PMID: 7085559Jul 1, 1982Paper

Purification and characterization of mannitol dehydrogenase from Aspergillus parasiticus

Journal of Bacteriology
W G Niehaus, R P Dilts


Mannitol dehydrogenase, NADP specific (EC, 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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Related Concepts

Mannitol Dehydrogenase (Cytochrome)
Substrate Specificity

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