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Applied and Environmental Microbiology, July 1999, p. 3244-3247, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of Methylglyoxal Synthase from Clostridium acetobutylicum ATCC 824 and Its Use in the Formation of 1,2-Propanediol

Ke-xue Huang, Frederick B. Rudolph, and George N. Bennett*

Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892

Received 15 December 1998/Accepted 30 April 1999

A gene encoding a putative 150-amino-acid methylglyoxal synthase was identified in Clostridium acetobutylicum ATCC 824. The enzyme was overexpressed in Escherichia coli and purified. Methylglyoxal synthase has a native molecular mass of 60 kDa and an optimum pH of 7.5. The Km and Vmax values for the substrate dihydroxyacetone phosphate were 0.53 mM and 1.56 mmol min-1 µg-1, respectively. When E. coli glycerol dehydrogenase was coexpressed with methylglyoxal synthase in E. coli BL21(DE3), 3.9 mM 1,2-propanediol was produced.

* Corresponding author. Mailing address: Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, TX 77005-1892. Phone: (713) 527-4920. Fax: (713) 285-5154. E-mail: gbennett{at}bioc.rice.edu.

Applied and Environmental Microbiology, July 1999, p. 3244-3247, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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