Sealy-Lewis H M, Fairhurst V
Department of Applied Biology, University of Hull, UK.
Curr Genet. 1992 Oct;22(4):293-6. doi: 10.1007/BF00317924.
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.
在构巢曲霉中,有一种依赖NADP(+)的甘油脱氢酶,在转移到D-半乳糖醛酸培养基上时会被特异性诱导。与之前表征的组成型依赖NADP(+)的甘油脱氢酶不同,它具有更广泛的底物特异性,具有乙醇脱氢酶活性,并且受到碳分解代谢物阻遏。除了这两种依赖NADP(+)的甘油脱氢酶外,在转移到D-半乳糖醛酸培养基上时也存在醇脱氢酶I和II,它们作为甘油脱氢酶的活性较弱。