In:
Advanced Synthesis & Catalysis, Wiley, Vol. 353, No. 2-3 ( 2011-02-11), p. 268-274
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.
Type of Medium:
Online Resource
ISSN:
1615-4150
,
1615-4169
DOI:
10.1002/adsc.v353.2/3
DOI:
10.1002/adsc.201000862
Language:
English
Publisher:
Wiley
Publication Date:
2011
detail.hit.zdb_id:
2041384-1
detail.hit.zdb_id:
2033084-4
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