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Volumn 499, Issue 1-2, 2010, Pages 1-5
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Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue
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Author keywords
Choline oxidase; Flavoprotein; Hydride transfer; Oxidase; Reductive half reaction; Substrate analogue
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Indexed keywords
3 HYDROXYPROPYL TRIMETHYLAMINE;
ALCOHOL;
ASPARTIC ACID;
CHOLINE OXIDASE;
ENZYME VARIANT;
GLUTAMINE;
HYDROGEN;
TRIMETHYLAMINE;
UNCLASSIFIED DRUG;
ALCOHOL DEHYDROGENASE;
CHOLINE;
DRUG DERIVATIVE;
METHYLAMINE;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME KINETICS;
ENZYME MODIFICATION;
ENZYME SUBSTRATE COMPLEX;
MOLECULAR INTERACTION;
OXIDATION;
PRIORITY JOURNAL;
PROTON TRANSPORT;
STEADY STATE;
AMINO ACID SUBSTITUTION;
ARTHROBACTER;
CHEMISTRY;
ENZYME SPECIFICITY;
ENZYMOLOGY;
GENETIC VARIABILITY;
GENETICS;
KINETICS;
METABOLISM;
PH;
ALCOHOL OXIDOREDUCTASES;
AMINO ACID SUBSTITUTION;
ARTHROBACTER;
CATALYTIC DOMAIN;
CHOLINE;
GENETIC VARIATION;
HYDROGEN-ION CONCENTRATION;
KINETICS;
METHYLAMINES;
SUBSTRATE SPECIFICITY;
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EID: 77953727643
PISSN: 00039861
EISSN: 10960384
Source Type: Journal
DOI: 10.1016/j.abb.2010.04.024 Document Type: Article |
Times cited : (10)
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References (23)
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