The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

MDH1  -  malate dehydrogenase 1, NAD (soluble)

Homo sapiens

Synonyms: Cytosolic malate dehydrogenase, Diiodophenylpyruvate reductase, HEL-S-32, MDH-s, MDHA, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of MDH1

  • Finally, over-expression of MDH1 is found in left ventricular cardiac muscle of dilated cardiomyopathy (DCM) patients when contrasted to the diseased non-DCM and normal heart muscle by in situ hybridization and Western blot [1].
  • The N-terminal amino acid sequence was enriched with hydrophobic amino acids, which showed a high degree of functional similarity to amino acids at the N-terminal ends of both Escherichia coli and Thermus flavus MDHs [2].
  • Malate dehydrogenase (MDH) from the moderately thermophilic bacterium Chloroflexus aurantiacus (CaMDH) is a tetrameric enzyme, while MDHs from mesophilic organisms usually are dimers [3].
  • Here we report an unbiased comparison of the same batch of six major E. granulosus antigens, namely, hydatid cyst fluid (HCF), native antigen B (AgB), two recombinant AgB subunits, an AgB-derived synthetic peptide, and recombinant cytosolic malate dehydrogenase from E. granulosus (EgMDH), against the same serum collection [4].
  • Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure [5].

High impact information on MDH1


Biological context of MDH1


Anatomical context of MDH1


Associations of MDH1 with chemical compounds


Co-localisations of MDH1

  • Starch gel electrophoresis followed by histochemical staining using either p-hydroxy-phenylpyruvic acid (HPPA) or malate as the substrate shows that KAR activity comigrates with MDH-s in all species studied except some marine species [19].

Regulatory relationships of MDH1

  • Antibodies raised against purified chicken MDH-s equally inhibited both MDH-s and KAR in chickens and humans [20].
  • Antisera raised against purified chicken MDH-s totally inhibited both MDH-s and KAR activity in chicken liver homogenates [19].

Other interactions of MDH1

  • The male individuals with schizophrenia compared to male controls showed reductions by 2.8- to 3.7-fold of HINT1, neuroserpin, and MDH1 by Q-PCR [11].
  • The decreases in mRNA abundance for MDH1 (P = 0.006), HINT1 (P = 0.050), and neuroserpin (P = 0.005) in DLPFC of male individuals with schizophrenia is consistent with prior reports [11].
  • A series of rodent-human hybrid clones exhibiting a mitotic separation of IDH1 and MDH1 indicated that ADCP is most probably situated between corresponding loci in human chromosome 2 [21].
  • The bulk of the KAR activity in human blood appears to be due to MDH-s, with a minor fraction catalysed by LDH, as is the case in most other species studied [20].
  • Locusta migratoria manilensi has two allele fixations in lactate dehydrogenase (LDH) and malic enzyme (ME); while Gastrimargus saussure has a fixed allele at MDH-1 and a unique fixation at MDH-2 [22].

Analytical, diagnostic and therapeutic context of MDH1


  1. Developmental regulation and cellular distribution of human cytosolic malate dehydrogenase (MDH1). Lo, A.S., Liew, C.T., Ngai, S.M., Tsui, S.K., Fung, K.P., Lee, C.Y., Waye, M.M. J. Cell. Biochem. (2005) [Pubmed]
  2. Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence. Rolstad, A.K., Howland, E., Sirevåg, R. J. Bacteriol. (1988) [Pubmed]
  3. Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface. Bjørk, A., Dalhus, B., Mantzilas, D., Eijsink, V.G., Sirevåg, R. J. Mol. Biol. (2003) [Pubmed]
  4. Comparative analysis of the diagnostic performance of six major Echinococcus granulosus antigens assessed in a double-blind, randomized multicenter study. Lorenzo, C., Ferreira, H.B., Monteiro, K.M., Rosenzvit, M., Kamenetzky, L., García, H.H., Vasquez, Y., Naquira, C., Sánchez, E., Lorca, M., Contreras, M., Last, J.A., González-Sapienza, G.G. J. Clin. Microbiol. (2005) [Pubmed]
  5. Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure. Charnock, C. J. Bacteriol. (1997) [Pubmed]
  6. Malate dehydrogenase: viability of cytosolic nulls and lethality of mitochondrial nulls in maize. Goodman, M.M., Newton, K.J., Stuber, C.W. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  7. Localization of human gene loci using spontaneous chromosome rearrangements in human-Chinese hamster somatic cell hybrids. Hamerton, J.L., Mohandas, T., McAlpine, J. Am. J. Hum. Genet. (1975) [Pubmed]
  8. Thioredoxin-h1 Reduces and Reactivates the Oxidized Cytosolic Malate Dehydrogenase Dimer in Higher Plants. Hara, S., Motohashi, K., Arisaka, F., Romano, P.G., Hosoya-Matsuda, N., Kikuchi, N., Fusada, N., Hisabori, T. J. Biol. Chem. (2006) [Pubmed]
  9. Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase. Porpaczy, Z., Sumegi, B., Alkonyi, I. J. Biol. Chem. (1987) [Pubmed]
  10. Further evidence by gene dosage for the regional assignment of erythrocyte acid phosphatase (ACP1) and malate dehydrogenase (MDH1) loci on chromosome 2p. Larson, L.M., Bruce, A.W., Saumur, J.H., Wasdahl, W.A. Clin. Genet. (1982) [Pubmed]
  11. Gene expression of metabolic enzymes and a protease inhibitor in the prefrontal cortex are decreased in schizophrenia. Vawter, M.P., Shannon Weickert, C., Ferran, E., Matsumoto, M., Overman, K., Hyde, T.M., Weinberger, D.R., Bunney, W.E., Kleinman, J.E. Neurochem. Res. (2004) [Pubmed]
  12. Duplication of 2p25: confirmation of the assignment of soluble acid phosphatase (ACP1) locus to 2p25. Wakita, Y., Narahara, K., Takahashi, Y., Kikkawa, K., Kimura, S., Oda, M., Kimoto, H. Hum. Genet. (1985) [Pubmed]
  13. Purification and characterization of two forms of methanol dehydrogenases from a marine methylotroph. Chang, A.K., Lim, C.Y., Kim, S.W., You, H.J., Hahm, K.S., Yoon, S.M., Park, J.K., Lee, J.S. J. Basic Microbiol. (2002) [Pubmed]
  14. Friedreich ataxia: III. Mitochondrial malic enzyme deficiency. Stumpf, D.A., Parks, J.K., Eguren, L.A., Haas, R. Neurology (1982) [Pubmed]
  15. Role of cytosolic malate dehydrogenase in oocyte maturation and embryo development. Yoon, S.J., Koo, D.B., Park, J.S., Choi, K.H., Han, Y.M., Lee, K.A. Fertil. Steril. (2006) [Pubmed]
  16. Ability of cytosolic malate dehydrogenase and lactate dehydrogenase to increase the ratio of NADPH to NADH oxidation by cytosolic glycerol-3-phosphate dehydrogenase. Fahien, L.A., Laboy, J.I., Din, Z.Z., Prabhakar, P., Budker, T., Chobanian, M. Arch. Biochem. Biophys. (1999) [Pubmed]
  17. Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate reduction in wheat. Ding, Y., Ma, Q.H. Biochimie (2004) [Pubmed]
  18. Mannitol is required for asexual sporulation in the wheat pathogen Stagonospora nodorum (glume blotch). Solomon, P.S., Waters, O.D., Jörgens, C.I., Lowe, R.G., Rechberger, J., Trengove, R.D., Oliver, R.P. Biochem. J. (2006) [Pubmed]
  19. The reduction of aromatic alpha-keto acids by cytoplasmic malate dehydrogenase and lactate dehydrogenase. Friedrich, C.A., Morizot, D.C., Siciliano, M.J., Ferrell, R.E. Biochem. Genet. (1987) [Pubmed]
  20. Biochemical and genetic identity of alpha-keto acid reductase and cytoplasmic malate dehydrogenase from human erythrocytes. Friedrich, C.A., Ferrell, R.E., Siciliano, M.J., Kitto, G.B. Ann. Hum. Genet. (1988) [Pubmed]
  21. Assignment of adenosine deaminase complexing protein (ADCP) gene(s) to human chromosome 2 in rodent-human somatic cell hybrids. Herbschleb-Voogt, E., Grzeschik, K.H., Pearson, P.L., Meera Khan, P. Hum. Genet. (1981) [Pubmed]
  22. Comparative allozyme analysis of severel grasshopper species. Qiao, H.X., Duan, Y.H., Ma, E.B., Han, Y. Yi Chuan Xue Bao (2002) [Pubmed]
  23. Microarray screening of lymphocyte gene expression differences in a multiplex schizophrenia pedigree. Vawter, M.P., Ferran, E., Galke, B., Cooper, K., Bunney, W.E., Byerley, W. Schizophr. Res. (2004) [Pubmed]
  24. Cloning and sequence analysis of cDNAs encoding plant cytosolic malate dehydrogenase. Ocheretina, O., Scheibe, R. Gene (1997) [Pubmed]
  25. Purification and partial characterization of cytosolic malate dehydrogenase from Tritrichomonas foetus. Hrdý, I. Folia Parasitol. (1993) [Pubmed]
WikiGenes - Universities