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.