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Literature summary for 3.4.11.18 extracted from

  • Watterson, S.J.; Mitra, S.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
    Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli (2008), Biochemistry, 47, 11885-11893.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H79A Co2+-loaded H79A exhibits an overall of more than 7000fold decrease in specific activity, the almost complete loss of activity is primarily due to a more than 6000fold decrease in kcat, the Km value obtained for Co2+-loaded H79A is approximately half the value observed for wild type MetAP-I, specific activity of Mn2+-loaded H79A decreases by about 2.6fold while kcat decreases by about 3.5fold, the observed Km value for Mn2+ loaded H79A is about 1.4fold larger than that observed for wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Mn2+ Escherichia coli
1.5
-
L-Met-Gly-L-Met-L-Met mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli
1.8
-
L-Met-Gly-L-Met-L-Met mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli
3.2
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
Escherichia coli
Mn2+
-
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
-
?

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
0.003
-
L-Met-Gly-L-Met-L-Met mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli
1.8
-
L-Met-Gly-L-Met-L-Met mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli
4.6
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Mn2+ Escherichia coli
18.3
-
L-Met-Gly-L-Met-L-Met wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+ Escherichia coli