Dipodascus magnusii (Saccharomycetes) contains multiple glucose-6-phosphate dehydrogenases with different NAD+/NADP+ dependencies.

A cell-free extract of a morphologically unstable strain of Dipodascus magnusii contained six proteins with activity of glucose-6-phosphate dehydrogenase (G6PDH). Two of these proteins displayed only NADP + -dependent activity, two could utilize both NAD + and NADP + , but had higher activity with NAD + , and two possessed only NAD + -dependent activity. When the cultivation was carried out in the presence of monoiodoacetic acid, only two proteins with G6PDH activity were produced, one of them NAD + -dependent and the other NADP + -dependent. In all cases, NAD + -dependent activity was less stable in the presence of proteinases than was the NADP + -dependent activity.