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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.1 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
3.4.19.1 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
3.4.19.1 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
3.4.19.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.1 0.00913
-
 Ac-Leu-p-nitroanilide mutant D15A Aeropyrum pernix K1
3.4.19.1 0.0094
-
 Ac-Leu-p-nitroanilide mutant R18A Aeropyrum pernix K1
3.4.19.1 0.00958
-
 Ac-Leu-p-nitroanilide mutant DELTAN21 Aeropyrum pernix K1
3.4.19.1 0.00963
-
 Ac-Leu-p-nitroanilide mutant D15A/R18A Aeropyrum pernix K1
3.4.19.1 0.01038
-
 Ac-Leu-p-nitroanilide wild-type Aeropyrum pernix K1

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix K1 Q9YBQ2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.1 using Hi-Trap Q-Sepharose and HiLoad Sephacryl S-200 columns Aeropyrum pernix K1

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 acylpeptide hydrolase
-
 Aeropyrum pernix K1
3.4.19.1 apAPH
-
 Aeropyrum pernix K1
3.4.19.1 APH
-
 Aeropyrum pernix K1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.1 77
-
 mutant DELTAN21 Aeropyrum pernix K1
3.4.19.1 92
-
 mutant D15A above 92° Aeropyrum pernix K1
3.4.19.1 92
-
 mutant R18A above 92° Aeropyrum pernix K1
3.4.19.1 95
-
 wild-type enzyme Aeropyrum pernix K1

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.1 2.04
-
 Ac-Leu-p-nitroanilide wild-type Aeropyrum pernix K1
3.4.19.1 2.1
-
 Ac-Leu-p-nitroanilide mutant R18A Aeropyrum pernix K1
3.4.19.1 2.14
-
 Ac-Leu-p-nitroanilide mutant D15A/R18A Aeropyrum pernix K1
3.4.19.1 2.21
-
 Ac-Leu-p-nitroanilide mutant D15A Aeropyrum pernix K1
3.4.19.1 2.64
-
 Ac-Leu-p-nitroanilide mutant DELTAN21 Aeropyrum pernix K1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.1 8
-
 activity assay Aeropyrum pernix K1