title: Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus.
abstract: This paper describes the determination of stereospecificity of hydride transfer reaction of an alcohol dehydrogenase isolated from the archaebacterium Sulfolobus solfataricus. The 1H-NMR and EI-MS data indicate that the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase.
authors.affiliation: Istituto per la Chimica di Molecole di Interesse Biologico CNR, Naples, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Trincone
authors.forename: L
authors.initials: L
authors.lastname: Lama
authors.forename: R
authors.initials: R
authors.lastname: Rella
authors.forename: S
authors.initials: S
authors.lastname: D'Auria
authors.forename: C A
authors.initials: CA
authors.lastname: Raia
authors.forename: B
authors.initials: B
authors.lastname: Nicolaus
mesh_terms: D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D001105:Archaea / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D009243:NAD; D000426:Alcohol Dehydrogenase