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Literature summary for 3.4.19.1 extracted from

  • Zhang, Z.; Zheng, B.; Wang, Y.; Chen, Y.; Manco, G.; Feng, Y.
    The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity (2008), Biochim. Biophys. Acta, 1784, 1176-1183.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
into the vector pET11a for expression in Escherichia coli BL21-CodonPlus DE3-RIL cells Aeropyrum pernix K1

Protein Variants

Protein Variants Comment Organism
D15A mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH Aeropyrum pernix K1
D15A/R18A mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH Aeropyrum pernix K1
DELTAN21 mutant, N-terminal helix deleted, no longer functional at the optimum temperature, 95°C, for the wild-type enzyme, low thermodynamic stability Aeropyrum pernix K1
R18A mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH Aeropyrum pernix K1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00913
-
Ac-Leu-p-nitroanilide mutant D15A Aeropyrum pernix K1
0.0094
-
Ac-Leu-p-nitroanilide mutant R18A Aeropyrum pernix K1
0.00958
-
Ac-Leu-p-nitroanilide mutant DELTAN21 Aeropyrum pernix K1
0.00963
-
Ac-Leu-p-nitroanilide mutant D15A/R18A Aeropyrum pernix K1
0.01038
-
Ac-Leu-p-nitroanilide wild-type 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
using Hi-Trap Q-Sepharose and HiLoad Sephacryl S-200 columns 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
77
-
mutant DELTAN21 Aeropyrum pernix K1
92
-
mutant D15A above 92° Aeropyrum pernix K1
92
-
mutant R18A above 92° Aeropyrum pernix K1
95
-
wild-type enzyme Aeropyrum pernix K1

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.04
-
Ac-Leu-p-nitroanilide wild-type Aeropyrum pernix K1
2.1
-
Ac-Leu-p-nitroanilide mutant R18A Aeropyrum pernix K1
2.14
-
Ac-Leu-p-nitroanilide mutant D15A/R18A Aeropyrum pernix K1
2.21
-
Ac-Leu-p-nitroanilide mutant D15A Aeropyrum pernix K1
2.64
-
Ac-Leu-p-nitroanilide mutant DELTAN21 Aeropyrum pernix K1

pH Optimum

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