NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae.

@article{Wales1994NADPdependentAD,
  title={NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae.},
  author={Martin R. Wales and Charles A. Fewson},
  journal={Microbiology},
  year={1994},
  volume={140 ( Pt 1)},
  pages={
          173-83
        }
}
An NADP-dependent constitutive alcohol dehydrogenase that can oxidize hexan-1-ol was detected in several Gram-positive and Gram-negative eubacteria and in two yeasts. The enzyme was purified to homogeneity from Acinetobacter calcoaceticus NCIB 8250 and from Saccharomyces cerevisiae D273-10B. The bacterial enzyme appears to be a tetramer of subunit M(r) 40,300 and the yeast enzyme appears to be a monomer of subunit M(r) 43,500. The N-terminal amino acid sequence of the bacterial enzyme has 34… CONTINUE READING

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