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.
Králová
B
B
Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague, Czech Republic. blanka.kralova@vscht.cz
Valentová
O
O
Demnerová
K
K
Silhánková
L
L
D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D009243:NAD / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D004718:Saccharomycetales / Q000201:enzymology*
D005656:Fungal Proteins; D007527:Isoenzymes; D009243:NAD; D009249:NADP; D005954:Glucosephosphate Dehydrogenase