An NADP(+)-dependent glycerol dehydrogenase in Aspergillus nidulans is inducible by D-galacturonate.
In Aspergillus nidulans there is an NADP(+)-dependent glycerol dehydrogenase that is specifically induced on transfer to D-galacturonate medium. In contrast to the previously characterised constitutive NADP(+)-dependent glycerol dehydrogenase it has a much broader substrate specificity, having activity as an ethanol dehydrogenase, and is subject to carbon-catabolite repression. In addition to the two NADP(+)-dependent glycerol dehydrogenases, alcohol dehydrogenase I and II are also present on transfer to D-galacturonate medium, and have weak activity as glycerol dehydrogenases.
Sealy-Lewis
H M
HM
Department of Applied Biology, University of Hull, UK.
Fairhurst
V
V
D000426:Alcohol Dehydrogenase / Q000235:genetics; D001233:Aspergillus nidulans / Q000201:enzymology* / Q000235:genetics; D004790:Enzyme Induction; D015966:Gene Expression Regulation, Fungal; D006603:Hexuronic Acids / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000235:genetics* / Q000378:metabolism
D006603:Hexuronic Acids; C007819:galacturonic acid; D009249:NADP; D013401:Sugar Alcohol Dehydrogenases; D000426:Alcohol Dehydrogenase; C020672:glycerol dehydrogenase