Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1, 2-propanediol.
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) microgram(-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.
Huang
K
K
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892, USA.
Rudolph
F B
FB
Bennett
G N
GN
D000595:Amino Acid Sequence; D019757:Carbon-Oxygen Lyases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D003001:Cloning, Molecular; D003013:Clostridium / Q000201:enzymology* / Q000235:genetics; D004269:DNA, Bacterial; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005818:Genetic Engineering; D008969:Molecular Sequence Data; D019946:Propylene Glycol / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
D004269:DNA, Bacterial; D011994:Recombinant Proteins; D019946:Propylene Glycol; D019757:Carbon-Oxygen Lyases; C021578:methylglyoxal synthase