| Literature DB >> 7883726 |
R Graf1, Y Dubaquié, G H Braus.
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.Entities:
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Year: 1995 PMID: 7883726 PMCID: PMC176788 DOI: 10.1128/jb.177.6.1645-1648.1995
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490