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Gene Review

mdh  -  malate dehydrogenase

Escherichia coli UTI89

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Disease relevance of mdh


High impact information on mdh

  • The results show that oxaloacetate is not transferred directly from AATase to MDH because no decrease in rate was observed in the presence of approximately 100 microM inactive mutants [3].
  • Clearly, a disulfide bond can and does form between Cys residues substituted into positions 121 or 122 in the nucleotide binding domain and 305 in the carbon substrate binding domain of this NAD-dependent malate dehydrogenase [4].
  • We have constructed a series of mutants in the mobile, active site loop of the Escherichia coli malate dehydrogenase that incorporate the complementary change, conversion of arginine 81 to glutamine, to evaluate the role of charge distribution and conformational flexibility within this loop in defining the substrate specificity of these enzymes [5].
  • Trapping beta-SP with morpholine or malate dehydrogenase plus NADH abolishes the transient red color; therefore, the intermediate accumulates by virtue of the reverse reaction of beta-SP with the pyridoxamine phosphate form of the enzyme [6].
  • The latter was localized in a gene cluster with genes for an NAD(H)-dependent malate dehydrogenase and a putative citrate lyase [7].

Associations of mdh with chemical compounds

  • First, molecular dynamics were analyzed for the hyperthermophile malate dehydrogenase from Methanococcus jannaschii and a mesophilic homologue, the lactate dehydrogenase from Oryctolagus cunniculus muscle [8].

Analytical, diagnostic and therapeutic context of mdh


  1. Multichannel reverse transcription-polymerase chain reaction microdevice for rapid gene expression and biomarker analysis. Toriello, N.M., Liu, C.N., Mathies, R.A. Anal. Chem. (2006) [Pubmed]
  2. Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase. Kather, B., Stingl, K., van der Rest, M.E., Altendorf, K., Molenaar, D. J. Bacteriol. (2000) [Pubmed]
  3. A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Geck, M.K., Kirsch, J.F. Biochemistry (1999) [Pubmed]
  4. Oxidation-reduction properties of two engineered redox-sensitive mutant Escherichia coli malate dehydrogenases. Setterdahl, A., Hirasawa, M., Bucher, L.M., Dholakia, C.A., Jacquot, P., Yards, H., Miller, F., Stevens, F.J., Knaff, D.B., Anderson, L.E. Arch. Biochem. Biophys. (2000) [Pubmed]
  5. Stringency of substrate specificity of Escherichia coli malate dehydrogenase. Boernke, W.E., Millard, C.S., Stevens, P.W., Kakar, S.N., Stevens, F.J., Donnelly, M.I. Arch. Biochem. Biophys. (1995) [Pubmed]
  6. Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid. Furumo, N.C., Kirsch, J.F. Arch. Biochem. Biophys. (1995) [Pubmed]
  7. Occurrence and expression of tricarboxylate synthases in Ralstonia eutropha. Ewering, C., Brämer, C.O., Bruland, N., Bethke, A., Steinbüchel, A. Appl. Microbiol. Biotechnol. (2006) [Pubmed]
  8. Fundamental and biotechnological applications of neutron scattering measurements for macromolecular dynamics. Tehei, M., Daniel, R., Zaccai, G. Eur. Biophys. J. (2006) [Pubmed]
  9. Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Madern, D., Pfister, C., Zaccai, G. Eur. J. Biochem. (1995) [Pubmed]
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