Abstract
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 K(m) and V(max) 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.
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CITATION STYLE
Huang, K. X., Rudolph, F. B., & Bennett, G. N. (1999). Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1,2-propanediol. Applied and Environmental Microbiology, 65(7), 3244–3247. https://doi.org/10.1128/aem.65.7.3244-3247.1999
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