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Volumn 41, Issue 19, 2002, Pages 6164-6169
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Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity
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Author keywords
[No Author keywords available]
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Indexed keywords
KINETIC PROPERTIES;
AMINO ACIDS;
DIMERS;
ENZYMES;
ION EXCHANGE;
PH EFFECTS;
YEAST;
DIMER;
HYBRID PROTEIN;
HYDROXIDE;
PYRUVATE DECARBOXYLASE;
TETRAMER;
UREA;
AMINO ACID SEQUENCE;
ARTICLE;
CONTROLLED STUDY;
DISSOCIATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME KINETICS;
ENZYME MECHANISM;
ENZYME STRUCTURE;
ION EXCHANGE;
NONHUMAN;
PH;
PHENOTYPE;
PRIORITY JOURNAL;
YEAST;
AMINO ACID SUBSTITUTION;
CATALYTIC DOMAIN;
CHROMATOGRAPHY, ION EXCHANGE;
DIMERIZATION;
HYDROGEN-ION CONCENTRATION;
KINETICS;
PROTEIN STRUCTURE, QUATERNARY;
PROTEIN SUBUNITS;
PYRUVATE DECARBOXYLASE;
SACCHAROMYCES CEREVISIAE;
VARIATION (GENETICS);
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EID: 0037076534
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0121712 Document Type: Article |
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Times cited : (6)
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References (17)
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