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Literature summary for 3.4.11.18 extracted from

  • Klinkenberg, M.; Ling, C.; Chang, Y.H.
    A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2 (1997), Arch. Biochem. Biophys., 347, 193-200.
    View publication on PubMed
Search for more literature for 3.4.11.18

Protein Variants

Protein Variants Comment Organism
D219N the mutant enzyme has 1000fold lower activity and a different substrate specificity when compared to wild-type enzyme. Expression of the mutant enzyme in yeast causes a slow-growth phenotype and interferes with wild-type metAP1 in a dominant manner. The mutant enzyme contains 0.43 mol of Co2+ per mol. The wild-type enzyme contains 0.75 mol of Co2+ per mol of enzyme. The mutant enzyme prefers substrates, having Ser or Pro at P1', over substrates that contain glycine and alanine at that position. The wild-type enzyme prefers substrates that have Ala, Gly, Ser or Pro at P1' Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.54
-
 Met-Ala-Ser pH 7.4, 37°C mutant enzyme D219N Saccharomyces cerevisiae
13.9
-
 Met-Gly-Met-Met pH 7.4, 37°C mutant enzyme D219N Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the mutant enzyme contains 0.43 mol of Co2+ per mol. The wild-type enzyme contains 0.75 mol of Co2+ per mol of enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 x * 43000, mutant enzyme D219N, SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 methionine aminopeptidase 1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Ala-Ser + H2O
-
 Saccharomyces cerevisiae Met + Ala-Ser
-
 ?
Met-Gly-Met-Met + H2O
-
 Saccharomyces cerevisiae Met + Gly-Met-Met
-
 ?
Met-Pro-Gly + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
Met-Ser-Gly + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
additional information the mutant enzyme prefers substrates, having Ser or Pro at P1', over substrates that contain glycine and alanine at that position. The wild-type enzyme prefers substrates that have Ala, Gly, Ser or Pro at P1'. Amino-terminal Met cannot be removed by either the mutant or wild-type enzyme from substrates having large and charged amino acids at P1' position Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
? x * 43000, mutant enzyme D219N, SDS-PAGE Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00325
-
 Met-Ala-Ser pH 7.4, 37°C mutant enzyme D219N Saccharomyces cerevisiae
0.0427
-
 Met-Gly-Met-Met pH 7.4, 37°C mutant enzyme D219N Saccharomyces cerevisiae