Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones

Biological Chemistry

Volumn 398, Issue 1, 2017, Pages 31-37

  Peters, Christin ^a   Rudroff, Florian ^b   Mihovilovic, Marko D ^b   Bornscheuer, Uwe T ^a  

^a UNIVERSITY OF GREIFSWALD   (Germany)

^b VIENNA UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

alcohol dehydrogenase; Baeyer Villiger monooxygenase; biocatalysis; enoate reductase; enzyme cascade; fusion proteins

Indexed keywords

ALCOHOL DEHYDROGENASE ENOATE REDUCTASE BAEYER VILLINGER MONOOXYGENASE FUSION PROTEIN; HYBRID PROTEIN; UNCLASSIFIED DRUG; LACTONE; MIXED FUNCTION OXIDASE; OXIDOREDUCTASE;

ACINETOBACTER; AMINO TERMINAL SEQUENCE; ARTICLE; BIOCATALYSIS; CARBOXY TERMINAL SEQUENCE; CHIRALITY; ENANTIOSELECTIVITY; ENZYME ACTIVITY; MOLECULAR WEIGHT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PSEUDOMONAS PUTIDA; SUBSTRATE CONCENTRATION; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; RHODOCOCCUS; STEREOISOMERISM;

BIOCATALYSIS; LACTONES; MIXED FUNCTION OXYGENASES; OXIDOREDUCTASES; RECOMBINANT FUSION PROTEINS; RHODOCOCCUS; STEREOISOMERISM;

EID: 85002647242     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2016-0150     Document Type: Article

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