Kx. Huang et al., Characterization of methylglyoxal synthase from Clostridium acetobutylicumATCC 824 and its use in the formation of 1,2-propanediol, APPL ENVIR, 65(7), 1999, pp. 3244-3247
A gene encoding a putative 150-amino-acid methylglyoxal synthase was identi
fied in Clostridium acetobutylicum ATCC 824. The enzyme was overexpressed i
n Escherichia coli and purified. Methylglyoxal synthase has a native molecu
lar mass of 60 kDa and an optimum pH of 7.5. The K-m and V-max values for t
he substrate dihydroxyacetone phosphate were 0.53 mM and 1.56 mmol min(-1)
mu g respectively. When E. coli glycerol dehydrogenase was coexpressed with
methylglyoxal synthase in E. coil BL21 (DE3), 3.9 mM 1,2-propanediol was p
roduced.