
-
human cytosolic APP1 is unstable and forms a high molecular weight aggregate at acidic pH
709048
7 - 10.5
-
optimal stability
36054
8 - 11
-
37°C, 2 h, maximal stability
36056
8.5 - 10
-
at 37°C, 2 h, most stable at
36054
10
-
stable, enzyme form APP-I
36039
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
-
reasonable stability at 0°C, 20°C and 37°C over 15 days
5 - 40
-
stable for 60 min
32
-
stable up to
37
-
pH 7.8, graduall loss of activity
45
-
pH 7.8, rapid denaturation above
50 - 60
-
stable
50
-
enzyme retains 50% of activity after 30 min of incubation
55
-
pH 6.8, 30 min, 0.1 M potassium phosphate buffer, stable up to
70 - 75
-
pH 6.8, 30 min, complete loss of activity
75
-
pH 6.8, 30 min, complete loss of activity
80
half-life above 100 min