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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 enzy...

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Bibliografiska uppgifter
Huvudupphovsmän: Graf, R, Dubaquié, Y, Braus, G H
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1995
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Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC176788/
https://ncbi.nlm.nih.gov/pubmed/7883726
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