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Gene Review

mdh  -  malate dehydrogenase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of mdh


High impact information on mdh

  • Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5 [4].
  • 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 [5].
  • Closer analysis of their specificity, however, reveals that the specificity of malate dehydrogenase is much stricter and less malleable than that of lactate dehydrogenase [6].
  • Stringency of substrate specificity of Escherichia coli malate dehydrogenase [6].
  • 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 [7].

Biological context of mdh


Associations of mdh with chemical compounds


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. Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62. Iijima, S., Saiki, T., Beppu, T. Biochim. Biophys. Acta (1980) [Pubmed]
  4. Purification and crystallization of recombinant Escherichia coli malate dehydrogenase. Hall, M.D., Levitt, D.G., McAllister-Henn, L., Banaszak, L.J. J. Mol. Biol. (1991) [Pubmed]
  5. A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Geck, M.K., Kirsch, J.F. Biochemistry (1999) [Pubmed]
  6. 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]
  7. 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]
  8. 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]
  9. Plant seeds contain several thioredoxins of regular size. Berstermann, A., Vogt, K., Follmann, H. Eur. J. Biochem. (1983) [Pubmed]
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