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Old Yellow Enzyme‐Catalyzed Dehydrogenation of Saturated Ketones
Author(s) -
Schittmayer Matthias,
Glieder Anton,
Uhl Michael K.,
Winkler Andreas,
Zach Simone,
Schrittwieser Jörg H.,
Kroutil Wolfgang,
Macheroux Peter,
Gruber Karl,
Kambourakis Spiros,
Rozzell J. David,
Winkler Margit
Publication year - 2011
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201000862
Subject(s) - chemistry , dehydrogenation , enzyme , ketone , catalysis , cofactor , nicotinamide , stereochemistry , organic chemistry
Abstract Enzymes from extremophiles have always been of great interest for biotechnology because of their ruggedness against various stress factors. We have isolated, cloned, heterologously expressed and characterized a thermostable old yellow enzyme (OYE) from Geobacillus kaustophilus. In addition to the expected ‘enone’ reduction, Gk OYE also catalyzes the reverse reaction, i.e., the desaturation of CC bonds adjacent to a carbonyl to give the corresponding α,β‐unsaturated ketone. The reaction proceeds at the expense of molecular oxygen without the need for a nicotinamide cofactor and represents an environmentally benign alternative to known chemical dehydrogenation methods.