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. 1982 Jul;151(1):243-50.
doi: 10.1128/jb.151.1.243-250.1982.

Purification and characterization of mannitol dehydrogenase from Aspergillus parasiticus

W G Niehaus Jr, R P Dilts Jr

Purification and characterization of mannitol dehydrogenase from Aspergillus parasiticus

W G Niehaus Jr et al. J Bacteriol. 1982 Jul.

Abstract

Mannitol dehydrogenase, NADP specific (EC 1.1.1.138), was purified from mycelium of Aspergillus parasiticus (1-11-105 Whl). The enzyme had a molecular weight of 1.4 X 10(5) and was composed of four 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. Zinc ion was a powerful inhibitor of the enzyme, inhibition being competitive with respect to mannitol, with Ki and 1 microM. It is proposed that the stimulation of polyketide synthesis by zinc ion may be mediated in part by inhibition of mannitol dehydrogenase.

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