Substitutions at the cofactor phosphate-binding site of a clostridial alcohol dehydrogenase lead to unexpected changes in substrate specificity

Protein Engineering, Design and Selection

Volumn 28, Issue 8, 2015, Pages 251-258

  Maddock, Danielle J ^a   Patrick, Wayne M ^a   Gerth, Monica L ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

Alcohol dehydrogenase; Clostridium autoethanogenum; Cofactor specificity; Enzyme engineering; Mutagenesis

Indexed keywords

ALCOHOL FUELS; CLOSTRIDIUM; ENZYMES; METABOLIC ENGINEERING; MUTAGENESIS;

ALCOHOL DEHYDROGENASE; CLOSTRIDIUM AUTOETHANOGENUM; COFACTOR SPECIFICITY; CONCOMITANT REDUCTION; ENZYME ENGINEERING; NICOTINAMIDE ADENINE DINUCLEOTIDES; SECONDARY ALCOHOL DEHYDROGENASE; SITE DIRECTED MUTAGENESIS;

BIOCHEMICAL ENGINEERING;

ACETONE; ALCOHOL DEHYDROGENASE; FUEL; PETROCHEMICAL AGENT; PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; BACTERIAL PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CLOSTRIDIUM; CLOSTRIDIUM AUTOETHANOGENUM; CLOSTRIDIUM BEIJERINCKII; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENETIC VARIABILITY; HIGH THROUGHPUT SCREENING; HYDROGEN BOND; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STEADY STATE; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ENZYMOLOGY; GENETICS;

ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CLOSTRIDIUM; SUBSTRATE SPECIFICITY;

EID: 84943253884     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzv028     Document Type: Article

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