PMID: 7085559Jul 1, 1982Paper

Purification and characterization of mannitol dehydrogenase from Aspergillus parasiticus

Journal of Bacteriology
W G Niehaus, R P Dilts

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.

Citations

Jan 1, 1993·The Journal of Applied Bacteriology·R H Luchese, W F Harrigan
Jan 27, 2000·Medical Mycology·A J Hamilton, M D Holdom
Feb 24, 2011·Phytopathology·Brittiney N ReeseCharles P Woloshuk
Jan 10, 1989·Biotechnology and Bioengineering·R N Pike, C Dennison
Feb 1, 1986·The Journal of Applied Bacteriology·R K BhatnagarT A Subramanian
Apr 13, 2006·The Journal of Biological Chemistry·Birgit Simon-NobbeMichael Breitenbach
Aug 7, 2003·Applied and Environmental Microbiology·Jung-Kul LeeHyung-Hwan Hyun
May 26, 2001·Applied and Environmental Microbiology·H HajjajP Duboc
Nov 11, 2010·Applied Microbiology and Biotechnology·Badal C Saha, F Michael Racine
Oct 6, 1998·Applied and Environmental Microbiology·B H Liu, F S Chu
Jan 7, 1998·Protein Expression and Purification·C Dennison, R Lovrien

Related Concepts

Aspergillus
Mannitol Dehydrogenase (Cytochrome)
Osmolality
Substrate Specificity
Zinc

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