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Literature summary for 3.4.11.18 extracted from

  • Walker, K.W.; Bradshaw, R.A.
    Yeast methionine aminopeptidase I. Alteration of substrate specificity by site-directed mutagenesis (1999), J. Biol. Chem., 274, 13403-13409.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
M329A mutation produces an avarage catalytic efficiency 1.5fold higher than the native enzyme on normal substrates and cleaves substrates containing penultimate Asn, Gln, Ile, Leu, Met and Phe Saccharomyces cerevisiae
S195A mutation has no effect on substrate specificity Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
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Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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methionine aminopeptidase 1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Met-Ala-Ser-His-Arg-Trp-Asp-Trp + H2O
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Saccharomyces cerevisiae Met + Ala-Ser-His-Arg-Trp-Asp-Trp
-
?
Met-Gly-Ser-His-Arg-Trp-Asp-Trp + H2O
-
Saccharomyces cerevisiae Met + Gly-Ser-His-Arg-Trp-Asp-Trp
-
?
Met-Pro-Ser-His-Arg-Trp-Asp-Trp + H2O
-
Saccharomyces cerevisiae Met + Pro-Ser-His-Arg-Trp-Asp-Trp
-
?
Met-Ser-Ser-His-Arg-Trp-Asp-Trp + H2O
-
Saccharomyces cerevisiae Met + Ser-Ser-His-Arg-Trp-Asp-Trp
-
?
Met-Thr-Ser-His-Arg-Trp-Asp-Trp + H2O
-
Saccharomyces cerevisiae Met + Thr-Ser-His-Arg-Trp-Asp-Trp
-
?
Met-Val-Ser-His-Arg-Trp-Asp-Trp + H2O
-
Saccharomyces cerevisiae Met + Val-Ser-His-Arg-Trp-Asp-Trp
-
?
additional information removal of the initiator methionine if the penultimate residue has a small radius of gyration (Gly, Ala, Ser, Thr, Pro, Val and Cys) Saccharomyces cerevisiae ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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additional information
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Saccharomyces cerevisiae