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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Bibliographic Details
Published inJournal of Bacteriology Vol. 177; no. 6; pp. 1645 - 1648
Main Authors Graf, R, Dubaquié, Y, Braus, G H
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.03.1995
Subjects
Allosteric Regulation - genetics
Amino acids
Bacteriology
Chorismate Mutase - genetics
Chorismate Mutase - metabolism
Enzymes
isomerasas
isomerase
isomerases
mutacion
Mutagenesis, Site-Directed
mutant
mutantes
mutants
mutation
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Structure-Activity Relationship
Tryptophan - metabolism
Tyrosine - metabolism
Yeast
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Summary: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.
Bibliography:F60
F
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.177.6.1645-1648.1995