Abstract
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.
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