Novel aldo-keto reductases for the biocatalytic conversion of 3- hydroxybutanal to 1,3-butanediol: Structural and biochemical studies

Applied and Environmental Microbiology

Volumn 83, Issue 7, 2017, Pages

  Kim, Taeho ^a   Flick, Robert ^a   Brunzelle, Joseph ^b   Singer, Alex ^a   Evdokimova, Elena ^a   Brown, Greg ^a   Joo, Jeong Chan ^c   Minasov, George A ^b   Anderson, Wayne F ^b   Mahadevan, Radhakrishnan ^a   Savchenko, Alexei ^a   Yakunin, Alexander F ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b NORTHWESTERN UNIVERSITY   (United States)

^c Korea Research Institute of Chemical Technology   (South Korea)

Author keywords

1,3 butanediol; Aldo keto reductase; Biocatalysis; Biotechnology; Crystal structure; Site directed mutagenesis

Indexed keywords

ACETALDEHYDE; ALDEHYDES; BIOCHEMISTRY; BIOTECHNOLOGY; ENZYME ACTIVITY; ENZYMES; MUTAGENESIS; PROTEINS; SALMONELLA; SUBSTRATES;

1,3-BUTANEDIOL; ALDO-KETO REDUCTASE; BIOCATALYSIS; COMPARATIVE STUDIES; PSEUDOMONAS AERUGINOSA; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; SITE DIRECTED MUTAGENESIS; SUBSTRATE SELECTIVITY;

CRYSTAL STRUCTURE;

ALCOHOL; ALDEHYDE; BACTERIUM; BIOACTIVITY; BIOCHEMICAL COMPOSITION; BIOTECHNOLOGY; BIOTRANSFORMATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYME; ENZYME ACTIVITY; MOLECULAR ANALYSIS; MUTATION; POLYMER; PROTEIN;

PSEUDOMONAS AERUGINOSA; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM;

1,3-BUTYLENE GLYCOL; 3-HYDROXYBUTANAL; ALDEHYDE; ALDEHYDE REDUCTASE; BUTANEDIOL; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

BIOCATALYSIS; BIOTECHNOLOGY; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PSEUDOMONAS AERUGINOSA; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; SITE DIRECTED MUTAGENESIS;

ALDEHYDE REDUCTASE; ALDEHYDES; BIOCATALYSIS; BIOTECHNOLOGY; BUTYLENE GLYCOLS; CATALYTIC DOMAIN; CRYSTALLIZATION; MUTAGENESIS, SITE-DIRECTED; NADP; PSEUDOMONAS AERUGINOSA; SALMONELLA TYPHIMURIUM; SUBSTRATE SPECIFICITY;

EID: 85015837417     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03172-16     Document Type: Article

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