Molecular and Cellular Biochemistry

, Volume 156, Issue 2, pp 117–124

Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase

  • Kanika Misra
  • Arun B. Banerjee
  • Subhankar Ray
  • Manju Ray
Article

DOI: 10.1007/BF00426333

Cite this article as:
Misra, K., Banerjee, A.B., Ray, S. et al. Mol Cell Biochem (1996) 156: 117. doi:10.1007/BF00426333

Abstract

Two enzymes, one NADPH-dependent and another NADH-dependent which catalyze the reduction of methylglyoxal to acetol have been isolated and substantially purified from crude extracts of Escherichia coli K12 cells. Substrate specificity and formation of acetol as the reaction product by both the enzymes, reversibility of NADH-dependent enzyme with alcohols as substrates and inhibitor study with NADPH-dependent enzyme indicate that NADPH-dependent and NADH-dependent enzymes are identical with an aldehyde reductase (EC 1.1.1.2) and alcohol dehydrogenase (EC 1.1.1.1) respectively. The Km for methylglyoxal have been determined to be 0.77 mM for NADPH-dependent and 3.8 mM for NADH-dependent enzyme. Stoichiometrically equimolar amount of acetol is formed from methylglyoxal by both NADPH- and NADH-dependent enzymes. In phosphate buffer, both the enzymes are active in the pH range of 5.8–6.6 with no sharp pH optimum. Molecular weight of both the enzymes were found to be 100,000 ± 3,000 by gel filtration on a Sephacryl S-200 column. Both NADPH- and NADH-dependent enzymes are sensitive to sulfhydryl group reagents.

Key words

methylglyoxalaldehyde reductasealcohol dehydrogenaseEscherichia coli

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Kanika Misra
    • 1
  • Arun B. Banerjee
    • 1
  • Subhankar Ray
    • 1
  • Manju Ray
    • 2
  1. 1.Department of Biochemistry, University College of ScienceUniversity of CalcuttaCalcutta
  2. 2.Department of Biological ChemistryIndian Association for the Cultivation of ScienceCalcuttaIndia