Summary: Glycerol dehydrogenase, NADP-specific (EC, was purified from mycelium of and using different purification procedures. Both enzymes had an 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 enzyme had a turnover number twice that of the enzyme at pH 6.0, whereas inhibition by NADP was less ( = 45 μM vs 13 μM). It is proposed that both enzymes catalyse the reduction of DHA to glycerol and that they are regulated by the anabolic reduction charge.


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