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Gene Review

MDH2  -  malate dehydrogenase 2, NAD (mitochondrial)

Sus scrofa

Synonyms: MDH, MMDH
 
 
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Disease relevance of MDH2

 

High impact information on MDH2

 

Chemical compound and disease context of MDH2

  • 0.4 M myo-Inositol was observed to raise the melting temperature (Tm) of GS from E. coli by 3.9 degrees C and MDH from pig heart by 3.4 degrees C, respectively [6].
  • Cpn60-(His)(6) mediated refolding of guanidine hydrochloride unfolded pig heart malic dehydrogenase (MDH) and Thermus flavus MDH at 25 and 70 degrees C, respectively, in an ATP-dependent manner [7].
  • Guanidinium chloride (GdmCl) unfolding experiments showed that there is only about a 4.2-kjoule/mol difference in delta G 0 between the pig and Thermus MDH [8].
 

Biological context of MDH2

 

Anatomical context of MDH2

 

Associations of MDH2 with chemical compounds

 

Other interactions of MDH2

 

Analytical, diagnostic and therapeutic context of MDH2

References

  1. Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro. Hartman, D.J., Surin, B.P., Dixon, N.E., Hoogenraad, N.J., Høj, P.B. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  2. Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase. Trejo, F., Gelpí, J.L., Ferrer, A., Boronat, A., Busquets, M., Cortés, A. Protein Eng. (2001) [Pubmed]
  3. Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide. Gietl, C. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  4. Quantitation of the interaction between citrate synthase and malate dehydrogenase. Tompa, P., Batke, J., Ovadi, J., Welch, G.R., Srere, P.A. J. Biol. Chem. (1987) [Pubmed]
  5. The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0-A resolution. Roderick, S.L., Banaszak, L.J. J. Biol. Chem. (1986) [Pubmed]
  6. Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation. Jaindl, M., Popp, M. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  7. Affinity purification of fusion chaperonin Cpn60-(His)(6) from thermophilic bacterium Bacillus strain MS and its use in facilitating protein refolding and preventing heat denaturation. Teshima, T., Kohda, J., Kondo, A., Yohda, M., Tamura, A., Fukuda, H. Biotechnol. Prog. (2000) [Pubmed]
  8. An investigation of the thermal stabilities of two malate dehydrogenases by comparison of their three-dimensional structures. Duffield, M.L., Nicholls, D.J., Atkinson, T., Scawen, M.D. Journal of molecular graphics. (1994) [Pubmed]
  9. Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase. Joh, T., Takeshima, H., Tsuzuki, T., Shimada, K., Tanase, S., Morino, Y. Biochemistry (1987) [Pubmed]
  10. Subunit interactions in mitochondrial malate dehydrogenase. Kinetics and mechanism of reassociation. Wood, D.C., Jurgensen, S.R., Geesin, J.C., Harrison, J.H. J. Biol. Chem. (1981) [Pubmed]
  11. Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase. Grant, P.M., Roderick, S.L., Grant, G.A., Banaszak, L.J., Strauss, A.W. Biochemistry (1987) [Pubmed]
  12. Electrostatic channeling of oxaloacetate in a fusion protein of porcine citrate synthase and porcine mitochondrial malate dehydrogenase. Shatalin, K., Lebreton, S., Rault-Leonardon, M., Vélot, C., Srere, P.A. Biochemistry (1999) [Pubmed]
  13. Comparison of the molecular structures of cytoplasmic and mitochondrial malate dehydrogenase. Birktoft, J.J., Fu, Z., Carnahan, G.E., Rhodes, G., Roderick, S.L., Banaszak, L.J. Biochem. Soc. Trans. (1989) [Pubmed]
  14. Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes. Webster, K.A., Freeman, K.B., Ohki, S. Biochem. J. (1980) [Pubmed]
  15. Tissue origin of MDH isozymes in blood serum of rats exposed to alkylmercurials. Breźnicka, E.A., Chmielnicka, J., Wójcikiewicz-Herma, L. Journal of applied toxicology : JAT. (1983) [Pubmed]
  16. Immunocytochemical localization of transferrin and mitochondrial malate dehydrogenase in the developing nervous system of the rat. Dion, T.L., Markelonis, G.J., Oh, T.H., Bregman, B.S., Pugh, M.A., Hobbs, S.L., Kim, Y.C. Dev. Neurosci. (1988) [Pubmed]
  17. Active subunits in hybrid-modified malate dehydrogenase. Jurgensen, S.R., Harrison, J.H. J. Biol. Chem. (1982) [Pubmed]
  18. Biphasic inactivation of procine heart mitochondrial malate dehydrogenase by pyridoxal 5'-phosphate. Wimmer, M.J., Mo, T., Sawyers, D.L., Harrison, J.H. J. Biol. Chem. (1975) [Pubmed]
  19. Regulation of mitochondrial malate dehydrogenase. Evidence for an allosteric citrate-binding site. Mullinax, T.R., Mock, J.N., McEvily, A.J., Harrison, J.H. J. Biol. Chem. (1982) [Pubmed]
  20. Inhibition of glutamate dehydrogenase and malate dehydrogenases by palmitoyl coenzyme A. Kawaguchi, A., Bloch, K. J. Biol. Chem. (1976) [Pubmed]
  21. The N-ethylmaleimide-sensitive cysteine residue in the pH-dependent subunit interactions of malate dehydrogenase. Wood, D.C., Hodges, C.T., Howell, S.M., Clary, L.G., Harrison, J.H. J. Biol. Chem. (1981) [Pubmed]
  22. Large-scale purification and some properties of the mitochondrial aspartate aminotransferase from pig heart. Barra, D., Bossa, F., Doonan, S., Fahmy, H.M., Martini, F., Hughes, G.J. Eur. J. Biochem. (1976) [Pubmed]
  23. The immobilization of mitochondrial malate dehydrogenase on Sepharose beads and the demonstration of catalytically active subunits. Jurgensen, S.R., Wood, D.C., Mahler, J.C., Harrison, J.H. J. Biol. Chem. (1981) [Pubmed]
  24. Investigation of the relation of the pH-dependent dissociation of malate dehydrogenase to modification of the enzyme by N-ethylmaleimide. Hodges, C.T., Wiggins, J.C., Harrison, J.H. J. Biol. Chem. (1977) [Pubmed]
  25. Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein. Gietl, C., Lehnerer, M., Olsen, O. Plant Mol. Biol. (1990) [Pubmed]
 
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