Title : Yeast methionine aminopeptidase I. Alteration of substrate specificity by site-directed mutagenesis.

Pub. Date : 1999 May 7

PMID : 10224104






3 Functional Relationships(s)
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1 In eukaryotes, two isozymes (I and II) of methionine aminopeptidase (MetAP) catalyze the removal of the initiator methionine if the penultimate residue has a small radius of gyration (glycine, alanine, serine, threonine, proline, valine, and cysteine). Alanine methionine aminopeptidase Saccharomyces cerevisiae S288C
2 In eukaryotes, two isozymes (I and II) of methionine aminopeptidase (MetAP) catalyze the removal of the initiator methionine if the penultimate residue has a small radius of gyration (glycine, alanine, serine, threonine, proline, valine, and cysteine). Alanine methionine aminopeptidase Saccharomyces cerevisiae S288C
3 Mutation of Gln356 (Gln233 in E. coli MetAP) to alanine results in a catalytic efficiency about one-third that of native with normal substrates but which can cleave methionine from substrates with penultimate histidine, asparagine, glutamine, leucine, methionine, phenylalanine, and tryptophan. Alanine methionine aminopeptidase Saccharomyces cerevisiae S288C