| Literature DB >> 19383697 |
Xueqian Liu1,2,3, Yanpeng Dong1,2,3, Jing Zhang1,2,3, Aixiang Zhang1,2,3, Lei Wang3,4,5,1,2, Lu Feng4,5,1,2,3.
Abstract
Two alkyl alcohol dehydrogenase (ADH) genes from the long-chain alkane-degrading strain Geobacillus thermodenitrificans NG80-2 were characterized in vitro. ADH1 and ADH2 were prepared heterologously in Escherichia coli as a homooctameric and a homodimeric protein, respectively. Both ADHs can oxidize a broad range of alkyl alcohols up to at least C(30), as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is ethanol for ADH1 and 1-octanol for ADH2. For both ADHs, the optimum assay condition is at 60 degrees C and pH 8.0, and both NAD and NADP can be used as the cofactor. Sequence analysis reveals that ADH1 and ADH2 belong to the Fe-containing/activated long-chain ADHs. However, the two enzymes contain neither Fe nor other metals, and Fe is not required for the activity, suggesting a new type of ADH. The ADHs characterized here are potentially useful in crude oil bioremediation and other bioconversion processes.Entities:
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Year: 2009 PMID： 19383697 DOI： 10.1099/mic.0.027201-0
Source DB: PubMed Journal: Microbiology ISSN： 1350-0872 Impact factor: 2.777