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Ala-Gly + H2O
Ala + Gly
-
-
-
ir
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Arg-Phe + H2O
Arg + Phe
-
-
-
ir
casein + H2O
?
-
assay at pH 8.0, 37°C
-
-
?
Cys-Gly + H2O
L-Cys + Gly
-
preferred substrate
-
-
?
DL-Ala-Gly-Gly + H2O
DL-Ala + Gly-Gly
-
-
-
ir
DL-Leu-Gly-DL-Phe + H2O
DL-Leu + Gly-DL-Phe
-
-
-
ir
DL-Leu-Gly-Gly + H2O
DL-Leu + Gly-Gly
-
-
-
ir
Glu-Phe + H2O
Glu + Phe
-
-
-
ir
glutathione + H2O
?
-
the enzyme is involved in turnover of glutathione
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gly
-
assay at pH 8.0, 37°C
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
Gly + 7-amino-4-methylcoumarin
-
very weak activity
-
-
?
Ile-amide + H2O
Ile + NH3
-
-
-
ir
Ile-Phe + H2O
Ile + Phe
-
-
-
ir
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
low activity
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Ala-L-Ala-L-Phe
-
assay at pH 8.0, 37°C
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
1% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
-
3% activity compared to L-Leu-p-nitroanilide
-
-
?
L-arginyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-arginine + 7-amino-4-carbamoylmethylcoumarin
L-Asp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Asp
-
assay at pH 8.0, 37°C
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
L-Cys-4-nitroanilide + H2O
L-Cys + 4-nitroaniline
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
-
-
?
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-cysteine + 7-amino-4-carbamoylmethylcoumarin
L-cystinyl-p-nitroanilide + H2O
L-cystine + p-nitroaniline
-
10% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gln
-
assay at pH 8.0, 37°C
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
very weak activity
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
L-Leu-Gly-Gly + H2O
L-Leu + Gly-Gly
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine anilide + H2O
L-leucine + aniline
-
-
-
?
L-leucine ethyl ester + H2O
L-leucine + ethanol
-
-
-
?
L-leucine-4-anisidide + H2O
L-leucine + anisidine
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-leucyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-leucine + 7-amino-4-carbamoylmethylcoumarin
L-leucyl-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucyl-L-leucyl-L-leucine + H2O
L-leucine + L-leucyl-L-leucine
-
-
-
?
L-Lys-4-nitroanilide + H2O
4-nitroaniline + L-Lys
-
assay at pH 8.0, 37°C
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-p-nitroanilide + H2O
L-Lys + p-nitroaniline
-
24% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Met
-
assay at pH 8.0, 37°C
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
L-methionyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-methionine + 7-amino-4-carbamoylmethylcoumarin
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-p-nitroanilide + H2O
L-Phe + p-nitroaniline
-
23% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Pro
-
assay at pH 8.0, 37°C
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Thr
-
assay at pH 8.0, 37°C
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
L-Thr + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Trp
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Tyr
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
low activity
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
-
very weak activity
-
-
?
L-Val-L-Phe + H2O
L-Val + L-Phe
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-amide + H2O
Leu + NH3
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
Leu-Gly + H2O
Leu + Gly
-
-
-
ir
Leu-methyl ester + H2O
Leu + methanol
-
-
-
ir
leucine-4-nitroaniline + H2O
?
-
enzyme also shows activity towards Arg-4-nitroaniline, Lys-4-nitroaniline and Met-4-nitroaniline
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Lys-Gly + H2O
Lys + Gly
-
-
-
ir
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
Met-amide + H2O
Met + NH3
-
-
-
ir
Met-beta-naphthylamide + H2O
Met + beta-naphthylamine
-
-
-
ir
Met-Leu-4-nitroanilide + H2O
Met-Leu + 4-nitroaniline
-
-
-
-
?
Met-Leu-7-amido-4-methylcoumarin + H2O
Met-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
Met-Phe + H2O
Met + Phe
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
norvalinamide + H2O
norvaline + NH3
-
-
-
-
?
oxidized insulin B chain + H2O
?
-
assay at pH 8.0, 37°C
-
-
?
peptides + H2O
N-terminal amino acid + peptide(n-1)
-
-
-
?
Phe-amide + H2O
Phe + NH3
-
-
-
ir
Phe-Asp-Ser-Ala-Val + H2O
Phe + Asp-Ser-Ala-Val
-
-
-
ir
Phe-beta-naphthylamide + H2O
Phe + beta-naphthylamine
Phe-Gly + H2O
Phe + Gly
-
-
-
ir
Phe-methyl ester + H2O
Phe + methanol
-
-
-
ir
Phe-Phe + H2O
Phe + Phe
-
-
-
ir
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
-
-
-
ir
Pro-Phe-Pro + H2O
Pro + Phe-Pro
-
-
-
ir
recombinant human methionine-interferon alpha-2b + H2O
L-methionine + recombinant human interferon alpha-2b
-
-
-
?
thionoleucine-4-anisidide + H2O
thionoleucine + anisidine
-
-
-
?
thionoleucine-S-anilide + H2O
thionoleucine + aniline
-
-
-
?
Thr-beta-naphthylamide + H2O
Thr + beta-naphthylamine
-
3.3% of rate of hydrolysis of Leu-beta-naphthylamide
-
ir
Tyr-Gly + H2O
Tyr + Gly
-
-
-
ir
Val-amide + H2O
Val + NH3
-
-
-
ir
Val-beta-naphthylamide + H2O
Val + beta-naphthylamine
-
-
-
ir
Val-Gly + H2O
Val + Gly
-
-
-
ir
additional information
?
-
albomycin + H2O
?
-
-
-
-
?
albomycin + H2O
?
-
PepA activates albomycin
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
74.5% activity compared to Leu-4-nitroanilide
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
74.5% activity compared to Leu-4-nitroanilide
-
-
?
Cys-Gly + H2O
Cys + Gly
-
-
-
-
?
Cys-Gly + H2O
Cys + Gly
-
glutathione-derived substrate, PepA is involved in the cysteine salvage pathway
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
best substrate
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-arginyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-arginine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-arginyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-arginine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-arginyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-arginine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
very weak activity
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Cys-4-nitroanilide + H2O
L-Cys + 4-nitroaniline
-
-
-
-
?
L-Cys-4-nitroanilide + H2O
L-Cys + 4-nitroaniline
-
-
-
-
?
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-cysteine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-cysteine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-cysteine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferably with Mn2+
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferred substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferred substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
assay at pH 8.0, 37°C
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-Gly-Gly + H2O
L-Leu + Gly-Gly
-
-
-
-
?
L-Leu-Gly-Gly + H2O
L-Leu + Gly-Gly
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
100% activity
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
enzyme in solution and immobilized on synthetic Mg2+ and Al2+ ion-containing layered double hydroxide particles
-
-
?
L-leucyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-leucine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-leucyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-leucine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-leucyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-leucine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
?
L-methionyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-methionine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-methionyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-methionine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-methionyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-methionine + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
ir
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
ir
Leu-Ala + H2O
Leu + Ala
-
-
-
ir
Leu-Ala + H2O
Leu + Ala
-
-
-
ir
Leu-amide + H2O
Leu + NH3
-
-
-
ir
Leu-amide + H2O
Leu + NH3
-
-
-
ir
Leu-Arg + H2O
Leu + Arg
-
-
-
ir
Leu-Arg + H2O
Leu + Arg
-
-
-
ir
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
ir
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
ir
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
ir
Leu-Ile + H2O
Leu + Ile
-
-
-
ir
Leu-Ile + H2O
Leu + Ile
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
-
-
-
ir
Leu-Met + H2O
Leu + Met
-
-
-
ir
Leu-Met + H2O
Leu + Met
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
-
-
-
ir
Leu-Trp + H2O
Leu + Trp
-
-
-
ir
Leu-Trp + H2O
Leu + Trp
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Val + H2O
Leu + Val
-
-
-
ir
Leu-Val + H2O
Leu + Val
-
-
-
ir
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
20% activity compared to Leu-4-nitroanilide
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
20% activity compared to Leu-4-nitroanilide
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
8.2% activity compared to Leu-4-nitroanilide
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
8.2% activity compared to Leu-4-nitroanilide
-
-
?
norleucinamide + H2O
norleucine + NH3
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
-
-
-
ir
Peptides + H2O
?
-
-
81170, 81171, 81172, 81173, 81174, 81175, 81176, 81177, 81178, 81179, 81180, 81181, 81182, 81183, 81184, 81185, 81186, 81187, 81189, 81190 -
-
?
Phe-beta-naphthylamide + H2O
Phe + beta-naphthylamine
-
-
-
ir
Phe-beta-naphthylamide + H2O
Phe + beta-naphthylamine
-
18% of rate of hydrolysis of Leu-beta-naphthylamide
-
ir
additional information
?
-
-
effect of adjacent amino acids on specificity
-
-
?
additional information
?
-
substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
-
-
?
additional information
?
-
-
the enzyme prefers large and hydrophobic amino acids in peptide and protein substrates
-
-
?
additional information
?
-
no activity is determined by using His-4-nitroanilide, Ile-4-nitroanilide, Ala-4-nitroanilide, Phe-4-nitroanilide, and Val-4-nitroanilide as substrates
-
-
?
additional information
?
-
sequences and masses of peptides of different length, which are generated by the recombinant BsuAP aminopeptidase from the peptide substrate, GFP B, overview. The GFP B peptide is 14 residues long and the enzyme progressively truncates the peptide by one amino acid residue from its N-terminus. BsuAP has N-terminal de-blocking capability
-
-
?
additional information
?
-
sequences and masses of peptides of different length, which are generated by the recombinant BsuAP aminopeptidase from the peptide substrate, GFP B, overview. The GFP B peptide is 14 residues long and the enzyme progressively truncates the peptide by one amino acid residue from its N-terminus. BsuAP has N-terminal de-blocking capability
-
-
?
additional information
?
-
no activity is determined by using His-4-nitroanilide, Ile-4-nitroanilide, Ala-4-nitroanilide, Phe-4-nitroanilide, and Val-4-nitroanilide as substrates
-
-
?
additional information
?
-
the enzyme is probably involved in amino acid supply in the organism deficient in amino acid synthesis pathways, and/or in peptide and/or protein processing
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
biological functions overview, the enzyme functions in the final steps of protein turnover during starvation and in degradation of abnormal proteins, the enzyme binds DNA and is active in both transcriptional regulation and site-specific recombination, and is involved in regulation of the carAB operon
-
-
?
additional information
?
-
-
PepA acts as DNA-binding protein in Xer site-specific DNA recombination serving as accessory protein
-
-
?
additional information
?
-
-
broad-range specificity, the enzyme binds DNA and is active in both transcriptional regulation and site-specific recombination, the enzyme prefers tripeptide substrates with N-terminal leucyl- or methionyl-residues, dipeptides or C3-C6 peptides are also cleaved but more slowly, no activity with albomycin
-
-
?
additional information
?
-
-
PepA binds DNA probably along the large groove that runs from the lower trimer face across the twofold molecular axis to the upper trimer face
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position
-
-
?
additional information
?
-
substrate specificity of HpM17AP, overview
-
-
?
additional information
?
-
-
substrate specificity of HpM17AP, overview
-
-
?
additional information
?
-
substrate specificity of HpM17AP, overview
-
-
?
additional information
?
-
substrate specificity of HpM17AP, overview
-
-
?
additional information
?
-
-
the enzyme is involved in transport and degradation of extracellular peptides, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
biological functions overview, the enzyme is involved in control of signal transduction leading to alginate expression
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position
-
-
?
additional information
?
-
-
LAP shows preference for leucine and methionine over other substrates
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
LAP shows broad substrate specificity and high enantioselectivity, structure-function relationship, active site metal composition and metal-dependent activity, overview
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
biological functions overview, the enzyme is involved in regulation of Xer sites-specific recombination
-
-
?
additional information
?
-
-
broad-range specificity, the enzyme prefers tripeptide substrates with N-terminal leucyl- or methionyl-residues, dipeptides or C3-C6 peptides are also cleaved but more slowly, no activity with peptides with proline at the second position
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position
-
-
?
additional information
?
-
-
no activity towards Asp-Gly, Glu-Cys-Gly, and L-Cys
-
-
?
additional information
?
-
-
difference in action towards oligopeptides and polypeptides, as compared to amides, may be due to ability of enzyme to bind larger substrates more effectively
-
-
?
additional information
?
-
-
also cleaved: gastrin peptide (carboxyterminal), various oligopeptides, Met-Lys-bradykinin, adrenocorticotropic hormone, glucagon, aminoethylated B-chain insulin, sperm whale myoglobin, ribunuclease, beta-lactoglobulin, egg white lysozyme, aminoethylated lysozyme
-
-
?
additional information
?
-
-
also cleaved: gastrin peptide (carboxyterminal), various oligopeptides, Met-Lys-bradykinin, adrenocorticotropic hormone, glucagon, aminoethylated B-chain insulin, sperm whale myoglobin, ribunuclease, beta-lactoglobulin, egg white lysozyme, aminoethylated lysozyme
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
investigation of the mode of action using a quantum mechanical/molecular mechanical approach
-
-
?
additional information
?
-
-
the enzyme prefers substrates with large and hydrophobic N-terminal amino acid residues
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position
-
-
?
additional information
?
-
recombinant enzyme rLAP is selective and specific to remove N-terminal groups from amino acids
-
-
?
additional information
?
-
-
LAP is an exopeptidase that catalyzes the hydrolysis of leucine residues from the N-terminus of a protein or peptide
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Na+
the sodium ion is coordinated by the main-chain carbonyl oxygen atoms of A461, G462, Y465 and three water molecules in an octahedral geometry
Ca2+
-
inhibits activity
Ca2+
-
weakly inhibits activity
Cd2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Cd2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Cd2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Cd2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
enhances activity
Co2+
activates to 228% activity at 0.1 mM
Co2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Co2+
-
CoCl2 at 1mM increases the specific activity 18fold
Co2+
-
reactivates the apoenzyme
Co2+
-
highly activating, about 5fold at 1-10 mM
Co2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Co2+
-
580% relative activity in the presence of 2.0 mM Co2+
Co2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Co2+
-
65% of activity of zinc enzyme
Co2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Co2+
-
spectroscopically distinct cobalt sites in heterodimetallic enzymes, implications for substrate binding
Co2+
2 Co2+ bound at the dinuclear active site, can be substituted by Zn2+, binding mode
Co2+
can substitute for Zn2+
Co2+
-
Co2+ can substitute for Cd2+ in the bimetallic enzyme
Co2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
can substitute for one or both Zn2+ ions
Co2+
-
Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Co2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Cu2+
-
weakly inhibits activity
Cu2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Cu2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Mg2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site
Mg2+
-
MgCl2 shows an optimal concentration at 10 mM that increases specific activity by 12fold
Mg2+
-
activates 2.9fold at 1 mM, 3.7fold at 10 mM
Mg2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Mg2+
-
258% relative activity in the presence of 2.0 mM Mg2+
Mn2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site
Mn2+
-
recombinant LAP activity is progressively activated by MnCl2 (0.001-10 mM) with an optimum at 1 mM, yielding a 43fold increase
Mn2+
-
highly activating, 5.6fold at 1-10 mM
Mn2+
at pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2. Mn2+ has a significant activation effect when bound to site 1 of ppLAP
Mn2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Mn2+
-
510% relative activity in the presence of 2.0 mM Mn2+
Mn2+
-
58% of activity of zinc enzyme
Ni2+
-
inhibits activity
Ni2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Ni2+
-
activates 3.5fold at 1 mM, 3.8fold at 10 mM
Ni2+
Mycobacterium tuberculosis LAP exhibits maximum activity in the presence of Ni2+, but it is active in the presence of a broad range of other metals
Ni2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Ni2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Zn2+
-
-
Zn2+
-
dinuclear zinc active center
Zn2+
zinc-metalloaminopeptidase, 2 Zn2+ per enzyme molecule
Zn2+
-
2 ions bound per enzyme molecule, binding to Glu354
Zn2+
-
metallopeptidase, dimetal site structure, overview
Zn2+
-
ZnCl2 modestly affects the enzymatic activity
Zn2+
two active-site positively charged zinc ions are coordinated by negatively charged side-chain oxygen atoms of three aspartate residues (D263, D281, D340) and one glutamate residue (E342), the side-chain nitrogen atom of K258 and two water molecules in a distorted octahedral coordination geometry
Zn2+
-
0.05 mM, required for activity
Zn2+
LAP is zinc-dependent. At pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2
Zn2+
-
bound zinc ion interacts directly with substrate during catalysis but not during substrate binding, contains 2 mol zinc per mol enzyme but only one site has to be occupied in order to faciliate catalysis
Zn2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than in the opposite sequence, which suggests two metal-binding sites with different functions
Zn2+
-
2 mol zinc per mol enzyme
Zn2+
-
no loss of zinc upon photoinactivation
Zn2+
-
zinc can be replaced by other metals, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of metal ions, sequence of addition effects activity
Zn2+
2 Zn2+ bound at the dinuclear active site, can be substituted by Co2+, binding mode
Zn2+
bound in the active site, binding structure, bridged bimetallic enzyme
Zn2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Zn2+
AAP is a metalloenzyme containing two Zn2+ per enzyme molecule
Zn2+
-
dinuclear Zn2+ metal center
Zn2+
dinuclear Zn2+ metal center, the binding of Zn2+ to the E151H mutant is much more weak than to the wild-type enzyme
Zn2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Zn2+
-
the enzyme is a two-zinc metallopeptidase, zinc-binding involved residues His97, Asp117, Glu152, Asp179, and His256
Zn2+
the enzyme is bridged bimetallic, the metal ions are involved in the reaction, overview
Zn2+
the metallopeptidase requires two divalent metal ions per enzyme molecule for full activity, binuclear metal center activation and reaction mechanism
Zn2+
-
zinc-dependent metallopeptidase, Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Zn2+
-
zinc-metallopeptidase, 2 ions per enzyme molecule
Zn2+
AAP is a binuclear zinc enzyme, Zn2+ is essential for its enzymatic activity
Zn2+
two zinc ions in close proximity have been identified to form the metal component of the active site
Zn2+
required, 2 Zn2+ per active site
additional information
-
API and APII are metallopeptidases
additional information
-
metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
-
no relevant stimulatory effect with NiCl2, FeSO4 and CuSO4
additional information
the enzyme is a metallopeptidase, most active with Mn2+, no activation by Zn2+
additional information
-
the enzyme is a metallopeptidase, most active with Mn2+, no activation by Zn2+
additional information
ppLAP requires the presence of divalent metal ions for its activity, in particular Zn2+ and/or Mn2+. At pH 5.2, the active site of ppLAP is highly disordered and metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267
additional information
-
metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
-
not stimulated by Zn2+ or Ca2+
additional information
-
metal ion interacts directly with the substrate atoms, as shown by multiple inhibitor studies
additional information
-
bimetallic enzyme, binding conformations, overview
additional information
detailed metal binding structure analysis, overview, the first metal ion in the dinuclear metal center is in a hexacoordinate/pentacoordinate equilibrium, while the second metal ion is six-coordinate
additional information
-
detailed metal binding structure and kinetic analysis with recombinant wild-type and mutant enzymes, overview
additional information
-
metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
-
metalloprotein active site, structure and mechanism overview
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1,2-Cyclohexanedione
-
Ki: 0.022-0.023 mM
1-Phenyl-2-thiourea
-
competitive
2,3-Butanedione
-
photochemical inactivation: effect only in the light, proportional to light intensity, modification of 5 Trp-, 3-4 Tyr-, 2 His- and 2Arg-residues, no photoinactivation in the absence of oxygen or in the presence of azide, protection also by Trp, Met, D-Met, L-2-thiol-His, 2-mercaptoethanol, Gly-Met, Ki: 5.1-19.8 mM
2,3-Pentanedione
-
photochemical inactivation: effect only in UV-light
2-amino-1,4-dihydro-2-isoquinolin-3-one
-
-
2-aminocycloheptanone
-
-
2-hydroxy-1,4-dihydro-2H-isoquinolin-3-one
-
-
2-methylquinolin-8-ol
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-carbohydroxamic acid
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-ethanone
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-phosphonic acid
-
-
3-amino-3,4-dihydro-1H-naphtalen-2-one
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(2-phenylethyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(3-phenylpropyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(4-phenylbutyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(5-phenylpentyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-benzyloxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-methyloxime
-
-
3-methyl-1,2-cyclopentanedione
-
Ki: 0.48-1.19 mM
3-methyl-1-butanol
-
Ki: 0.98 mM
3-methylquinolin-8-ol
-
-
4-iodo-D-phenylalanine hydroxamate
5,7-dibromoquinolin-8-ol
-
-
5,7-dichloroquinolin-8-ol
-
-
5,7-diiodoquinolin-8-ol
-
-
5-(trifluoromethyl)quinolin-8-ol
-
-
5-bromo-2-methylquinolin-8-ol
-
-
5-bromo-8-hydroxy-2-methylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,2-dimethylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,N,2-trimethylquinoline-7-sulfonamide
-
-
5-chloro-2-methylquinolin-8-ol
-
-
5-chloro-7-iodoquinolin-8-ol
-
-
5-chloro-8-hydroxy-N,N-dimethylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxy-N-methylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxyquinoline-7-sulfonamide
-
-
5-chloroquinolin-8-ol
-
-
5-fluoroquinolin-8-ol
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-oxime
-
-
8-hydroxy-N,N-dimethylquinoline-5-sulfonamide
-
-
amastatin
-
reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1
Amino acid hydroxamates
-
-
Aprotinin
-
the recombinant enzyme shows 58.9% relative activity in the presence of 0.001 mM aprotinin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
benzyl alcohol
-
Ki: 2.6 mM
D-Leu-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Leu-hydroxamate
-
Ki: 2 nM, L-isomer bound 150 times less tightly
D-Val-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Val-hydroxamate
-
Ki: 5 nM
DL-Ala-hydroxamate
-
Ki: 0.0055 mM
DL-Phe-hydroxamate
-
Ki: 0.0008 mM
DL-Thr-hydroxamate
-
Ki: 0.002 mM
DL-Val-hydroxamate
-
Ki: 10 nM
E-64
-
the recombinant enzyme shows 43% relative activity in the presence of 0.005 mM E-64 on hydrolysis of L-Leu-7-amido-4-methylcoumarin
epibestatin
-
Ki: 0.07 mM
H2O2
-
the enzyme is sensitive against oxidative damage by H2O2
L-Ala-hydroxamate
-
Ki: 0.02 mM
L-cysteine
-
strongly inhibited by cysteine
L-leucine
competitive inhibition
L-leucine 4-nitroanilide
-
L-leucine phosphonic acid
L-leucinephosphonic acid
competitive, interacts with both metal ions in the dinuclear active site, inhibition mechanism
L-Phe-hydroxamate
-
Ki: 0.0088 mM
L-Thr-hydroxamate
-
Ki: 0.066 mM
L-trans-epoxysuccinylleucylamido-4-guanidino butane
E-64
L-Val-hydroxamate
-
Ki: 0.0022 mM
Leu-chloromethyl ketone
-
reversible, Ki: 670 nM; succinimido derivative, reversible, Ki: 0.17 mM
leucine phosphonic acid
competitive inhibition
leupeptin
-
the recombinant enzyme shows 32.7% relative activity in the presence of 0.01 mM leupeptin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
methylglyoxal
-
photochemical inactivation: effect only in UV-light, Ki: 1.8-2.0 mM
Mg2+
slight inhibition at 1 mM
N-alpha-tosyl-L-lysine chlormethyl ketone
-
the recombinant enzyme shows 28.9% relative activity in the presence of 0.005 mM N-alpha-tosyl-L-lysine chlormethyl ketone on hydrolysis of L-Leu-7-amido-4-methylcoumarin
N-mercapto-leucyl-4-nitroanilides
-
-
N-mercaptoacyl-leucyl-p-nitroaniline
-
synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition, Ki: 2.5-57 nM
-
Na2S
-
60% loss of activity at 10 mM
Ni2+
92.5% inhibition at 1 mM
p-iodo-D-Phe hydroxamate
-
structure of enzyme-inhibitor complex: Glu151 has crucial functional role
pepstatin A
-
the recombinant enzyme shows 26.1% relative activity in the presence of 1 mM pepstatin A on hydrolysis of L-Leu-7-amido-4-methylcoumarin
phenylmethylsulfonyl fluoride
t-butyloxycarbonyl-L-Leu
-
bromomethyl ketone derivative, utilized for purification procedure
Thioglycollate
-
60% loss of activity at 10 mM
thionoleucine-S-anilide
-
-
thionoleucine-S-anisidide
-
-
tosyl phenylalanyl chloromethyl ketone
TPCK
tosyl-lysylchloromethane
TLCK
Tris
buffer inhibition; chelated to active site Zn2+
1,10-phenanthroline
-
99% inhibition at 1 mM
1,10-phenanthroline
complete inhibition, reversible by Zn2+
1,10-phenanthroline
complete inhibition at 0.25 mM, reversible by Zn2+, not by other divalent cations, overview
1,10-phenanthroline
-
strong inhibition
1,10-phenanthroline
-
the recombinant enzyme shows 18.8% relative activity in the presence of 1 mM 1,10-phenanthroline on hydrolysis of L-Leu-7-amido-4-methylcoumarin
1,10-phenanthroline
86.5% inhibition
1-Butaneboronate
-
enhances zinc uptake by enzyme, Ki: 0.0027 mM
1-butaneboronic acid
binding mode
1-butaneboronic acid
-
binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
2-mercaptoethanol
strong inhibition
4-iodo-D-phenylalanine hydroxamate
binding mode
4-iodo-D-phenylalanine hydroxamate
-
-
bestatin
-
99% inhibition at 0.05 mM
bestatin
complete inhibition at 0.1 mM, not reversible by divalent cations
bestatin
-
strongly inhibited by bestatin, 20.5% relative activity in the presence of bestatin
bestatin
-
inhibits the enzyme activity and cell growth
bestatin
(2S)-2-[[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]amino]-4-methylpentanoic acid, inhibits HpM17AP and suppresses Helicobacter pylori growth, enzyme binding structure analysis from the crystal structures of HpM17AP and its complex with bestatin. The position of the D-phenylalanine moiety of the inhibitor with respect to the active-site metal ions, bicarbonate ion and with respect to other M17 aminopeptidases suggests that this residue binds to the S1 subsite of HpM17AP
bestatin
complete enzyme inhibition at 0.03 mM with substrate L-Leu-7-amido-4-methylcoumarin, in a murine model of tuberculosis, bestatin treatment reduces bacterial burden and lesion in the lungs of infected mice. Bestatin inhibits Mycobacterium tuberculosis growth in in vitro and ex vivo
bestatin
binding structure and comparison, overview
bestatin
-
reversible, slow, tight binding, transition state analog complex, Ki: 18 nM, stoichiometry of inhibition 1:1
Ca2+
68.4% inhibition at 1 mM
Ca2+
-
44% relative activity at 10 mM Ca2+
Ca2+
-
78% inhibition at 0.1 mM, 94% inhibition at 1 mM, 96% inhibition at 10 mM
Ca2+
-
22% residual activity in the presence of 2.0 mM Ca2+
Cu2+
-
-
Cu2+
slight inhibition at 1 mM
cysteine
-
strong inhibition
cysteine
-
60% loss of activity at 10 mM
dithiothreitol
-
54% inhibition at 5 mM
dithiothreitol
-
the recombinant enzyme shows 20.5% relative activity in the presence of 5 mM dithiothreitol on hydrolysis of L-Leu-7-amido-4-methylcoumarin
DTT
complete inhibition at 1 mM, 50°C, 1 h
DTT
complete inhibition at 20 mM
EDTA
-
10% inhibition at 1 mM
EDTA
complete inhibition at 1 mM, 50°C, 1 h, the activity can be restored by Co2+ and partially by Zn2+
EDTA
50% inhibition at 10 mM, reversible by divalent cations, best by Zn2+
EDTA
-
97% inhibition at 0.1 mM
EDTA
strong inhibition, inhibition is reversible by Mn2+
EDTA
-
2% residual activity in the presence of 0.2 mM EDTA
EDTA
-
complete inactivation, reversible by Zn2+, Co2+, Ni2+, or Cu2+
L-leucine phosphonic acid
binding mode
L-leucine phosphonic acid
-
transition state inhibitor, binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
L-leucinethiol
-
-
L-leucinethiol
-
i.e. LeuSH, kinetic and spectroscopic characterization of the slow, tight-binding peptide inhibitor-enzyme complex, inhibition mechanism
Leu-bromomethyl ketone
-
succinamic acid derivative, Ki: 0.0069 mM
Leu-bromomethyl ketone
-
reversible, Ki: 200 nM
Leu-methyl ketone
-
derivatives, Ki: 0.14 - 0.17 mM
Leu-methyl ketone
-
reversible, Ki: 0.018 mM
Leu-methyl ketone
-
derivatives
Mn2+
-
-
Mn2+
slight inhibition at 1 mM
n-valeramide
-
no effect on enzyme zinc uptake, Ki: 0.0006 mM
n-valeramide
enzyme-inhibitor complex represents snapshot of proteolytic reaction between Michaelis-Menten and transition state
Phenylglyoxal
-
-
Phenylglyoxal
-
Ki: 0.002-0.0023 mM
phenylmethylsulfonyl fluoride
-
the recombinant enzyme shows 24.5% relative activity in the presence of 1 mM phenylmethylsulfonyl fluoride on hydrolysis of L-Leu-7-amido-4-methylcoumarin
phenylmethylsulfonyl fluoride
PMSF
Zn2+
slight inhibition at 1 mM
Zn2+
-
65% inhibition at 0.1 mM, 78% inhibition at 1 mM, 91% inhibition at 10 mM
Zn2+
-
23% residual activity in the presence of 2.0 mM Zn2+
additional information
no or poor inhibition by PMSF, E64, TLCK, pepstatin A, and leupeptin
-
additional information
-
no inhibition by PMSF
-
additional information
no inhibition by leupeptin and pepstatin A
-
additional information
-
no inhibition by leupeptin and pepstatin A
-
additional information
-
inhibition mechanisms, overview
-
additional information
the propeptides internally inhibits the enzyme in the 54 kDa zymogen in a cooperative inhibitory interaction
-
additional information
-
inhibited to a greater extend by D- than by L-hydroxamates of amino acids and aliphatic acids, pH-dependent
-
additional information
-
multiple inhibition study with substrate analogs and transition state analogs
-
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.14
Gly-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
10
L-Ala-4-nitroanilide
pH 8.0, 30°C
0.231
L-Ala-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.26
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
0.6
L-Arg-4-nitroanilide
pH 8.0, 30°C
0.078
L-Arg-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
1 - 7.51
L-Arg-p-nitroanilide
0.077
L-Cys-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.056 - 0.11
L-cystinyl-p-nitroanilide
0.01 - 4.4
L-Leu-4-nitroanilide
0.038 - 0.18
L-Leu-7-amido-4-methylcoumarin
25
L-Leu-Gly-Gly
-
pH 7.6-7.8, 60°C
0.57 - 1.79
L-Leu-p-nitroanilide
0.01 - 15
L-leucine 4-nitroanilide
45 - 78
L-leucine anilide
0.7
L-leucine ethyl ester
-
-
32 - 50
L-leucine-4-anisidide
0.22 - 0.85
L-Lys-4-nitroanilide
0.093 - 0.24
L-Met-7-amido-4-methylcoumarin
0.066
L-Phe-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.06
L-Thr-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
19
L-Val-4-nitroanilide
pH 8.0, 30°C
0.97
Leu-4-nitroanilide
pH 8.5, 50°C, recombinant enzyme
0.1 - 0.43
Leu-beta-naphthylamide
0.97
leucine-4-nitroaniline
-
pH 8.5, 60°C
0.96
Met-beta-naphthylamide
-
-
0.52
Phe-beta-naphthylamide
-
-
0.02726
recombinant human methionine-interferon alpha-2b
pH 6.0, 37°C
-
4 - 7
thionoleucine-4-anisidide
4 - 11
thionoleucine-S-anilide
0.19
Val-beta-naphthylamide
-
-
additional information
additional information
-
0.39
Cys-Gly
-
recombinant enzyme, at pH 8.0
0.44
Cys-Gly
-
recombinant enzyme, at pH 7.3
0.48
Cys-Gly
-
native enzyme, at pH 7.3
1
L-Arg-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
7.51
L-Arg-p-nitroanilide
-
mutant enzyme D198P/F221E, at pH 8.0 and 37°C
0.056
L-cystinyl-p-nitroanilide
-
mutant enzyme D198I/F221W, at pH 8.0 and 37°C
0.11
L-cystinyl-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
0.01
L-Leu-4-nitroanilide
mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.0106
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
0.013
L-Leu-4-nitroanilide
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.025
L-Leu-4-nitroanilide
mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.0317
L-Leu-4-nitroanilide
apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.245
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
0.25
L-Leu-4-nitroanilide
-
pH 8.0, 37°C, APII
0.311
L-Leu-4-nitroanilide
pH 8.0, 70°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
0.34
L-Leu-4-nitroanilide
mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.658
L-Leu-4-nitroanilide
-
pH 7.6-7.8, 60°C
0.9
L-Leu-4-nitroanilide
60°C, recombinant wild-type enzyme
0.902
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation
0.95
L-Leu-4-nitroanilide
-
wild type enzyme, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
1
L-Leu-4-nitroanilide
-
pH 8.5, 45°C, API
1.2
L-Leu-4-nitroanilide
60°C, recombinant mutant H191L
2.1
L-Leu-4-nitroanilide
-
pH 8.0, 55°C, recombinant wild-type enzyme
2.12
L-Leu-4-nitroanilide
-
mutant enzyme Y352D, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
2.83
L-Leu-4-nitroanilide
-
mutant enzyme Y352L, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
3.05
L-Leu-4-nitroanilide
-
mutant enzyme D380N, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
3.39
L-Leu-4-nitroanilide
-
mutant enzyme D380E, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
3.41
L-Leu-4-nitroanilide
-
mutant enzyme D380V, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
3.6
L-Leu-4-nitroanilide
pH 8.0, 30°C
4.4
L-Leu-4-nitroanilide
60°C, recombinant mutant H227L
0.038
L-Leu-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.18
L-Leu-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
0.57
L-Leu-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
1.15
L-Leu-p-nitroanilide
-
mutant enzyme D198F/F221I, at pH 8.0 and 37°C
1.72
L-Leu-p-nitroanilide
-
recombinant enzyme, at pH 7.3
1.79
L-Leu-p-nitroanilide
-
recombinant enzyme, at pH 8.0
0.01
L-leucine 4-nitroanilide
pH 8.0, 25°C
0.019
L-leucine 4-nitroanilide
-
-
0.019 - 0.0215
L-leucine 4-nitroanilide
-
native enzyme, buffer dependent
0.02
L-leucine 4-nitroanilide
-
-
0.021
L-leucine 4-nitroanilide
-
native enzyme
0.028
L-leucine 4-nitroanilide
-
-
0.032
L-leucine 4-nitroanilide
-
diethylpyrocarbonate-treated enzyme
0.055
L-leucine 4-nitroanilide
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
0.06
L-leucine 4-nitroanilide
-
nitro-enzyme
0.126
L-leucine 4-nitroanilide
-
photoinactivated enzyme
0.136
L-leucine 4-nitroanilide
-
azo-enzyme
4.6
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
7.8
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
15
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
45
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
61
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
78
L-leucine anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
32
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
34
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
50
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
0.22
L-Lys-4-nitroanilide
-
pH 8.0, 37°C
0.85
L-Lys-4-nitroanilide
pH 8.0, 30°C
0.093
L-Met-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.24
L-Met-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
0.1
Leu-beta-naphthylamide
-
-
0.43
Leu-beta-naphthylamide
-
-
0.05
Leu-Phe
-
-
4
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
4
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
5
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
7
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
4
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
8
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
10
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
11
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
additional information
additional information
kinetics
-
additional information
additional information
-
amides and dipeptides
-
additional information
additional information
-
amides and dipeptides
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
kinetics with metal-bound enzyme variants
-
additional information
additional information
-
kinetics of apoenzyme and metal-bound wild-type and mutant enzymes, isothermal titration measurement, thermodynamics, overview
-
additional information
additional information
kinetics of different native and recombinant enzyme forms, overview
-
additional information
additional information
-
kinetics of raw starch-binding by the chimeric mutant enzyme
-
additional information
additional information
-
kinetics of wild-type and methionine mutant enzymes, overview
-
additional information
additional information
-
kinetics with Zn and/or Cd-containing enzyme, overview
-
additional information
additional information
pH-dependence of kinetics, isothermal titration measurement, thermodynamics, overview
-
additional information
additional information
thermodynamics and Michaelis-Menten kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11
Gly-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
0.37
L-Ala-4-nitroanilide
pH 8.0, 30°C
192000
L-Ala-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
10
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
34
L-Arg-4-nitroanilide
pH 8.0, 30°C
59900
L-Arg-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
1.26 - 82
L-Arg-p-nitroanilide
288100
L-Cys-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
3.71 - 46.7
L-cystinyl-p-nitroanilide
0.017 - 10180
L-Leu-4-nitroanilide
17 - 246000
L-Leu-7-amido-4-methylcoumarin
49540
L-Leu-Gly-Gly
-
pH 7.6-7.8, 60°C
30 - 128
L-Leu-p-nitroanilide
1.1 - 4320
L-leucine 4-nitroanilide
6.3 - 16
L-leucine anilide
96
L-leucine ethyl ester
-
-
3.8 - 9.5
L-leucine-4-anisidide
10 - 17.7
L-Lys-4-nitroanilide
20 - 283200
L-Met-7-amido-4-methylcoumarin
33800
L-Phe-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
16200
L-Thr-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
0.43
L-Val-4-nitroanilide
pH 8.0, 30°C
29.6 - 38
Leu-beta-naphthylamide
8.2
Met-beta-naphthylamide
-
-
6.3
Phe-beta-naphthylamide
-
-
0.000853
recombinant human methionine-interferon alpha-2b
pH 6.0, 37°C
-
7.5 - 12.2
thionoleucine-4-anisidide
7.7 - 23.3
thionoleucine-S-anilide
0.26
Val-beta-naphthylamide
-
-
additional information
additional information
-
43.3
Cys-Gly
-
recombinant enzyme, at pH 8.0
46.7
Cys-Gly
-
native enzyme, at pH 7.3
60
Cys-Gly
-
recombinant enzyme, at pH 7.3
1.26
L-Arg-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
82
L-Arg-p-nitroanilide
-
mutant enzyme D198P/F221E, at pH 8.0 and 37°C
3.71
L-cystinyl-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
46.7
L-cystinyl-p-nitroanilide
-
mutant enzyme D198I/F221W, at pH 8.0 and 37°C
0.017
L-Leu-4-nitroanilide
apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.033
L-Leu-4-nitroanilide
pH 8.0, recombinant mutant E151H
0.035
L-Leu-4-nitroanilide
-
mutant enzyme D380E, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.048
L-Leu-4-nitroanilide
-
mutant enzyme D380V, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.113
L-Leu-4-nitroanilide
-
mutant enzyme Y352L, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.135
L-Leu-4-nitroanilide
-
mutant enzyme D380N, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.153
L-Leu-4-nitroanilide
-
mutant enzyme Y352D, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.29
L-Leu-4-nitroanilide
60°C, recombinant wild-type enzyme
0.303
L-Leu-4-nitroanilide
-
wild type enzyme, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C
0.46
L-Leu-4-nitroanilide
60°C, recombinant mutant H191L
0.7
L-Leu-4-nitroanilide
mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.817
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation
0.86
L-Leu-4-nitroanilide
60°C, recombinant mutant H227L
1.6
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
6.31
L-Leu-4-nitroanilide
-
pH 8.0, 55°C, recombinant wild-type enzyme
7
L-Leu-4-nitroanilide
mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
15.8
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
48.45
L-Leu-4-nitroanilide
pH 8.0, 70°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
55
L-Leu-4-nitroanilide
pH 8.0, 30°C
60
L-Leu-4-nitroanilide
mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
65
L-Leu-4-nitroanilide
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
71.33
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
73
L-Leu-4-nitroanilide
pH 8.0, recombinant wild-type enzyme
10180
L-Leu-4-nitroanilide
-
pH 7.6-7.8, 60°C
17
L-Leu-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
246000
L-Leu-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
30
L-Leu-p-nitroanilide
-
recombinant enzyme, at pH 7.3
41.3
L-Leu-p-nitroanilide
-
wild type enzyme, at pH 8.0 and 37°C
41.7
L-Leu-p-nitroanilide
-
recombinant enzyme, at pH 8.0
128
L-Leu-p-nitroanilide
-
mutant enzyme D198F/F221I, at pH 8.0 and 37°C
1.1
L-leucine 4-nitroanilide
-
-
1.1
L-leucine 4-nitroanilide
-
photoinactivated enzyme
3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
4
L-leucine 4-nitroanilide
-
azo-enzyme
5.3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
14.3
L-leucine 4-nitroanilide
-
nitro-enzyme
42
L-leucine 4-nitroanilide
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
50 - 69
L-leucine 4-nitroanilide
-
native enzyme, buffer dependent
55.5
L-leucine 4-nitroanilide
-
diethylpyrocarbonate-treated enzyme
60
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
64
L-leucine 4-nitroanilide
-
-
67
L-leucine 4-nitroanilide
-
-
67.3
L-leucine 4-nitroanilide
-
native enzyme
4320
L-leucine 4-nitroanilide
pH 8.0, 25°C
6.3
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
15.1
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
16
L-leucine anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
3.8
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
9.3
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
9.5
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
10
L-Lys-4-nitroanilide
pH 8.0, 30°C
17.7
L-Lys-4-nitroanilide
-
pH 8.0, 37°C
20
L-Met-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
283200
L-Met-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
29.6
Leu-beta-naphthylamide
-
-
38
Leu-beta-naphthylamide
-
-
41
Leu-Phe
-
-
7.5
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
7.9
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.1
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
12.2
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
7.7
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
10.6
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.5
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
16.9
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
23.3
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
additional information
additional information
-
penultimative substituents influence rate of hydrolysis
-
additional information
additional information
-
penultimative substituents influence rate of hydrolysis
-
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0.0001
-
recombinant enzyme, using L-Glu-7-amido-4-methylcoumarin as substrate, at 37°C
0.0002
-
native enzyme, using L-Glu-7-amido-4-methylcoumarin as substrate, at 37°C
0.0003
-
native enzyme, using L-Asp-7-amido-4-methylcoumarin as substrate, at 37°C
0.0005
-
native enzyme, using Gly-7-amido-4-methylcoumarin as substrate, at 37°C
0.0006
-
native enzyme, using L-Val-7-amido-4-methylcoumarin as substrate, at 37°C
0.0012
-
recombinant enzyme, using L-Asp-7-amido-4-methylcoumarin as substrate, at 37°C
0.0021
-
recombinant enzyme, using L-Ser-7-amido-4-methylcoumarin as substrate, at 37°C
0.0025
-
recombinant enzyme, using L-Val-7-amido-4-methylcoumarin as substrate, at 37°C
0.003
supernatant clarification, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.0032
-
native enzyme, using L-Pro-7-amido-4-methylcoumarin as substrate, at 37°C
0.0054
-
native enzyme, using L-Tyr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0056
-
recombinant enzyme, using L-Pro-7-amido-4-methylcoumarin as substrate, at 37°C
0.0062
-
recombinant enzyme, using L-Ile-7-amido-4-methylcoumarin as substrate, at 37°C
0.0064
-
recombinant enzyme, using L-Tyr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0068
-
recombinant enzyme, using L-Phe-7-amido-4-methylcoumarin as substrate, at 37°C
0.0075
-
recombinant enzyme, using L-Ala-7-amido-4-methylcoumarin as substrate, at 37°C
0.0083
-
native enzyme, using L-Ala-7-amido-4-methylcoumarin as substrate, at 37°C
0.0093
-
native enzyme, using L-Ile-7-amido-4-methylcoumarin as substrate, at 37°C
0.0141
-
native enzyme, using L-Phe-7-amido-4-methylcoumarin as substrate, at 37°C
0.0253
-
recombinant enzyme, using L-Met-7-amido-4-methylcoumarin as substrate, at 37°C
0.0291
-
recombinant enzyme, using L-Arg-7-amido-4-methylcoumarin as substrate, at 37°C
0.0355
-
recombinant enzyme, using L-Thr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0657
-
native enzyme, using L-Met-7-amido-4-methylcoumarin as substrate, at 37°C
0.0694
-
native enzyme, using L-Thr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0752
-
native enzyme, using L-Arg-7-amido-4-methylcoumarin as substrate, at 37°C
0.0831
-
recombinant enzyme, using L-Cys-7-amido-4-methylcoumarin as substrate, at 37°C
0.0953
-
native enzyme, using L-Cys-7-amido-4-methylcoumarin as substrate, at 37°C
0.1344
-
native enzyme, using L-Leu-7-amido-4-methylcoumarin as substrate, at 37°C
0.2145
-
recombinant enzyme, using L-Leu-7-amido-4-methylcoumarin as substrate, at 37°C
10.41
-
free recombinant wild-type enzyme
104.9
-
mutant enzyme Y532D, at 60°C, using L-Leu-4-nitroanilide as substrate
13.8
-
mutant enzyme D380E, at 60°C, using L-Leu-4-nitroanilide as substrate
132.5
purified native enzyme, pH 8.5, 50°C, substrate Leu-4-nitroanilide
133.4
purified recombinant wild-type enzyme
15.1
-
mutant enzyme D380V, at 60°C, using L-Leu-4-nitroanilide as substrate
15.86
-
immobilized recombinant wild-type enzyme
16
substrate L-leucine-4-nitroanilidepH 8.0, 37°C
18.22
-
free recombinant Lys9-tagged enzyme
20
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
21.71
-
free recombinant Lys3-tagged enzyme
22
-
mutant enzyme D198M/F221W, using L-Leu-p-nitroanilide as a substrate
240.48
purified recombinant enzyme, pH 8.5, 50°C, substrate Leu-4-nitroanilide
25
-
value about, substrate Gly-7-amido-4-methylcoumarin
34.5
-
mutant enzyme Y532L, at 60°C, using L-Leu-4-nitroanilide as substrate
4.17
-
value about, substrate L-Pro-7-amido-4-methylcoumarin
466.7
-
purified recombinant enzyme
55.3
-
mutant enzyme D380N, at 60°C, using L-Leu-4-nitroanilide as substrate
572.5
-
wild type enzyme, at 60°C, using L-Leu-4-nitroanilide as substrate
60.73
-
immobilized recombinant Lys3-tagged enzyme
60.8
purified recombinant mutant H227L
64
purified recombinant enzyme
68
-
wild type enzyme, using L-Leu-p-nitroanilide as a substrate
76.91
-
immobilized recombinant Lys9-tagged enzyme
8.3
-
value about, substrate L-Tyr-7-amido-4-methylcoumarin
80 - 115
-
native enzyme, buffer dependent
84
-
diethylpyrocarbonate-treated enzyme
91.3
purified recombinant mutant H191L
91.6
-
purified recombinant wild-type enzyme
0.0019
-
native enzyme, using L-Ser-7-amido-4-methylcoumarin as substrate, at 37°C
0.0019
-
recombinant enzyme, using Gly-7-amido-4-methylcoumarin as substrate, at 37°C
1.67
-
value about, substrate L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
1.67
-
value about, substrate L-Asp-7-amido-4-methylcoumarin
1.67
-
value about, substrate L-Gln-7-amido-4-methylcoumarin
1.67
-
value about, substrate L-Thr-7-amido-4-methylcoumarin
1.67
-
value about, substrate L-Trp-7-amido-4-methylcoumarin
120
purified Zn2+-bound enzyme
120
purified enzyme, in 10 mM Tricine buffer, pH 8.0, at 25°C
33.3
-
value about, substrate L-Leu-7-amido-4-methylcoumarin
33.3
-
value about, substrate L-Lys-4-nitroanilide
33.3
-
value about, substrate L-Met-7-amido-4-methylcoumarin
additional information
-
additional information
-
activities of free and immobilized recombinant Lys-tagged enzymes, overview
additional information
-
-
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Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites
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-
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Spectroscopic and thermodynamic characterization of the E151D and E151A altered leucine aminopeptidases from Aeromonas proteolytica
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32
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