Stereospecificity of hydrogen transfer by the NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.
Investigation of the stereochemistry of the hydride transfer in reactions catalyzed by the recently isolated NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123 was accomplished by using 1H NMR spectroscopy of the deuterated coenzyme. It was found that this new psychrophilic enzyme is a type A dehydrogenase. Moraxella sp. ADH reduces stereospecifically 2-butanone to produce (S)-2-butanol.
Velonia
K
K
Department of Chemistry, University of Crete, Greece.
Tsigos
I
I
Bouriotis
V
V
Smonou
I
I
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism*; D000864:Antarctic Regions; D000440:Butanols / Q000737:chemistry / Q000378:metabolism; D002074:Butanones / Q000737:chemistry / Q000378:metabolism; D003067:Coenzymes / Q000737:chemistry / Q000378:metabolism; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D009016:Moraxella / Q000201:enzymology*; D009243:NAD / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity