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2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
2-aminobenzoyl-EALFQGPF(NO2)A + H2O
?
very good substrate
-
-
?
2-aminobenzoyl-EFSPF(NO2)RA + H2O
?
-
-
-
?
2-aminobenzoyl-GFEPF(NO2)RA + H2O
?
good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide
-
-
?
2-aminobenzoyl-KARVLF(NO2)EA-Nle + H2O
?
poor substrate
-
-
?
2-aminobenzoyl-RPIITTAGPSF(NO2)A + H2O
?
-
-
-
?
2-aminobenzoyl-SAVLQSGF(NO2)A + H2O
?
good substrate
-
-
?
2-naphthyl butyrate + H2O
2-naphthol + butanoate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Abz-EFSPF(NO2)RA + H2O
?
-
-
-
?
Abz-GFEPF(NO2)RA + H2O
?
-
-
-
?
Abz-KARVLF(NO2)EANle + H2O
?
-
-
-
?
Abz-SAVLQSGF(NO2)A + H2O
?
-
-
-
?
Ac-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
-
-
-
?
Ac-Ala-7-amido-4-methylcoumarin + H2O
N-acetyl-L-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Ac-Leu-4-nitroanilide + H2O
Ac-Leu + 4-nitroaniline
-
-
-
?
Ac-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
Ac-Phe-2-naphthylamide + H2O
?
-
-
-
?
Ac-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
-
-
-
?
Ac-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
-
-
-
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
acetyl-Ala-7-amido-4-methylcoumarin + H2O
?
very slow hydrolysis
-
-
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
acetyl-Ala-Ala methyl ester + H2O
?
-
-
-
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
acetyl-Ala-Ala-Phe-Gly + H2O
?
-
-
-
-
?
acetyl-Ala-Gly-D-Ala-Ala + H2O
?
-
-
-
-
?
acetyl-Ala-Met + H2O
acetyl-Ala + Met
-
native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
acetyl-Gly-Leu + H2O
acetyl-Gly + Leu
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
acetyl-Met-7-amido-4-methylcoumarin + H2O
acetyl-Met + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
acetyl-Met-Asn + H2O
acetyl-Met + Asn
-
native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
acetyl-Met-Phe + H2O
acetyl-Met + Phe
native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Phe-2-naphthylamide + H2O
?
classical substrate of AAP
-
-
?
acetyl-Phe-2-naphthylamide + H2O
acetyl-Phe + 2-naphthylamine
-
-
-
?
acetyl-Phe-4-nitroanilide + H2O
acetyl-Phe + 4-nitroaniline
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
acetyl-Tyr-4-nitroanilide + H2O
acetyl-Tyr + 4-nitroaniline
AB009494
-
-
-
?
Ala-Ala-Ala + H2O
Ala + Ala-Ala
Ala-Ala-Ala + H2O
Ala-Ala + Ala
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala + Ala-Ala-Ala
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
alpha-melanocyte stimulating hormone + H2O
?
-
-
-
-
?
amyloid-beta peptide + H2O
?
-
-
-
-
?
Asp-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
Asp-Pro-p-nitroanilide + H2O
?
-
-
-
-
?
butyryl thiocholine + H2O
?
-
-
-
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
formyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
formyl-Gly-Val + H2O
formyl-Gly + Val
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Met-Ala + H2O
formyl-Met + Ala
AB009494
-
-
-
?
formyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
formyl-Met-Ala-Ser + H2O
formyl-Met + Ala-Ser
AB009494
-
-
-
?
formyl-Met-Leu-Gly + H2O
formyl-Met + Leu-Gly
AB009494
-
-
-
?
formylalanine-Ala-Ala + H2O
?
-
-
-
-
?
formylalanine-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
formylmethionine p-nitroanilide + H2O
formylmethionine + p-nitroaniline
-
-
-
-
?
formylmethionine-Ala + H2O
formylmethionine + Ala
-
-
-
-
?
formylmethionine-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
formylmethionine-Ala-Ser + H2O
?
-
-
-
-
?
formylmethionine-beta-naphthylamide + H2O
formylmethionine + beta-naphthylamine
-
-
-
-
?
formylmethionine-Leu + H2O
formylmethionine + Leu
-
-
-
-
?
formylmethionine-Leu-Gly + H2O
?
-
-
-
-
?
formylmethionine-Leu-Phe + H2O
?
-
-
-
-
?
formylmethionine-Leu-Tyr + H2O
?
-
-
-
-
?
formylmethionine-Phe + H2O
formylmethionine + Phe
-
-
-
-
?
formylmethionine-Trp + H2O
formylmethionine + Trp
-
-
-
-
?
formylmethionine-Val + H2O
formylmethionine + Val
-
-
-
-
?
glutaryl-GGF-7-amido-4-methylcoumarin + H2O
?
has a rate constant comparable to that of acetyl-Phe-2-naphthylamide
-
-
?
Gly-Ala-Ala + H2O
Gly-Ala + Ala
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
?
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
-
-
-
?
glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O
?
-
no degradation of the native protein
-
?
isoAsp-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
isoD/DAEFRHDSGYEVHHQKLVFFAEDVGSNKGA-NH2 + H2O
?
-
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
N-acetyl-Ala ethyl ester + H2O
N-acetyl-Ala + ethanol
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
N-acetyl-Ala-Ala-Ala-Ala-Glu-Glu-Glu-Lys + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Arg-Gly + H2O
N-acetyl-Ala + Ala-Arg-Gly
-
-
-
-
?
N-acetyl-Ala-Ala-Gln-Nepsilon-acetyl-Lys + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Gln-Nepsilon-succinyl-Lys + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-His-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Phe-Gly + H2O
N-acetyl-Ala + Ala-Phe-Gly
-
-
-
-
?
N-acetyl-Ala-Ala-Pro + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Pro-Ala + H2O
N-acetyl-Ala + Ala-Pro-Ala
-
-
-
-
?
N-acetyl-Ala-Asp + H2O
N-acetyl-Ala + Asp
-
-
-
-
?
N-acetyl-Ala-beta-naphthylamide + H2O
N-acetyl-Ala + beta-naphthylamine
-
-
-
-
?
N-acetyl-Ala-Gly + H2O
N-acetyl-Ala + Gly
-
-
-
-
?
N-acetyl-Ala-Gly-Ala-D-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-His-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Leu + H2O
N-acetyl-Ala + Leu
-
-
-
-
?
N-acetyl-Ala-Lys + H2O
N-acetyl-Ala + Lys
-
-
-
-
?
N-acetyl-Ala-Met + H2O
N-acetyl-Ala + Met
-
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
N-acetyl-Ala-Phe + H2O
N-acetyl-Ala + Phe
-
-
-
-
?
N-acetyl-Ala-Ser + H2O
N-acetyl-Ala + Ser
-
-
-
-
?
N-acetyl-Ala-Thr + H2O
N-acetyl-Ala + Thr
-
-
-
-
?
N-acetyl-Ala-Trp + H2O
N-acetyl-Ala + Trp
-
-
-
-
?
N-acetyl-Ala-Tyr + H2O
N-acetyl-Ala + Tyr
-
-
-
-
?
N-acetyl-Ala-Tyr-Ile + H2O
?
-
-
-
-
?
N-acetyl-alanyl-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
-
-
-
?
N-acetyl-Glu p-nitroanilide + H2O
N-acetyl-Glu + p-nitroaniline
-
-
-
-
?
N-acetyl-Gly-Ala + H2O
N-acetyl-Gly + Ala
-
weak activity
-
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
N-acetyl-L-alanine 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
N-acetyl-L-Met-alpha-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-Ala-NH2
-
-
-
-
?
N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-L-Ala-NH2
-
-
-
?
N-acetyl-L-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
N-acetyl-Leu p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
-
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-Leu + 4-nitroaniline
-
-
-
-
?
N-acetyl-Leu-Ala + H2O
N-acetyl-Leu + Ala
-
-
-
-
?
N-acetyl-Leu-p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
N-acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Met-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
-
-
-
-
?
N-acetyl-Met-Asp-Arg-Val-Leu-Ser-Arg-Tyr + H2O
?
-
-
-
-
?
N-acetyl-Met-Asp-Glu-Thr-Gly-Asp-Thr-Ala-Leu-Val-Ala + H2O
?
-
-
-
-
?
N-acetyl-Met-epsilon-Lys + H2O
N-acetyl-Met + Lys
-
-
-
?
N-acetyl-Met-Leu + H2O
?
-
-
-
-
?
N-acetyl-Met-Leu-Gly + H2O
?
-
-
-
-
?
N-acetyl-Met-Leu-Phe + H2O
?
-
-
-
-
?
N-acetyl-Met-Lys + H2O
N-acetyl-Met + Lys
-
-
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
kinetic assay
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
N-acetyl-Phe-Ala + H2O
N-acetyl-Phe + Ala
-
weak activity
-
-
?
N-acetyl-Ser-Ala + H2O
N-acetyl-Ser + Ala
-
-
-
-
?
N-acetyl-Tyr p-nitroanilide + H2O
N-acetyl-Tyr + p-nitroaniline
-
-
-
-
?
N-acetyl-Tyr-Ala + H2O
N-acetyl-Tyr + Ala
-
weak activity
-
-
?
N-acylpeptide + H2O
?
-
acylpeptide hydrolase catalyzes the hydrolysis of short peptides of the type Nalpha-acyl to form an acyl amino acid and a peptide with a free N-terminus
-
-
?
naphthyl butyrate + H2O
naphthol + butyrate
-
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
?
-
-
-
-
?
p-nitrophenyl caprylate + H2O
nitrophenol + caprylate
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
-
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propionate
-
-
-
-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
-
-
-
-
?
Phe-beta-naphthylamide + H2O
Phe + 2-naphthylamine
-
-
-
-
?
Phe-p-nitroanilide + H2O
Phe + p-nitroaniline
-
prefered substrate for PMH
-
-
?
Pro-beta-naphthylamide + H2O
Pro + 2-naphthylamine
-
-
-
-
?
puromycin + H2O
?
-
-
-
-
?
succinyl-AAA-4-nitroanilide + H2O
succinyl-AAA + 4-nitroaniline
-
-
-
?
succinyl-AAPF-2-naphthylamide + H2O
?
hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide
-
-
?
succinyl-GGF-4-nitroanilide + H2O
succinyl-GGF + 4-nitroaniline
-
-
-
?
Tyr-beta-naphthylamide + H2O
Tyr + 2-naphthylamine
-
-
-
-
?
Z-GGL-4-nitroanilide + H2O
Z-GGL + 4-nitroaniline
-
-
-
?
additional information
?
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
endopeptidase activity
-
-
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
endopeptidase activity
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
substrate peptidase assay
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
-
substrate peptidase assay
-
-
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
AB009494
the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
-
-
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
-
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
AB009494
-
-
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
-
native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
-
native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
AB009494
-
-
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
-
native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
AB009494
the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
-
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
-
-
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
-
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
AB009494
-
-
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
-
native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Ala-Ala + H2O
Ala + Ala
-
-
-
?
Ala-Ala + H2O
Ala + Ala
-
-
-
?
Ala-Ala-Ala + H2O
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
Ala + Ala-Ala
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
prefered substrate for PMH
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
prefered substrate for PMH
-
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
-
native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
-
native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
AB009494
-
-
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
-
-
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
N-acetyl-Ala-Ala
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
N-acetyl-Ala-Ala-Ala
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
-
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
-
-
?
N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
-
-
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
-
-
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
-
-
-
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
-
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
-
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
-
-
-
-
?
Tyr-Phe + H2O
Tyr + Phe
-
-
-
-
?
Tyr-Phe + H2O
Tyr + Phe
-
-
-
-
?
additional information
?
-
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
the enzyme is also active with fatty acid esters, e.g. with 4-nitrophenyl caprylate. Substrate binding mechanism analysis, and random acceleration and steered molecular dynamics simulations of ligands unbinding pathways from APH. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. Overview
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess
-
-
?
additional information
?
-
the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess
-
-
?
additional information
?
-
-
the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme
-
-
?
additional information
?
-
-
the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins
-
?
additional information
?
-
-
the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
-
-
?
additional information
?
-
APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
-
APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
-
-
?
additional information
?
-
-
acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
-
-
?
additional information
?
-
-
rapid removal of acetyl-Thr, acetyl-Ala, acetyl-Met, acetyl-Ser and more slowly acetyl-Gly from peptides of different lengths. Other N-acetylated amino acids, Cys, Tyr, Asp, Val, Phe, Ile, Leu, may be removed at 1% or less of the rate of the good substrates
-
-
?
additional information
?
-
-
N-acetylated peptides with D-Ala in position 3 or 4 as are good substrates as those containing L-Ala. Peptides with Pro in position 2 are inactive, and most of the peptides with Pro in the third position are very good substrates. Only the peptide acetyl-AAP gives 30% of the activity of acetyl-AAA, which is reduced to 1-2% if additional residues are present at the C-terminus, acety-AAPA or acetyl-AAPAA. The presence of a positive charge in position 2,3,4,5 and 6 gives strong reduction in hydrolase activity, varying with the charge's distance from the N-terminus from 9 to 15-20% of the rate obtained with the reference peptides without positive charges. Deprotonation of His at high pH generates excellent substrates, and removal of the positive charges of Lys by acetylation or succinylation give improved substrate quality. Long peptides with 10-29 residues, are poor substrates, especially when they contain positive charges and Pro
-
-
?
additional information
?
-
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
-
-
?
additional information
?
-
-
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
-
-
?
additional information
?
-
AB009494
high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
-
-
?
additional information
?
-
-
high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
-
-
?
additional information
?
-
-
specific for N-terminal acylmethionine residues
-
-
?
additional information
?
-
no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity
-
-
?
additional information
?
-
-
no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity
-
-
?
additional information
?
-
no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
-
-
?
additional information
?
-
-
no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
-
-
?
additional information
?
-
no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide
-
-
?
additional information
?
-
no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity
-
-
?
additional information
?
-
no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
-
-
?
additional information
?
-
no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide
-
-
?
additional information
?
-
promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
-
-
?
additional information
?
-
the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
-
-
?
additional information
?
-
promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
-
-
?
additional information
?
-
the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
-
-
?
additional information
?
-
promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
-
-
?
additional information
?
-
promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
-
-
?
additional information
?
-
the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
-
-
?
additional information
?
-
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
-
-
?
additional information
?
-
promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
-
-
?
additional information
?
-
-
peptidase activity is only exerted on peptides with Gly or Ala at their N-termini
-
-
?
additional information
?
-
-
the enzyme might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins
-
-
?
additional information
?
-
-
the enzyme may be involved in regulation of neuropeptide turnover
-
?
additional information
?
-
-
His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
-
-
?
additional information
?
-
-
catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
-
-
?
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(10E,12Z)-octadeca-10,12-dienoic acid
-
non-competitive inhibition mechanism
1-butane boronic acid
-
-
1-ethyl-3,3'-dimethylaminopropylcarbodiimide
-
-
1-methylethyl dodecylphosphonofluoridoate
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
4-(2-aminoethyl) benzenesulfonyl fluoride
-
-
5,5'-dithiobis-(2-nitrobenzoate)
-
partial
Ac-Ala
-
competitive inhibitor
Ac-Gly-prolineboronic acid
-
-
Ac-Leu-CH2-Cl
-
irreversible inhibitor
Ac-Met
-
competitive inhibitor
Ac-Phe-OH
product-like inhibitor
acephate
-
IC50: 0.0062 mM
acetyl-Gly-prolineboronic acid
-
selectivity for APH 25fold higher than for fibroblast activation protein
activated-thiol-Sepharose
-
-
-
benzyloxycarbonyl-Gly-Gly-Phe-chloromethyl ketone
CMK, chloromethyl ketone inhibitor, enzyme binding structure analysis, molecular dynamics studies, overview
bis(1-methylethyl) 4-nitrophenyl phosphate
-
IC50: 0.016 mM
bis(sulfosuccinimidyl)suberate
-
-
CaCl2
100 mM, 52% inhibition
carbodiimide/aminoalkyl-agarose
-
-
-
carbodiimide/dicarboxylic acid
-
-
-
chlorfenvinphos
-
IC50 at pH 7.4, 37°C: 1386 nM
chlorpyrifos isopropyl
-
IC50: 0.0033 mM
chlorpyrifos n-butyl
-
IC50: 0.00006 mM
chlorpyrifos n-propyl
-
IC50: 0.00007 mM
chlorpyrifos-methyl oxon
-
IC50 at pH 7.4, 37°C: 18.3 nM
chlorpyrifosmethyl oxon
-
Cl-
-
activity towards N-acetyl-Ala-Ala and N-acetyl-Ala-Ala-Ala
CoCl2
-
1 mM, 21% inhibition
di(2-pyridyl)disulfide
-
-
dicyclohexyl 2,2-dichloroethenyl phosphate
diethyl 4-methyl-3-nitrophenyl phosphate
-
IC50: 0.002 mM
diisopropyl fluorophosphate
diisopropylfluorophosphate
diphenylphosphinic fluoride
EDTA
1 mM, 10% inhibition
ethyl octylphosphonofluoridoate
FeCl2
-
1 mM, 21% inhibition
Guanidine-HCl
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
guanidine/HCl
-
1 M, complete inactivation
heptyl ethylphosphonofluoridoate
malaoxon
-
IC50 at pH 7.4, 37°C: 1400000 nM
malathion
significantly inhibits the activity of enzyme APH both in vitro and in vivo
Mipafox
-
IC50 at pH 7.4, 37°C: 3013 nM
N,N-Dimethylformamide
-
-
N-acetyl-Ala chloromethyl ketone
-
inactivation follows first order kinetics, acetyl-Ala protects
N-acetyl-Leu chloromethyl ketone
-
-
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
i.e. Woodward's reagent
N-hydroxysuccinimide agarose
-
-
-
NaCl
-
1 mM, 78% loss of activity
nonyl ethylphosphonofluoridoate
octane-1-sulfonyl fluoride
octyl methylphosphonofluoridoate
p-hydroxymercuribenzoate
-
-
p-nitrophenyl-N-propyl carbamate
-
potent active site-directed, pseudo-first-order kinetics
pentyl ethylphosphonofluoridoate
peptide SsCEI 2
-
specific and efficient inhibition. No inhibition in presence of peptide SsCEI 3 and peptide SsCEI 4
-
phenylmethylsulfonyl fluoride
-
-
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
phoxim
significantly inhibits the activity of enzyme APH both in vitro and in vivo
profenofos
-
IC50: 0.002 mM
SCN-
-
activity towards N-acetyl-Ala-Ala and N-acetyl-Ala-Ala-Ala
Sulfolobus solfataricus chymotrypsin-elastase inhibitor
specific inhibition
-
Trichlorfon
-
IC50: 0.018 mM
tridecyl methylphosphonofluoridoate
Triton X-100
1 mg/ml, 4% inhibition
Tween 20
1 mg/ml, 10% inhibition
Tween 80
1 mg/ml, 18% inhibition
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.00026 mM
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.0015 mM
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00018 mM
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00023 mM
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0015 mM
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0011 mM
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0014 mM
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0016 mM
Acetyl-Phe
forms hydrogen bonds with both NH groups of the oxyanion binding site of AAP. In the mutant enzyme the NH bond of Gly369 points in a different direction
chlorpyrifos
binding structure, docking study, and molecular dynamics simulations using structure PDB ID 1VE7 as search model, and umbrella sampling calculations, molecular mechanical/GBSA calculations, enzyme-inhibitor complex structure, overview
chlorpyrifos
significantly inhibits the activity of enzyme APH both in vitro and in vivo
chlorpyrifos
-
IC50: 0.000021 mM
chlorpyrifos
-
IC50: 0.000071 mM
chlorpyrifos cyclohexyl
-
IC50: 0.00086 mM
chlorpyrifos cyclohexyl
-
IC50: 0.00035 mM
chlorpyrifos methyl
-
IC50: 0.000080 mM
chlorpyrifos methyl
-
IC50: 0.00031 mM
Cu2+
1 mM, complete inhibition of recombinant enzyme
Cu2+
-
1 mM, complete inhibition of recombinant enzyme
DFP
-
-
DFP
-
IC50 at pH 7.4, 37°C: 22.5 nM
DFP
-
the reactive residue is Ser587
diazoxon
-
IC50: 0.00093 mM
diazoxon
-
IC50: 0.00089 mM
diazoxon
-
IC50 at pH 7.4, 37°C: 1386 nM
dichlorvos
-
dichlorvos
-
IC50: 0.00023 mM
dichlorvos
-
shows selectivity for acylpeptide hydrolase inhibition in vivo
dichlorvos
-
IC50: 0.00056 mM
dichlorvos
-
acylpeptide hydrolase activity shows a significant inhibition
dichlorvos
-
IC50 at pH 7.4, 37°C: 118.6 nM
dichlorvos
-
exhibits high affinity for acylpeptide hydrolase, possibly blocks its activity toward N-acylpeptide
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00010 mM
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00025 mM
diethyl dicarbonate
-
-
diisopropyl fluorophosphate
1 mM, complete inactivation
diisopropyl fluorophosphate
-
1 mM, complete inactivation
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropylfluorophosphate
-
IC50: 0.000011 mM
diisopropylfluorophosphate
-
IC50: 0.000017 mM
dipentyl fluorophosphate
-
IC50: 0.000011 mM
dipentyl fluorophosphate
-
IC50: 0.0000099 mM
diphenylphosphinic fluoride
-
IC50: 0.00041 mM
diphenylphosphinic fluoride
-
IC50: 0.00024 mM
ethyl octylphosphonofluoridoate
-
IC50: 0.00011 mM
ethyl octylphosphonofluoridoate
-
IC50: 0.00021 mM
heptyl ethylphosphonofluoridoate
-
IC50: 0.000027 mM
heptyl ethylphosphonofluoridoate
-
IC50: 0.00023 mM
Hg2+
-
-
iodoacetamide
-
-
iodoacetic acid
-
partial
N-acetyl-Ala
-
-
N-acetyl-Ala
-
competitive
N-acetyl-Ala
-
N-acetyl-D-Ala; N-acetyl-L-Ala
N-acetyl-Met
-
-
naled
-
IC50: 0.00037 mM
NEM
1 mM
nonyl ethylphosphonofluoridoate
-
IC50: 0.000052 mM
nonyl ethylphosphonofluoridoate
-
IC50: 0.00028 mM
octane-1-sulfonyl fluoride
-
IC50: 0.073 mM
octane-1-sulfonyl fluoride
-
IC50: 0.067 mM
octyl methylphosphonofluoridoate
-
IC50: 0.000043 mM
octyl methylphosphonofluoridoate
-
IC50: 0.00016 mM
paraoxon
-
IC50: 0.0047 mM
paraoxon
-
IC50 at pH 7.4, 37°C: 3805 nM
PCMB
0.1 mM
pentyl ethylphosphonofluoridoate
-
IC50: 0.00013 mM
pentyl ethylphosphonofluoridoate
-
IC50: 0.00027 mM
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
-
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
-
PMSF
1 mM, 50% inhibition
PMSF
-
1 mM, 50% inhibition
SDS
-
-
SDS
above 0.3 mM, complete inhibition
SDS
1 mg/ml, complete inhibition
tridecyl methylphosphonofluoridoate
-
IC50: 0.00032 mM
tridecyl methylphosphonofluoridoate
-
IC50: 0.0048 mM
Urea
-
-
Urea
6 M, about 70% loss of activity, regains activity at almost all urea concentrations upon removal of the denaturinf agent
Zn2+
1 mM, complete inhibition of recombinant enzyme
Zn2+
-
1 mM, complete inhibition of recombinant enzyme
Zn2+
-
most potent inhibitor
additional information
different organophosphorous compounds bind to the enzyme inducing conformational changes in two domains, namely, alpha/beta hydrolase and beta-propeller, computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos, and molecular dynamics simulations of enzyme bound to the inhibitors, the starting model of APH is derived from 2.7 A resolution crystal structure of acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (PDB ID 1VE7), overview. The docking study reveals that Val471 and Gly368 are important residues for chlorpyrifosmethyl oxon and dichlorvos binding
-
additional information
-
alphabeta peptide (1-40) can inhibit APH activity from the cell lysates of APH transfected cells after IP at 0.01 and 0.001 mM concentration, while reversed alphabeta peptide (40-1) at the same concentrations does not show any inhibitory effect
-
additional information
-
acylpeptide hydrolase is a direct target for some organophosphate compounds
-
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metabolism
AB009494
the existence of the acylamino acid-releasing enzyme in archaea suggests that the mechanisms of protein degradation or initiation of protein synthesis or both in archaea may be similar to those in eukaryotes
evolution
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
evolution
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
evolution
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
evolution
the enzyme belongs to a class of serine-type protease belonging to the prolyl oligopeptidase (POP) family. The members of the POP family are involved in numerous metabolic processes
evolution
the enzyme belongs to a serine peptidase family
evolution
the enzyme belongs to the prolyl oligopeptidase family of serine proteases
evolution
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
-
the enzyme belongs to a serine peptidase family
-
evolution
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
-
the enzyme belongs to a serine peptidase family
-
malfunction
-
overexpression of AARE/OPH exhibits no apparent effect on the level of oxidized proteins because wild types have inherently high AARE/OPH activity
malfunction
-
the AtAARE-suppressed plants using RNAi became susceptible to oxidative stress corresponding to enhanced accumulation of oxidized proteins
malfunction
-
transgenic overexpression of APH results in crystallin cleavage, impaired lens development, and cataract
physiological function
-
APH is involved in the generation of peptides that have the potential to induce protein aggregation
physiological function
-
AtAARE contributes to eliminate oxidized proteins to sustain the antioxidant system in the cytoplasm
physiological function
acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides
physiological function
enzyme APEH is a component of the cellular response to DNA damage. APEH is primarily localised in the cytoplasm, but a subfraction of the enzyme is sequestered at sites of nuclear damage following UVA irradiation or following oxidative stress. Localization of APEH at sites of nuclear damage is mediated by direct interaction with XRCC1, a scaffold protein that accelerates the repair of DNA single-strand breaks. APEH interacts with the amino-terminal domain of XRCC1, and APEH facilitates both single-strand break repair and cell survival following exposure to H2O2 in human cells
physiological function
enzyme BmAPHmay be involved in enhancing silkworm tolerance to organophosphorus (OP) insecticides
additional information
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
additional information
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
additional information
exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations, overview
additional information
molecular docking and molecular dynamics simulations using the structure with PDB ID 1VE7, substrate binding structures, overview
additional information
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
-
substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686
additional information
-
the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686
additional information
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
additional information
the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold
additional information
-
the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
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D524A
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
D524N
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
F488G/R526V/T560W
1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
H367A
displays significantly reduced catalytic activity. Unlike the reaction of the wild-type, the reaction of the mutant displays completely linear temperature dependence. Its reaction is associated with unfavourable entropy of activation
R526 I
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 17.3fold higher than the wild-type ratio
R526A
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 11.7fold higher than the wild-type ratio
R526E
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 115.5fold higher than the wild-type ratio
R526K
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 13.9fold higher than the wild-type ratio
R526L
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 14.8fold higher than the wild-type ratio
R526V/T560W
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
W474V/F488G/R526V/T560W
the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V
W474V/R526V/T560W
3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
D524A
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
-
D524N
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
-
F488G/R526V/T560W
-
1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
-
R526V
-
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
-
R526V/T560W
-
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
-
W474V/R526V/T560W
-
3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
-
D15A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
D15A/R18A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
DELTA1-21
-
optimal temperature of a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is decreased by 15°C
DELTAN21
mutant, N-terminal helix deleted, no longer functional at the optimum temperature, 95°C, for the wild-type enzyme, low thermodynamic stability
E88A
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, catalytic activity almost abolished
E88A/R526E
mutant, lower thermodynamic stability than the wild-type
E88A/R526K
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, positive charge at position 526, catalytic activity almost abolished
E88A/R526V
mutant, lower thermodynamic stability than the wild-type
E88D
mutant, lower thermodynamic stability than the wild-type
H367A
mutant, displays significantly reduced catalytic activity
R18A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
S445A
nearly inactive. Remaining activity of the mutant can cause cleavage in the peptide
R526V
Ac-Leu-4-nitroanilide bound to R526V AAP to form a more disordered loop (residues 552-562) in the alpha/beta-hydrolase fold like of AAP, which causes an open and inactive AAP domain form, secondly, binding 4-nitrophenylcaprylate and Ac-Leu-4-nitroanilide to AAP can decrease the flexibility of residues 225-250, 260-270 and 425-450, in which the ordered secondary structures may contain the suitable geometrical structure and so it is useful to serine attack
S587A
-
mutated in the active site
E10A
-
a 20-min pre-incubation at 50°C leads to a residual of 65% (wild-type: 70%)
K6A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
K6A/E10A
-
a 20-min pre-incubation at 50°C leads to a residual of 45% (wild-type: 70%)
N3A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
R14A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
A587S
-
no hydrolytic activity
N675S
-
no hydrolytic activity
Y707H
-
no hydrolytic activity
R526V
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 22.3fold higher than the wild-type ratio
R526V
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
additional information
construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology
additional information
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
additional information
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
additional information
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
-
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
-
additional information
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
-
enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
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Homo sapiens
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Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix K1 (Q9YBQ2)
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Homo sapiens, Sus scrofa
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Zhang, Z.; Zheng, B.; Wang, Y.; Chen, Y.; Manco, G.; Feng, Y.
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Aeropyrum pernix K1 (Q9YBQ2), Aeropyrum pernix K1
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Pyrococcus horikoshii (O58323), Pyrococcus horikoshii
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Aeropyrum pernix K1 (Q9YBQ2), Aeropyrum pernix K1
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Saccharolobus solfataricus (Q97VD6), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VD6)
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Pyrococcus horikoshii (O58323), Pyrococcus horikoshii DSM 12428 (O58323)
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Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YBQ2)
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Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods
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Deinococcus radiodurans
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Arabidopsis thaliana
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Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Aeropyrum pernix NBRC 100138 (Q9YBQ2)
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Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii JCM 10545 (Q973W9), Sulfurisphaera tokodaii 7T (Q973W9)
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Sulfurisphaera tokodaii (Q973W9), Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Sulfurisphaera tokodaii 7 (Q973W9), Sulfurisphaera tokodaii DSM 16993 (Q973W9), Sulfurisphaera tokodaii JCM 10545 (Q973W9), Aeropyrum pernix NBRC 100138 (Q9YBQ2), Sulfurisphaera tokodaii NBRC 100140 (Q973W9)
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Yu, X.; Wang, Q.; Zhou, Y.; Gao, R.; Wang, Y.
Cloning and application of a new acylaminoacyl peptidase from Bacillus subtilis 168 for aldol reaction
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Bacillus subtilis (A8CWI2), Bacillus subtilis 168 (A8CWI2)
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Zeng, Z.; Rulten, S.; Breslin, C.; Zlatanou, A.; Coulthard, V.; Caldecott, K.
Acylpeptide hydrolase is a component of the cellular response to DNA damage
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Homo sapiens (P13798), Homo sapiens
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Sporosarcina psychrophila (E1VFE0), Sporosarcina psychrophila
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Fu, P.; Sun, W.; Zhang, Z.
Molecular cloning, expression and characterization of acylpeptide hydrolase in the silkworm, Bombyx mori
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Bombyx mori (A0A0X9PFK4), Bombyx mori
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Yu, X.; Perez, B.; Zhang, Z.; Gao, R.; Guo, Z.
Mining catalytic promiscuity from thermophilic archaea an acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) for nitroaldol reactions
Green Chem.
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Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii 7 (Q973W9), Sulfurisphaera tokodaii DSM 16993 (Q973W9), Sulfurisphaera tokodaii JCM 10545 (Q973W9), Sulfurisphaera tokodaii NBRC 100140 (Q973W9)
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Jin, H.; Zhou, Z.; Wang, D.; Guan, S.; Han, W.
Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos
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Aeropyrum pernix (Q9YBQ2)
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Wang, D.; Jin, H.; Wang, J.; Guan, S.; Zhang, Z.; Han, W.
Exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations
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Aeropyrum pernix (Q9YBQ2)
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Zhu, J.; Wang, Y.; Li, X.; Han, W.; Zhao, L.
Understanding the interactions of different substrates with wild-type and mutant acylaminoacyl peptidase using molecular dynamics simulations
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Homo sapiens (P13798), Homo sapiens, Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Aeropyrum pernix NBRC 100138 (Q9YBQ2)
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Jin, H.; Zhu, J.; Dong, Y.; Han, W.
Exploring the different ligand escape pathways in acylaminoacyl peptidase by random acceleration and steered molecular dynamics simulations
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Aeropyrum pernix (Q9YBQ2)
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