Type of Publication: | Journal article |
Publication status: | Published |
URI (citable link): | http://nbn-resolving.de/urn:nbn:de:bsz:352-0-383757 |
Author: | Frey, Jasmin; Rusche, Hendrik; Schink, Bernhard; Schleheck, David |
Year of publication: | 2016 |
Published in: | BMC Microbiology ; 16 (2016). - 280. - eISSN 1471-2180 |
Pubmed ID: | 27884109 |
DOI (citable link): | https://dx.doi.org/10.1186/s12866-016-0899-9 |
Summary: |
Background
The strictly anaerobic, sulfate-reducing bacterium Desulfococcus biacutus can utilize acetone as sole carbon and energy source for growth. Whereas in aerobic and nitrate-reducing bacteria acetone is activated by carboxylation with CO2 to acetoacetate, D. biacutus involves CO as a cosubstrate for acetone activation through a different, so far unknown pathway. Proteomic studies indicated that, among others, a predicted medium-chain dehydrogenase/reductase (MDR) superfamily, zinc-dependent alcohol dehydrogenase (locus tag DebiaDRAFT_04514) is specifically and highly produced during growth with acetone. Results The MDR gene DebiaDRAFT_04514 was cloned and overexpressed in E. coli. The purified recombinant protein required zinc as cofactor, and accepted NADH/NAD+ but not NADPH/NADP+ as electron donor/acceptor. The pH optimum was at pH 8, and the temperature optimum at 45 °C. Highest specific activities were observed for reduction of C3 - C5-aldehydes with NADH, such as propanal to propanol (380 ± 15 mU mg−1 protein), butanal to butanol (300 ± 24 mU mg−1), and 3-hydroxybutanal to 1,3-butanediol (248 ± 60 mU mg−1), however, the enzyme also oxidized 3-hydroxybutanal with NAD+ to acetoacetaldehyde (83 ± 18 mU mg−1). Conclusion The enzyme might play a key role in acetone degradation by D. biacutus, for example as a bifunctional 3-hydroxybutanal dehydrogenase/reductase. Its recombinant production may represent an important step in the elucidation of the complete degradation pathway. |
Subject (DDC): | 570 Biosciences, Biology |
Keywords: | Acetone activation; Sulfate-reducing bacteria; Carbonylation; Bifunctional MDR superfamily oxidoreductase |
Link to License: | In Copyright |
Bibliography of Konstanz: | Yes |
FREY, Jasmin, Hendrik RUSCHE, Bernhard SCHINK, David SCHLEHECK, 2016. Cloning, functional expression and characterization of a bifunctional 3-hydroxybutanal dehydrogenase /reductase involved in acetone metabolism by Desulfococcus biacutus. In: BMC Microbiology. 16, 280. eISSN 1471-2180. Available under: doi: 10.1186/s12866-016-0899-9
@article{Frey2016-12Cloni-37677, title={Cloning, functional expression and characterization of a bifunctional 3-hydroxybutanal dehydrogenase /reductase involved in acetone metabolism by Desulfococcus biacutus}, year={2016}, doi={10.1186/s12866-016-0899-9}, volume={16}, journal={BMC Microbiology}, author={Frey, Jasmin and Rusche, Hendrik and Schink, Bernhard and Schleheck, David}, note={Article Number: 280} }
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