Modulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue-Reference-Cited by-同舟云学术

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

Published:1995-03 Issue:6 Volume:177 Page:1645-1648
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Graf R¹,Dubaquié Y¹,Braus G H¹

Affiliation:

1. Institut für Mikrobiologie, Biochemie & Genetik, Friedrich-Alexander Universität, Erlangen-Nürnberg, Germany.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.177.6.1645-1648.1995

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