Comparison of D-malate and beta, beta-dimethylmalate dehydrogenases from Pseudomonas fluorescens UK-1.
D-Malate dehydrogenase (D-malate:NAD+ oxidoreductase (decarboxylating), EC 1.1.1.83) was purified to homogeneity from Pseudomonas fluorescens UK-1 grown on D-malate and some properties of the purified enzyme were compared with those of beta, beta-dimethylmalate dehydrogenase (3,3-dimethyl-D-malate:NAD+ oxidoreductase (decarboxylating), EC 1.1.1.84). D-Malate dehydrogenase has the molecular weight and subunit size of 140 000 and 34 000, respectively (the same as those of beta, beta-dimethylmalate dehydrogenase). The amino acid compositions of the two enzymes are similar as well. D-Malate dehydrogenase cross-reacted with anti-beta, beta-dimethylmalate dehydrogenase and beta, beta-dimethylmalate dehydrogenase cross-reacted with anti-D-malate dehydrogenase. The two dehydrogenases have similar catalytical properties. Both of the dehydrogenases were unaffected by sulphydryl reagents but were inactivated by 1,2-butanedione. NAD provided better protection against inactivation than D-malate or beta,beta-dimethyl-DL-malate.
D000429:Alcohol Oxidoreductases / Q000276:immunology / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D008291:Malate Dehydrogenase / Q000276:immunology / Q000302:isolation & purification*; D008293:Malates / Q000276:immunology / Q000302:isolation & purification; D008970:Molecular Weight; D011551:Pseudomonas fluorescens / Q000201:enzymology*
D000596:Amino Acids; D001426:Bacterial Proteins; D008293:Malates; D000429:Alcohol Oxidoreductases; D008291:Malate Dehydrogenase; C020067:dimethylmalate dehydrogenase