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
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
strain TH-4
SwissProt
Manually annotated by BRENDA team
isoform APP II
-
-
Manually annotated by BRENDA team
strain NA1, expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
strain NA1, 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
-
-
-
?
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-L-Ala + H2O
L-Phe + L-Pro-L-Ala
show the reaction diagram
L-Phe-L-Pro-L-Gly + H2O
L-Phe + L-Pro-Gly
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
0.14
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
-
mutant H350, pH 8.1, 37C
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, 37C
0.51 - 0.86
FPHFD
0.4697
Gly-Pro-4-nitroanilide
-
pH 8, 37C
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, 37C
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, 80C
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, 37C, 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
Escherichia coli
-
-
20
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
Escherichia coli
-
-
7.3 - 95
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
73
Arg-Pro
Rattus norvegicus
-
-
49 - 230
Arg-Pro-Pro
125
Arg-Pro-Pro-benzylamide
Cavia porcellus
-
-
17
Arg-Pro-Pro-Gly
Rattus norvegicus
-
-
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
Rattus norvegicus
-
-
1.5 - 487
L-Ala-L-Pro-4-nitroanilide
0.77
L-Ala-L-Pro-L-Ala
Escherichia coli
-
wild-type, pH 8.1, 37C
7.7
L-Arg-L-Pro-L-Pro
Homo sapiens
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37C
541
L-Met-L-Pro
Thermococcus sp.
Q2QC92
pH 5.0, 80C
3.1
Substance P
Homo sapiens
Q9NQW7
pH 8.2, 37C, recombinant wild-type enzyme
40
Tyr-Pro-Leu-Gly-NH2
Rattus norvegicus
-
-
58
Tyr-Pro-Phe-NH2
Rattus norvegicus
-
-
32
Tyr-Pro-Phe-Pro-Gly
Rattus norvegicus
-
-
26
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
Rattus norvegicus
-
-
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, 37C
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, 37C
0.95
-
mutant R404A, presence of guanidine, pH 7.5, 37C
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
-
enzyme form APP-I
8 - 8.2
-
-
8
-
6 mM imidazole buffer, Arg-Pro-Pro as substrate
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
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
native PAGE, SDS-PAGE
41600
-
gel filtration
60000
-
SDS-PAGE
73000
-
SDS-PAGE, mature form
90000
-
calculated from cDNA, native form
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 4C, 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 37C
709048
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
-
37C, 2 h, maximal stability
36056
8.5 - 10
-
at 37C, 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 0C, 20C and 37C over 15 days
5 - 40
-
stable for 60 min
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
90
half-life 90C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity after dialysis
-
loss of activity after lyophilization
-
polyethylene glycol 20000 improves stability in the pH-range 4.5-7.0
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C to 4C, 0.5 mg/ml recombinant GST-fusion enzyme, several weeks without significant loss of activity
-20C, pH 6.8, stable for at least 1 month
-
4C, bicine buffer, pH 7.8, 1 mM dithiothreitol, 1 mM MnCl2, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immunoaffinity purification
-
Ni-NTA affinity chromatography
-
Ni-NTA resin column chromatography and Hitrap Q HP affinity column chromatography
-
partial
recombinant enzyme from Escherichia coli
-
recombinant His-tagged enzyme from Ecscherichia coli
recombinant His-tagged enzyme from Escherichia coli
recombinant isozyme APP2 from Escherichia coli
using a Ni2+-charged His-Trap column
-
using His-tag affinity chromatography and desalting
-
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
cloning, DNA and amino acid sequence determination and analysis, and functional expression of open reading frame W03H9.4 from EST yk91g4 in Caenorhabditis elegans as GFP-fusion protein and as His-tagged enzyme in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli
DNA and amino acid sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme, and in COS-1 cells
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Pichia pastoris
-
expressed in Streptomyces lividans using the pTONA5a plasmid
expression as a fusion with the yellow fluorescent protein allele Citrine or with hemagglutinin tag in Plasmodium falciparum
expression in Escherichia coli
gene LeAPP1, DNA and amino acid sequence determination and analysis; gene LeAPP2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli in N-terminal fusion with GST, a mutant form lacking 11 amino acids from the N-terminus is not active
overexpression in Escherichia coli
-
recombinant expression in Escherichia coli as a His-tagged fusion protein
-
transient expression of wild-type and mutants in COS-1 cells
-