Fine tuning of coenzyme specificity in family 2 aldo-keto reductases revealed by crystal structures of the Lys-274 → Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+ and NADP+

FEBS Letters

Volumn 579, Issue 3, 2005, Pages 763-767

  Leitgeb, Stefan ^a,b   Petschacher, Barbara ^a   Wilson, David K ^b   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Dual coenzyme specificity; Loop ordering; Selectivity; Xylose fermentation

Indexed keywords

2 ALDO KETO REDUCTASE; ARGININE; GLUTAMIC ACID 227; GLUTAMIC ACID DERIVATIVE; HYDROXYL GROUP; LYSINE 274; LYSINE DERIVATIVE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHOSPHATE; UNCLASSIFIED DRUG; WATER; XYLOSE;

AMINO ACID SEQUENCE; ARTICLE; CANDIDA; CATALYSIS; COENZYME; COMPARATIVE STUDY; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ALCOHOL OXIDOREDUCTASES; ARGININE; CANDIDA; COENZYMES; CRYSTALLOGRAPHY, X-RAY; KINETICS; LYSINE; NAD; NADP; PROTEIN CONFORMATION;

CANDIDA; CANDIDA TENUIS;

EID: 12844288097     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.063     Document Type: Article

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