Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus.
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.
Trincone
A
A
Istituto per la Chimica di Molecole di Interesse Biologico CNR, Naples, Italy.
Lama
L
L
Rella
R
R
D'Auria
S
S
Raia
C A
CA
Nicolaus
B
B
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
D009243:NAD; D000426:Alcohol Dehydrogenase