Modulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue.
Chorismate mutase (EC 5.4.99.5) from the yeast Saccharomyces cerevisiae is an allosteric enzyme which can be locked in its active R (relaxed) state by a single threonine-to-isoleucine exchange at position 226. Seven new replacements of residue 226 reveal that this position is able to direct the enzyme's allosteric equilibrium, without interfering with the catalytic constant or the affinity for the activator.
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Institut für Mikrobiologie, Biochemie & Genetik, Friedrich-Alexander Universität, Erlangen-Nürnberg, Germany.
Dubaquié
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Braus
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D000494:Allosteric Regulation / Q000235:genetics; D002826:Chorismate Mutase / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D013329:Structure-Activity Relationship; D014364:Tryptophan / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D014443:Tyrosine; D014364:Tryptophan; D002826:Chorismate Mutase