Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1, 2-propanediol

Appl Environ Microbiol. 1999 Jul;65(7):3244-7. doi: 10.1128/AEM.65.7.3244-3247.1999.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carbon-Oxygen Lyases / chemistry
  • Carbon-Oxygen Lyases / genetics
  • Carbon-Oxygen Lyases / isolation & purification*
  • Carbon-Oxygen Lyases / metabolism*
  • Cloning, Molecular
  • Clostridium / enzymology*
  • Clostridium / genetics
  • DNA, Bacterial
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Genetic Engineering
  • Molecular Sequence Data
  • Propylene Glycol / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Substrate Specificity

Substances

  • DNA, Bacterial
  • Recombinant Proteins
  • Propylene Glycol
  • Carbon-Oxygen Lyases
  • methylglyoxal synthase