An iron-activated alcohol dehydrogenase.
An alcohol dehydrogenase isolated from Zymomonas mobilis was found to be activated by ferrous ions but not by zinc, after inactivation with metal-complexing agents. Cobaltous ions also re-activated to a lesser extent. It is suggested that in this species the alcohol dehydrogenase naturally contains iron. Kinetic studies on the iron-treated enzyme indicate an 'alcohol activation' phenomenon, which may have physiological relevance in overcoming product inhibition during fermentation.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D003035:Cobalt / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D007501:Iron / Q000494:pharmacology*; D014737:Vibrionaceae / Q000201:enzymology; D015032:Zinc / Q000494:pharmacology
D001426:Bacterial Proteins; D003035:Cobalt; D007501:Iron; D000429:Alcohol Oxidoreductases; D015032:Zinc