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

@article{Walker1999YeastMA,
  title={Yeast methionine aminopeptidase I. Alteration of substrate specificity by site-directed mutagenesis.},
  author={Kevin C. Walker and Ralph A. Bradshaw},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 19},
  pages={
          13403-9
        }
}
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). Using site-directed mutagenesis, recombinant yeast MetAP I derivatives that are able to cleave N-terminal methionine from substrates that have larger penultimate residues have been expressed. A Met to Ala change at 329 (Met206 in Escherichia coli… CONTINUE READING
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