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Literature summary for 3.4.11.18 extracted from

  • Copik, A.J.; Swierczek, S.I.; Lowther, W.T.; D'Souza, V.M.; Matthews, B.W.; Holz, R.C.
    Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli (2003), Biochemistry, 42, 6283-6292.
    View publication on PubMed
Search for more literature for 3.4.11.18

Protein Variants

Protein Variants Comment Organism
H178A the mutant enzyme binds only one equivalent of Co(II) or Fe(II) tightly with affinities that are identical to the wild-type. The turnover-number for Co(II) loaded H178A decreases 70fold towards Met-Gly-Met-Met ans 290fold towards Met-Pro-p-nitroanilide. The KM-value for Met-Gly-Met-Met remains unaffected, while that for Met-Pro-p-nitroanilide increases approximately 2fold for Co(II) - and Fe(II)-loaded H178A. The ratio of turnover-number to Km-value for both Co(II)- and Fe(II)-loaded H178A towards both substrates ranges from 50fold to 580fold reduction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 Met-Pro-4-nitroanilide wild-type enzyme, Co(II) loaded, pH 7.5 Escherichia coli
0.09
-
 Met-Pro-4-nitroanilide wild-type enzyme, Fe(II) loaded, pH 7.5 Escherichia coli
0.12
-
 Met-Pro-4-nitroanilide mutant enzyme H178A, Co(II) loaded, pH 7.5 Escherichia coli
0.13
-
 Met-Pro-4-nitroanilide mutant enzyme H178A, Fe(II) loaded, pH 7.5 Escherichia coli
2
-
 Met-Gly-Met-Met wild-type enzyme and mutant enzyme H178A, Fe(II) loaded, pH 7.5 Escherichia coli
3.2
-
 Met-Gly-Met-Met wild-type enzyme and mutant enzyme H178A, Co(II) loaded, pH 7.5 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Gly-Met-Met + H2O
-
 Escherichia coli Gly-Met-Met + Met
-
 ?
Met-Pro-4-nitroanilide + H2O
-
 Escherichia coli Met + Pro-4-nitroanilide
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.002
-
 Met-Pro-p-nitroanilide mutant enzyme H178A, Co(II) loaded, pH 7.5 Escherichia coli
0.01
-
 Met-Pro-p-nitroanilide mutant enzyme H178A, Fe(II) loaded, pH 7.5 Escherichia coli
0.54
-
 Met-Gly-Met-Met mutant enzyme H178A, Co(II) loaded, pH 7.5 Escherichia coli
0.56
-
 Met-Gly-Met-Met mutant enzyme H178A, Fe(II) loaded, pH 7.5 Escherichia coli
0.59
-
 Met-Pro-p-nitroanilide wild-type enzyme, Co(II) loaded, pH 7.5 Escherichia coli
1.4
-
 Met-Pro-p-nitroanilide wild-type enzyme, Fe(II) loaded, pH 7.5 Escherichia coli
28
-
 Met-Gly-Met-Met wild-type enzyme, Fe(II) loaded, pH 7.5 Escherichia coli
39
-
 Met-Gly-Met-Met wild-type enzyme, Co(II) loaded, pH 7.5 Escherichia coli