The stereospecificity of hydrogen transfer to NAD(P)+ catalyzed by lactol dehydrogenases

Biochem Biophys Res Commun. 1997 Apr 28;233(3):681-6. doi: 10.1006/bbrc.1997.6519.

Abstract

The stereochemistry of hydrogen transfer to NAD(P)+ has been determined for five lactol dehydrogenases. It was found that D-glucose dehydrogenases from Bacillus megaterium and Cryptococcus uniguttulatus and L-rhamnose dehydrogenase from Aureobasidium pullulans are pro-S (B) specific, while D-glucose dehydrogenase from Thermoplasma acidophilum and D-xylose dehydrogenase from procine liver are pro-R (A) specific. The latter two enzymes are the first examples of A-specific dehydrogenases oxidizing aldoses at the anomeric carbon. These findings are discussed in terms of functional and historical models that seek to make predictive generalizations regarding dehydrogenase stereospecificity.

MeSH terms

  • Animals
  • Bacillus megaterium / enzymology
  • Carbohydrate Dehydrogenases / metabolism*
  • Cryptococcus / enzymology
  • Hydrogen / metabolism*
  • Liver / enzymology
  • Magnetic Resonance Spectroscopy
  • Mitosporic Fungi / enzymology
  • NAD / chemistry
  • NAD / metabolism*
  • NADP / chemistry
  • NADP / metabolism*
  • Stereoisomerism
  • Substrate Specificity
  • Swine
  • Thermoplasma / enzymology

Substances

  • NAD
  • NADP
  • Hydrogen
  • Carbohydrate Dehydrogenases