Information on EC 3.4.11.24 - aminopeptidase S

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

EC NUMBER
COMMENTARY hide
3.4.11.24
-
RECOMMENDED NAME
GeneOntology No.
aminopeptidase S
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
CAS REGISTRY NUMBER
COMMENTARY hide
124404-20-2
-
9031-94-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NCTC8325-4
-
-
Manually annotated by BRENDA team
strain NCTC8325-4
-
-
Manually annotated by BRENDA team
strain K-1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phenylphosphonate + H2O
4-nitrophenol + phenylphosphonate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-L-leucine + H2O
4-nitrophenol + L-leucine
show the reaction diagram
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-OBzl + benzyl alcohol
show the reaction diagram
bis(4-nitrophenyl) phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
bis(4-nitrophenyl) phosphate + H2O
?
show the reaction diagram
-
assay at pH 8.0, 30°C
-
-
?
bis(p-nitrophenyl)phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
D-Arg-OMe + L-Pro-OBzl
c(L-Pro-D-Arg) + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
D-Arg-OMe + L-Pro-OBzl
L-Pro-D-Arg-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Leu-OBzl + D-Leu-OBzl
D-Leu-D-Leu-OBzl + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Leu-OMe + D-Leu-OMe
D-Leu-D-Leu-OMe + methanol
show the reaction diagram
-
-
-
-
?
D-Leu-OMe + D-Pro-OBzl
D-Pro-D-Leu-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Leu-OMe + L-Pro-OBzl
L-Pro-D-Leu-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Phe-OMe + D-Pro-OBzl
D-Pro-D-Phe-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Phe-OMe + L-Pro-OBzl
L-Pro-D-Phe-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Trp-OMe + D-Pro-OBzl
D-Pro-D-Trp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Trp-OMe + L-Pro-OBzl
L-Pro-D-Trp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Tyr-OMe + D-Pro-OBzl
D-Pro-D-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Tyr-OMe + L-Pro-OBzl
L-Pro-D-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Val-OBzl + D-Val-OBzl
D-Val-D-Val-OBzl + benzyl alcohol
show the reaction diagram
-
-
-
-
?
D-Val-OMe + L-Pro-OBzl
L-Pro-D-Val-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
show the reaction diagram
-
5.4% of the activity with Lys-4-nitroanilide
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Gly-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
human hemoglobin alpha-chain + H2O
?
show the reaction diagram
-
hydrolysis of the first few residues to proline at the 4th position
-
?
human hemoglobin beta-chain + H2O
?
show the reaction diagram
-
hydrolysis of the first few residues to proline at the 5th position
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
L-Ala-OMe + L-Pro-OBzl
L-Pro-L-Ala-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-alanine-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
L-alanine-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
show the reaction diagram
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
L-Arg-OMe + beta-Ala-OBzl
beta-Ala-L-Arg-OMe + benzyl alcohol
show the reaction diagram
L-Arg-OMe + L-Pro-OBzl
c(L-Pro-L-Arg) + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-Arg-OMe + L-Pro-OBzl
L-Pro-L-Arg-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Asn-OMe + beta-Ala-OBzl
beta-Ala-L-Asn-OMe + benzyl alcohol
show the reaction diagram
L-Asp-OMe + L-Pro-OBzl
L-Pro-L-Asp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Glu-OMe + L-Pro-OBzl
L-Pro-L-Glu-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-His-OMe + beta-Ala-OBzl
beta-Ala-L-His-OMe + benzyl alcohol
show the reaction diagram
L-His-OMe + D-Pro-OBzl
c(D-Pro-L-His) + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-His-OMe + D-Pro-OBzl
D-Pro-L-His-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-His-OMe + L-Pro-OBzl
c(L-Pro-L-His) + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-His-OMe + L-Pro-OBzl
L-Pro-L-His-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Ile-OMe + beta-Ala-OBzl
beta-Ala-L-Ile-OMe + benzyl alcohol
show the reaction diagram
L-Ile-OMe + D-Pro-OBzl
D-Pro-L-Ile-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Ile-OMe + L-Pro-OBzl
L-Pro-L-Ile-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Leu-NH2 + H2O
L-Leu + NH3
show the reaction diagram
L-Leu-O-methyl ester + H2O
L-Leu + methanol
show the reaction diagram
L-Leu-OEt + beta-Ala-OBzl
beta-Ala-L-Leu-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Leu-OEt + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Leu-beta-Ala-OBzl + benzyl alcohol + ethanol
show the reaction diagram
-
-
-
-
?
L-Leu-OEt + D-Pro-OBzl
D-Pro-L-Leu-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Leu-OEt + L-Pro-OBzl
L-Pro-L-Leu-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
L-Lys-OMe + beta-Ala-OBzl
beta-Ala-L-Lys-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Lys-OMe + L-Pro-OBzl
L-Pro-L-Lys-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
-
good substrate
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
show the reaction diagram
L-Met-OMe + beta-Ala-OBzl
beta-Ala-L-Met-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Met-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Met-OMe + benzyl alcohol +
show the reaction diagram
-
-
-
-
?
L-Met-OMe + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Met-beta-Ala-OBzl + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-Met-OMe + D-Pro-OBzl
D-Pro-L-Met-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Met-OMe + L-Met-OMe + beta-Ala-OBzl
beta-Ala-L-Met-L-Met-OMe + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-Met-OMe + L-Pro-OBzl
L-Pro-L-Met-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
show the reaction diagram
-
very good substrate
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
show the reaction diagram
L-Phe-NH2 + H2O
L-Phe + NH3
show the reaction diagram
-
-
-
?
L-Phe-O-methyl ester + H2O
L-Phe + methanol
show the reaction diagram
-
-
-
?
L-Phe-OEt + beta-Ala-OBzl
beta-Ala-L-Phe-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Phe-OEt + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Phe-beta-Ala-OBzl + benzyl alcohol + ethanol
show the reaction diagram
-
-
-
-
?
L-Phe-OEt + D-Pro-OBzl
D-Pro-L-Phe-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Phe-OEt + L-Phe-OEt + beta-Ala-OBzl
beta-Ala-L-Phe-L-Phe-OMe + benzyl alcohol + ethanol
show the reaction diagram
-
-
-
-
?
L-Phe-OEt + L-Pro-OBzl
L-Pro-L-Phe-OEt + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-phenylalanine ethyl ester + L-phenylalanine + H2O
L-Phe-L-Phe + cyclo(L-phenylalanine-L-phenylalanine) + L-Phe-L-Phe ethyl ester
show the reaction diagram
L-phenylalanine-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
show the reaction diagram
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
show the reaction diagram
-
very good substrate
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
show the reaction diagram
very low activity
-
-
?
L-Pro-OMe + beta-Ala-OBzl
L-Pro-beta-Ala-OBzl + methanol
show the reaction diagram
-
-
-
-
?
L-Pro-OMe + beta-Ala-OBzl + beta-Ala-OBzl
L-Pro-(beta-Ala)2-OBzl + methanol + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-proline-4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
-
good substrate
-
?
L-proline-p-nitroanilide + H2O
L-Pro + 4-nitroaniline
show the reaction diagram
L-Ser-OMe + L-Pro-OBzl
L-Pro-L-Ser-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Thr-OMe + beta-Ala-OBzl
beta-Ala-L-Thr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Thr-OMe + L-Pro-OBzl
L-Pro-L-Thr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Thr-OMe + L-Thr-OMe
(L-Thr)2-OMe + methanol
show the reaction diagram
-
-
-
-
?
L-Thr-OMe + L-Thr-OMe
L-Thr-L-Thr-OMe + methanol
show the reaction diagram
-
-
-
-
?
L-Trp-OMe + beta-Ala-OBzl
beta-Ala-L-Trp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Trp-OMe + D-Pro-OBzl
D-Pro-L-Trp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Trp-OMe + L-Pro-OBzl
L-Pro-L-Trp-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Tyr-OMe + beta-Ala-OBzl
beta-Ala-L-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Tyr-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Tyr-OMe + D-Pro-OBzl
D-Pro-L-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Tyr-OMe + L-Pro-OBzl
L-Pro-L-Tyr-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Tyr-OMe + L-Tyr-OMe + beta-Ala-OBzl
beta-Ala-L-Tyr-L-Tyr-OMe + benzyl alcohol + methanol
show the reaction diagram
-
-
-
-
?
L-Val-OBzl + L-Val-OBzl
L-Val-L-Val-OBzl + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Val-OMe + beta-Ala-OBzl
beta-Ala-L-Val-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Val-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Val-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Val-OMe + D-Pro-OBzl
D-Pro-L-Val-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-Val-OMe + L-Pro-OBzl
L-Pro-L-Val-OMe + benzyl alcohol
show the reaction diagram
-
-
-
-
?
L-valine-4-nitroanilide + H2O
L-valine + 4-nitroaniline
show the reaction diagram
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
Leu-Gly-Gly + H2O
Leu + Gly-Gly
show the reaction diagram
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
peptide + H2O
?
show the reaction diagram
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
show the reaction diagram
-
11.7% of the activity with Lys-4-nitroanilide
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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
peptide + H2O
?
show the reaction diagram
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
dinuclear metal-enzyme derivative, structure
Ni2+
-
dinuclear metal-enzyme derivative, structure
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
4-iodo-L-phenylalanine
-
weak inhibition, binds at the active site via the two zinc ions displacing the metal ions, binding structure analysis
amastatin
antipain
-
0.01 mg/ml, 93% inhibition
bestatin
bis(p-nitrophenyl)phosphate
-
-
Chloroquine
-
5 mM, 79% inhibition
CrCl2
-
1 mM, 83% inhibition in presence of 1 mM CoCl2
CuCl2
-
1 mM, 96% inhibition in presence of 1 mM CoCl2
D-phenylalanine
-
-
diisopropylphosphofluoridate
-
pretreatment, complete inhibition
EGTA
-
complete inhibition, activity can be completely restored by addition of 1 mM CaCl2
fluoride
free amino acids
-
competitive inhibition, highest inhibition by L-histidine
-
HgCl2
-
5 mM, 98% inhibition in presence of 1 mM CoCl2
L-arginine
-
-
L-aspartate
-
-
L-leucine
L-leucine chloromethyl ketone
-
-
L-methionine
L-phenylalanine
L-phenylalanine chloromethyl ketone
-
-
L-tryptophan
-
weak inhibition, binds at the active site via the two zinc ions displacing the metal ions, binding structure analysis
Leu-hydroxamate
-
1 mM, 73% inhibition
leucine
leupeptin
-
0.01 mg/ml, 51% inhibition
Lys-hydroxamate
methionine
weak inhibitor, binding structure, overview
MgSO4
-
1 mM, 24% inhibition in presence of 1 mM CoCl2
MnSO4
-
1 mM, 26% inhibition in presence of 1 mM CoCl2
NiSO4
-
1 mM, 40% inhibition in presence of 1 mM CoCl2
nitrilotriacetic acid
-
5 mM, 95% inhibition
p-hydroxymercuribenzoate
-
5 mM, 90% inhibition
phenylalanine
weak inhibitor, binding structure, overview
phenylmethylsulfonyl fluoride
-
1 mM, 95% inhibition
phosphate
PMSF
-
1 mM, complete inhibition
tosyl-lysine chloromethyl ketone
ZnCl2
-
1 mM, 70% inhibition in presence of 1 mM CoCl2
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 14.9
4-nitrophenyl phenylphosphonate
7.8
Ala-4-nitroanilide
-
pH 8.0, 30°C
0.16
Arg-4-nitroanilide
3.8 - 12.8
bis(4-nitrophenyl) phosphate
3.4
bis(p-nitrophenyl)phosphate
-
pH 8.0, 30°C
1.4
Gly-4-nitroanilide
-
pH 8.0, 30°C
4.08
L-Ala-4-nitroanilide
-
pH 8.0, 30°C
3.84 - 4.81
L-alanine-4-nitroanilide
0.25 - 4.07
L-Leu-4-nitroanilide
8.31 - 42.7
L-Leu-NH2
15.8 - 16.1
L-Leu-O-methyl ester
0.55 - 2.97
L-leucine-4-nitroanilide
0.34 - 1.85
L-Phe-4-nitroanilide
6.98 - 24.2
L-Phe-NH2
6.9 - 12.8
L-Phe-O-methyl ester
0.53
L-Val-4-nitroanilide
-
pH 8.0, 30°C
0.79 - 2.15
L-valine-4-nitroanilide
0.00229 - 3.31
Leu-4-nitroanilide
0.16 - 5
Lys-4-nitroanilide
0.58
Met-4-nitroanilide
-
pH 8.0, 30°C
0.18
Val-4-nitroanilide
-
pH 8.0, 30°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0033 - 0.022
4-nitrophenyl phenylphosphonate
4.9
Ala-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
0.0064 - 0.74
bis(4-nitrophenyl) phosphate
0.42
bis(p-nitrophenyl)phosphate
Streptomyces griseus
-
pH 8.0, 30°C
1.1
Gly-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
1.71 - 2.94
L-Ala-4-nitroanilide
0.47 - 2.94
L-alanine-4-nitroanilide
0.49 - 391
L-Leu-4-nitroanilide
31.7 - 155
L-Leu-NH2
64.2 - 169
L-Leu-O-methyl ester
1.31 - 153
L-leucine-4-nitroanilide
17.6 - 229
L-Phe-4-nitroanilide
10.7 - 115
L-Phe-NH2
0.64 - 224
L-Phe-O-methyl ester
0.191
L-Val-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
0.13 - 0.26
L-valine-4-nitroanilide
0.0433 - 657
Leu-4-nitroanilide
2.8
Lys-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
43.3
Met-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
0.28
Val-4-nitroanilide
Streptomyces griseus
-
pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.1
bis(4-nitrophenyl) phosphate
1697
7.89 - 441
Leu-4-nitroanilide
1622
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000011 - 0.00079
amastatin
0.0026 - 0.065
bestatin
2.31
bis(p-nitrophenyl)phosphate
-
pH 5.0, 30°C
36.6
D-phenylalanine
-
pH 8.0, 30°C, in presence of Ca2+
1.1 - 108
fluoride
12.4 - 100
L-leucine
0.0005 - 0.0055
L-leucine chloromethyl ketone
8.7 - 9.1
L-methionine
12.7
L-phenylalanine
-
pH 8.0, 30°C, in presence of Ca2+
0.0019 - 0.0053
L-phenylalanine chloromethyl ketone
10.3
leucine
-
pH 8.0, 30°C
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0016
-
Ni2+-enzyme, substrate 4-nitrophenyl phenylphosphonate; Ni2+-enzyme, substrate bis(4-nitrophenyl) phosphate
0.0017
-
Zn2+-enzyme, substrate 4-nitrophenyl phenylphosphonate
0.0033
-
Mn2+-enzyme, substrate 4-nitrophenyl phenylphosphonate
0.0048
-
Co2+-enzyme, substrate 4-nitrophenyl phenylphosphonate
0.0078
-
Cd2+-enzyme, substrate bis(4-nitrophenyl) phosphate
0.0097
-
Cd2+-enzyme, substrate 4-nitrophenyl phenylphosphonate
0.02
-
substrate beta-Ala-4-nitroanilide
0.031
-
Mn2+-enzyme, substrate bis(4-nitrophenyl) phosphate
0.136
-
Co2+-enzyme, substrate bis(4-nitrophenyl) phosphate
0.158
-
Zn2+-enzyme, substrate bis(4-nitrophenyl) phosphate
5.13
-
substrate L-Pro-4-nitroanilide
38.4
-
substrate L-Phe-4-nitroanilide
306
-
purified API
317
-
purified APII
461
-
purified API in presence of 1 mM CaCl2
625.1
-
purified enzyme; purified recombinant enzyme
830
-
purified recombinant wild-type enzyme
1244
-
substrate L-Ala-4-nitroanilide
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
bell-shaped pH-profile
6 - 8
-
pH 6: about 55% of maximal activity, pH 11: about 35% of maximal activity
6.3 - 11.5
-
at 0.05 mM Ca2+
6.3 - 9.5
-
at 50 mM Ca2+
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
assay at, substrate 4-nitrophenyl phenylphosphonate
65
-
in absence of Ca2+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 75
-
in absence of Ca2+
30 - 90
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
-
isoelectric focusing; recombinant enzyme, isoelectric focusing and amino acid sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
protease type XIV i.e. pronase E, a protease mixture form Streptomyces griseus
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
API, gel filtration
22500
-
APII, gel filtration
26800
-
recombinant enzyme, gel filtration
29000 - 29730
-
native PAGE and mass spectrometry
29720
amino acid sequence determination
29723
1 * 29723, amino acid sequence determination
30800
-
1 * 30800, recombinant enzyme, SDS-PAGE
33000
-
1 * 33000, API, SDS-PAGE, 1 * 34000, APII, SDS-PAGE
34000
-
1 * 33000, API, SDS-PAGE, 1 * 34000, APII, SDS-PAGE
290000
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M HEPES/NaOH, pH 7.6, 2.0 M ammonium sulfate, and 2% PEG 400, 4 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
hanging drop vapour diffusion method, 18-25 mg/ml purified enzyme in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM CaCl2, plus an equal volume of sodium acetate buffer at pH 5.0 to 6.0, 16-20% w/v polyethylene glycol 4000, suspended over 1 ml reservoir solution of sodium acetate, pH 5.0-6.0, 16-20% PEG 4000, 3-4 weeks, X-ray diffraction structure determination at 47.2 to 1.9 A resolution and analysis
-
protein with or without bound Zn2+ or replaced with Hg2+, hanging drop vapour diffusion method, 20 mg/ml purified enzyme in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM CaCl2, plus an equal volume of sodium acetate buffer at pH 5.0 to 6.0, 16-20% w/v polyethylene glycol 4000, suspended over 1 ml reservoir solution of sodium acetate, pH 5.0-6.0, 16-20% PEG 4000, 4-5 weeks to full size crystals, X-ray diffraction structure determination at 2.1 to 1.75 A resolution and analysis
-
purified enzyme complexed with L-methionine, L-phenylalanine, or L-leucine, hanging-drop vapour diffusion method, protein solution: 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, 100 mM L-methionine or 200 mM L-leucine, plus equal volume of precipitant solution: 24% w/v PEG 4000, 0.1 M ammonium sulfate, equilibrated against 1 ml of reservoir precipitant solution, 3-4 days, cyrstals of enzyme complexed with L-Phe were precipitated with 0.1 M acetate buffer, pH 5.5 instead in the same procedure within 8-10 weeks, X-ray complex structure determination at 1.6 A resolution and analysis
-
purified enzyme complexed with methionine, hanging-drop vapour diffusion method, protein solution: 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, 0.1 M methionine, plus equal volume of precipitant solution: 24% w/v PEG 4000, 0.1 M ammonium sulfate, equilibrated against 1 ml reservoir of the precipitant solution, 3-4 days, X-ray diffraction structure determination at 1.53 A high resolution and analysis; purified native enzyme in complex with product analogous weak inhibiting amino acids phenylalanine, leucine, and methionine, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM L-methionine or 200 mM L-leucine, the precipitant solution contains 24% w/v PEG 4000 and 0.1 M ammonium sulfate, equilibration against 1 ml reservoir solution, microseeding, 3-4 days, with phenylalanine a protein solution containing 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM Phe is mixed with a reservoir solution containing 18% w/v PEG 4000, and 0.1 M acetate buffer, pH 5.5, microseeding, 3-4 days, X-ray diffraction structure determination and analysis at 1.8 A, 1.7 A, and 1.53 A resolution, respectively, structure modelling
purified enzyme in complex with tryptophan or 4-iodo-L-phenylalanine, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM tryptophan or 2 mM 4-iodo-L-phenylalanine, equal volumes of protein and reservoir solution are mixed, the latter containing 18% w/v PEG 4000 and 0.1 M sodium acetate, pH 5.5, equilibration against 1 ml reservoir solution for 1 day, microseeding, 3-4 days, X-ray diffraction structure determination and analysis at 1.3 A resolution
-
structure determination and analysis
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 60
30 min, recombinant enzyme, stable
50
-
20 min, stable
75
-
rate constant for inactivation Kin is 0.00028/s in absence of Ca2+, and 0.000025/s in presence of Ca2+
78
30 min, recombinant enzyme, 50% loss of activity
80
-
30 min, 50% loss of activity, in presence of Ca2+
95
-
enzyme inactivation after 30 min at 95°C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, liquid and freeze-dried, stable for at least 8 weeks, no loss of activity
-
4°C, 50% loss of activity after 4 days, 80% loss of activity after 8 days. Remains active for 2 months, when concentrated and kept in a suspension with 4 M ammonium sulfate in 20 mM MOPS/Tris, pH 7
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sephacel column
-
from commercial product
-
from commercial product, 2 peaks API and APII, endopeptidase is eliminated
-
from commercial product, purification of the acetylated enzyme derivatives by DEAE cellulose chromatography
-
native enzyme by ion exchange chromatography, ammonium sulfate fractionation, and gel filtration, recombinant enzyme from Escherichia coli strain BL21(DE3) culture supernatant by ion exchange chromatography
recombinant enzyme from Streptomyces lividans cells by diafiltration, hydrophobic interaction chromatography, and gel filtration to homogeneity; recombinant from Streptomyces lividans cell culture medium, high purity, 19% recovery
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, and gel filtration
-
recombinant soluble wild-type and mutant enzymes 28fold from Escherichia coli strain BL21(DE3) by heat treatment for 20 min at 50°C and anion exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
to homogeneity from strain K-1 pronase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
-
DNA and amino acid sequence determination, subcloning and expression of the recombinant enzyme possessing a Asp70 and Asp184 residues in Escherichia coli strain BL21(DE3), the soluble enzyme is inducible by growth on 1 M sorbitol, optimization of the expression method
-
expression in Escherichia coli BL21
-
expression in Streptomyces lividans by insertional cloning and protoplast transformation, the expression system contains the constitutive Streptomyces fradiae aph promoter; gene SGAP, standard protoplast transformation and expression in Streptomyces lividans, excretion to the medium
-
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene Sgap, DNA and amino acid sequence determination and analysis, overexpression as secreted enzyme in Escherichia coli
-
gene Sgap, screening of 21 strains with strain NBRC12875 showing the highest activity
gene Ssap, genomic library screening, DNA and amino acid sequence determination and analysis, overexpression as secreted enzyme in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D3A/D262G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E131
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E131D
-
a general acid-base mutant, thermodynamic parameters for the reaction are similar to the wild-type enzyme, but the kcat of the mutant is 4fold reduced, while the activation energy is elevated compared to the wild-type enzyme
E196A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y246
-
site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
F221A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
F221G
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
F221S
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
the enzyme is clinically important as a model for undestanding the structure and mechanism of action of other metallopeptidases
biotechnology
Show AA Sequence (323 entries)
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