caa a22 4500 477118674 CHVBK 20180405111629.0 cr unu---uuuuu 170330e19960901xx s 000 0 eng 10.1007/BF00426333 doi (NATIONALLICENCE)springer-10.1007/BF00426333 Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase [Elektronische Daten] [Kanika Misra, Arun Banerjee, Subhankar Ray, Manju Ray] 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. Kluwer Academic Publishers, 1996 methylglyoxal nationallicence aldehyde reductase nationallicence alcohol dehydrogenase nationallicence Escherichia coli nationallicence Misra Kanika Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut Banerjee Arun Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut Ray Subhankar Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut Ray Manju Department of Biological Chemistry, Indian Association for the Cultivation of Science, 700 032, Calcutta, India aut Molecular and Cellular Biochemistry Kluwer Academic Publishers 156/2(1996-09-01), 117-124 0300-8177 156:2<117 1996 156 11010 https://doi.org/10.1007/BF00426333 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00426333 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Misra Kanika Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut NATIONALLICENCE 700 1- Banerjee Arun Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut NATIONALLICENCE 700 1- Ray Subhankar Department of Biochemistry, University College of Science, University of Calcutta, 700 019, Calcutta aut NATIONALLICENCE 700 1- Ray Manju Department of Biological Chemistry, Indian Association for the Cultivation of Science, 700 032, Calcutta, India aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers 156/2(1996-09-01), 117-124 0300-8177 156:2<117 1996 156 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer