RT Journal Article SR Electronic(1) A1 Schuurink, R. A1 Busink, R. A1 Hondmann, D. H. A. A1 Wltteveen, C. F. B. A1 Vlsser, J.YR 1990 T1 Purification and properties of NADP+-dependent glycerol dehydrogenases from Aspergillus nidulans and A. niger JF Microbiology, VO 136 IS 6 SP 1043 OP 1050 DO https://doi.org/10.1099/00221287-136-6-1043 PB Microbiology Society, SN 1465-2080, AB Glycerol dehydrogenase, NADP+-specific (EC 1.1.1.72), was purified from mycelium of Aspergillus nidulans and Aspergillus niger using different purification procedures. Both enzymes had an M r of approximately 38000 and were immunologically cross-reactive, but had different amino acid compositions and isoelectric points. For both enzymes, the substrate specificity was limited to glycerol and erythritol for the oxidative reaction and to dihydroxyacetone (DHA), diacetyl, methylglyoxal, erythrose and d-glyceraldehyde for the reductive reaction. The A. nidulans enzyme had a turnover number twice that of the A. niger enzyme at pH 6·0, whereas inhibition by NADP+ was less (K i = 45 µm vs 13 µm). It is proposed that both enzymes catalyse in vivo the reduction of DHA to glycerol and that they are regulated by the anabolic reduction charge., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-136-6-1043