Document Detail

Characterization of an aldo-keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum.
MedLine Citation:
PMID:  23338701     Owner:  NLM     Status:  MEDLINE    
A novel aldo-keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %.
Yuan-Hui Ma; Dan-Qing Lv; Shuo Zhou; Dun-Yue Lai; Zhen-Ming Chen
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-22
Journal Detail:
Title:  Biotechnology letters     Volume:  35     ISSN:  1573-6776     ISO Abbreviation:  Biotechnol. Lett.     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-05-02     Completed Date:  2013-10-31     Revised Date:  2014-03-18    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  757-62     Citation Subset:  IM    
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MeSH Terms
Alcohol Oxidoreductases / chemistry*,  metabolism*
Enzyme Stability
Substrate Specificity
Thermotoga maritima / enzymology*
Reg. No./Substance:
EC 1.1.-/Alcohol Oxidoreductases; EC reductase (NADPH)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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