Purification and characterization of mannitol dehydrogenase from Aspergillus parasiticus

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Abstract
Mannitol dehydrogenase, NADP specific (EC 1.1.1.138), was purified from mycelium of A. parasiticus (1-11-105 Whl). The enzyme had a MW of 1.4 .times. 105 and was composed of 4 subunits of apparently equal size. The substrate specificity was limited to D-mannitol, D-glucitol, D-arabinitol, 1-deoxy-D-mannitol and 1-deoxy-D-glucitol. Zn2+ was a powerful inhibitor of the enzyme, inhibition being competitive with respect to mannitol with Ki .apprx. 1 .mu.M. Evidently, the stimulation of polyketide synthesis by Zn2+ may be mediated in part by inhibition of mannitol dehydrogenase.