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Literature summary for 3.4.19.1 extracted from

  • Yang, G.; Bai, A.; Gao, L.; Zhang, Z.; Zheng, B.; Feng, Y.
    Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability (2009), Biochim. Biophys. Acta, 1794, 94-102.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
for expression in Escherichia coli BL21-CodonPlus DE3-RIL cells Aeropyrum pernix K1

Protein Variants

Protein Variants Comment Organism
E88A mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, catalytic activity almost abolished Aeropyrum pernix K1
E88A/R526E mutant, lower thermodynamic stability than the wild-type Aeropyrum pernix K1
E88A/R526K mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, positive charge at position 526, catalytic activity almost abolished Aeropyrum pernix K1
E88A/R526V mutant, lower thermodynamic stability than the wild-type Aeropyrum pernix K1
E88D mutant, lower thermodynamic stability than the wild-type Aeropyrum pernix K1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.467
-
Ac-Leu-p-nitroanilide mutant R526V, in the presence of 1 M sodium chloride Aeropyrum pernix K1
0.49
-
Ac-Leu-p-nitroanilide wild-type Aeropyrum pernix K1
0.695
-
Ac-Leu-p-nitroanilide mutant E88A/R526V, in the presence of 1 M sodium chloride Aeropyrum pernix K1
0.748
-
Ac-Leu-p-nitroanilide wild-type, in the presence of 1 M sodium chloride Aeropyrum pernix K1
1.14
-
Ac-Leu-p-nitroanilide mutant E88A Aeropyrum pernix K1
1.19
-
Ac-Leu-p-nitroanilide mutant E88A/R526V Aeropyrum pernix K1
1.76
-
Ac-Leu-p-nitroanilide mutant E88A, in the presence of 1 M sodium chloride Aeropyrum pernix K1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Aeropyrum pernix K1 removal of an N-acylated amino acid from blocked peptides ?
-
?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix K1 Q9YBQ2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix K1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Leu-p-nitroanilide + H2O substrate peptidase assay Aeropyrum pernix K1 Ac-Leu + p-nitroaniline
-
?
additional information removal of an N-acylated amino acid from blocked peptides Aeropyrum pernix K1 ?
-
?

Synonyms

Synonyms Comment Organism
acylpeptide hydrolase
-
Aeropyrum pernix K1
apAPH
-
Aeropyrum pernix K1
APH
-
Aeropyrum pernix K1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
activity assay Aeropyrum pernix K1
90
-
-
Aeropyrum pernix K1

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.49
-
Ac-Leu-p-nitroanilide mutant E88A Aeropyrum pernix K1
8.75
-
Ac-Leu-p-nitroanilide mutant E88A/R526V Aeropyrum pernix K1
10.5
-
Ac-Leu-p-nitroanilide mutant R526V, in the presence of 1 M sodium chloride Aeropyrum pernix K1
10.6
-
Ac-Leu-p-nitroanilide wild-type Aeropyrum pernix K1
10.9
-
Ac-Leu-p-nitroanilide mutant E88A/R526V, in the presence of 1 M sodium chloride Aeropyrum pernix K1
32.4
-
Ac-Leu-p-nitroanilide mutant E88A, in the presence of 1 M sodium chloride Aeropyrum pernix K1
36.4
-
Ac-Leu-p-nitroanilide wild-type, in the presence of 1 M sodium chloride Aeropyrum pernix K1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
activity assay Aeropyrum pernix K1