The stereospecificity of the ferrous-ion-dependent alcohol dehydrogenase from Zymomonas mobilis.
Alcohol dehydrogenase from Zymomonas mobilis has been found to transfer the pro-R hydrogen of NADH to acetaldehyde. This is the first report of the stereospecificity of a dehydrogenase in the mechanistic and structural class of Fe2+-dependent alcohol dehydrogenases and offers an opportunity to expand mechanistic hypotheses relating stereospecificity, reaction mechanism and reaction thermodynamics in dehydrogenases.
Glasfeld
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A
Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Benner
S A
SA
D000079:Acetaldehyde / Q000378:metabolism; D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D001421:Bacteria, Anaerobic / Q000201:enzymology; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D007501:Iron / Q000494:pharmacology*; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D013237:Stereoisomerism
D007527:Isoenzymes; D009243:NAD; D007501:Iron; D000426:Alcohol Dehydrogenase; D000079:Acetaldehyde