Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2

Microbiology (Reading). 2009 Jun;155(Pt 6):2078-2085. doi: 10.1099/mic.0.027201-0. Epub 2009 Apr 21.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / isolation & purification
  • Alcohol Oxidoreductases / metabolism*
  • Alcohols / metabolism
  • Amino Acid Sequence
  • Bacillaceae / drug effects
  • Bacillaceae / enzymology*
  • Bacillaceae / genetics
  • Biodegradation, Environmental
  • Chelating Agents / pharmacology
  • DNA, Bacterial / analysis
  • DNA, Bacterial / genetics
  • Edetic Acid / pharmacology
  • Iron / metabolism
  • Molecular Sequence Data
  • NAD / metabolism
  • NADP / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / isolation & purification
  • Sequence Analysis
  • Substrate Specificity


  • Alcohols
  • Chelating Agents
  • DNA, Bacterial
  • Recombinant Proteins
  • NAD
  • NADP
  • Edetic Acid
  • Iron
  • Alcohol Oxidoreductases
  • long-chain-alcohol dehydrogenase