Broadening the cofactor specificity of a thermostable alcohol dehydrogenase using rational protein design introduces novel kinetic transient behavior

Biotechnology and Bioengineering

Volumn 107, Issue 5, 2010, Pages 763-774

  Campbell, Elliot ^a   Wheeldon, Ian R ^b,c   Banta, Scott ^a  

^a Columbia University ^*  (United States)

^b BRIGHAM AND WOMEN S HOSPITAL   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Alcohol dehydrogenase; Aldo keto reductase; Cofactor specificity; Enzyme catalysis; Pre steady state kinetics; Site directed mutagenesis; Thermostable

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDO-KETO REDUCTASE; COFACTOR SPECIFICITY; ENZYME CATALYSIS; PRE-STEADY-STATE KINETICS; SITE-DIRECTED MUTAGENESIS; THERMOSTABLE;

AMINO ACIDS; CATALYSIS; ENZYMES; EXPERIMENTS; MUTAGENESIS;

ENZYME ACTIVITY;

ALCOHOL DEHYDROGENASE; ALDO KETO REDUCTASE; ARGININE; MEMBRANE COFACTOR PROTEIN; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SPECIFICITY; HYPERTHERMOPHILE; PROTEIN EXPRESSION; PYROCOCCUS FURIOSUS; SITE DIRECTED MUTAGENESIS;

ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; BINDING SITES; COENZYMES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PYROCOCCUS FURIOSUS;

PYROCOCCUS FURIOSUS;

EID: 77958556843     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22869     Document Type: Article

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