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Literature summary for 3.4.11.18 extracted from

  • Mitra, S.; Bennett, B.; Holz, R.C.
    Mutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli (2009), Biochim. Biophys. Acta, 1794, 137-143.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
mutant H63A is expressed in Escherichia coli BL21 Star(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
H63A the mutation does not affect the ability of the enzyme to bind divalent metal ions but affects the hydrolysis of small peptide substrates whereas large peptides can overcome the observed loss in binding energy by additional hydrophilic and hydrophobic interactions Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
1
-
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
3
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
3.1
-
L-Met-Gly-L-Met-L-Met mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
12
-
L-Met-L-Ala-L-Ser wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
15
-
L-Met-L-Ala-L-Ser mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the kcat value increases as a function of Co2+ ion concentration and exhibits a maximum after the addition of one equivalent of Co2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29630
-
SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Met-Gly-L-Met-L-Met + H2O
-
Escherichia coli L-Met + Gly-L-Met-L-Met
-
?
L-Met-L-Ala-L-Ser + H2O
-
Escherichia coli L-Met + L-Ala-L-Ser
-
?
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp + H2O
-
Escherichia coli L-Met + L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
?

Synonyms

Synonyms Comment Organism
MetAP-I
-
Escherichia coli
methionine aminopeptidase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3
-
L-Met-L-Ala-L-Ser mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
4.8
-
L-Met-Gly-L-Met-L-Met mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
11
-
L-Met-L-Ala-L-Ser wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
18.3
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
70
-
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli
84
-
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C Escherichia coli