Abstract
A NAD-dependent, oxygen-labile alcohol dehydrogenase was purified from Desulfovibrio gigas. It was decameric, with subunits of M(r) 43,000. The best substrates were ethanol (K(m), 0.15 mM) and 1-propanol (K(m), 0.28 mM). N-terminal amino acid sequence analysis showed that the enzyme belongs to the same family of alcohol dehydrogenases as Zymomonas mobilis ADH2 and Bacillus methanolicus MDH.
Original language | English |
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Pages (from-to) | 2859-2863 |
Number of pages | 5 |
Journal | Journal of Bacteriology |
Volume | 175 |
Issue number | 10 |
Publication status | Published - May-1993 |
Keywords
- SULFATE-REDUCING BACTERIA
- ZYMOMONAS-MOBILIS
- SACCHAROMYCES-CEREVISIAE
- ESCHERICHIA-COLI
- SP-NOV
- GENE
- IRON
- SEQUENCE
- PROTEIN
- ETHANOL