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J. Bacteriol., 03 1995, 1645-1648, Vol 177, No. 6
Copyright © 1995, American Society for Microbiology

Modulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue

R Graf, Y Dubaquie and GH Braus
Institut fur Mikrobiologie, Biochemie & Genetik, Friedrich-Alexander Universitat, Erlangen-Nurnberg, Germany.

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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