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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
-
-
?