Malate Dehydrogenase: Distribution, Function and Properties

General Physiology and Biophysics

Volumn 17, Issue 3, 1998, Pages 193-210

  Musrati, R A ^a   Kollarova M ^a   Mernik, N ^a   Mikulasova D ^a  

^a Physics and Informatics   (Slovakia)

Author keywords

Isoenzymes; Malate dehydrogenase; Protein structure

Indexed keywords

ISOENZYME; MALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ANIMAL; ARCHAEBACTERIUM; BACTERIUM; CHEMISTRY; ENZYMOLOGY; FUNGUS; MACROMOLECULE; MAMMAL; METABOLISM; PLANT; PROTEIN CONFORMATION; REVIEW;

ANIMALS; ARCHAEA; BACTERIA; FUNGI; ISOENZYMES; MACROMOLECULAR SUBSTANCES; MALATE DEHYDROGENASE; MAMMALS; NAD; NADP; PLANTS; PROTEIN CONFORMATION;

EID: 0032153389     PISSN: 02315882     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (83)

1. Banaszak L. J., Bradshow R. A. (1975): Malate dehydrogenase. In: The Enzymes, 3rd. ed. (Ed. P. Boyer), 11, pp. 369-396, Academic Press, New York
2. Beevers H. (1969): Glyoxysomes of castor bean endosperm and their relation to glyconeogenesis, Ann. NY Acad. Sci. 168, 313-324
3. Birktoft J. J., Banaszak L. J. (1983): The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. J. Biol. Chem. 258, 472-482
4. Birktoft J. J., Bradshaw R. A., Banaszak L. J. (1987): Structure of porcine heart cytoplasmic malate dehydrogenase: combinig X-ray diffraction and chemical sequence data in structural studies. Biochemistry USA 26, 2722-2734
5. Birktoft J. J., Fu Z., Carnahan G. E., Rhodes G., Roderick S. L., Banaszak L. J. (1989a): Comparison of the molecular structure of cytoplasmic and mitochondrial malate dehydrogenase. Biochem. Soc. Trans. 17, 301-304
6. Birktoft J. J., Rhodes G., Banaszak L, J. (1989b): Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution. Biochemistry USA 28, 6065-6089
7. Bleile D. M., Schulz R. A., Gregoxy E. M., Harrison J. H. (1977): Investigation of the subunit interactions in malate dehydrogenase. J. Biol. Chem. 252, 755-758
8. Breiter D. R., Resnik E., Banaszak L. J. (1994): Engineering the quaternary structure of an enzyme: construction and analysis of monomeric form of malate dehydrogenase from Escherichia coli. Protein Sci. 3, 2023-2032
9. Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., Mevarech M. (1993): Cloning, sequencing and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry USA 32, 4308-4313
10. Chien S. M., Freeman K. B. (1984): Import of rat liver mitochondrial malate dehydrogenase. Binding of the precursor to mitochondria, an intermediate step in import. J. Biol. Chem. 259, 3337-3343
11. Christian J. H. B., Waltho J. A. (1962): Water relations of Salmonella, oranieburg; stimulation of respiration by amino acids. Biochim. Biophys. Acta 65, 506-508
12. Ciriacy M. (1977): Isolation and characterization of yeast mutants defective in intermediary carbon metabolism and in carbon catabolite derepression. Mol. Gen. Genet. 154, 213-220
13. Clarke A. R., Wiglez D. B., Chia W. N., Barstow D., Atkinson T., Holbrook J. J. (1986): Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis. Nature 324, 699-702
14. Cooper T. (1971): Activation of fatty acids in castor bean endosperm. Biol. Chem. 246, 3451-3455
15. Cretin C., Luchetta P., Joly C., Decottignies P., Lepiniec L., Gadal P., Sallantin M., Huet J. C., Pernollet J. C. (1990): Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD). Eur J. Biochem. 192, 299-303
16. Curry R. A., Ting I. P. (1973): Purification and crystallization of three isoenzymes of malate dehydrogenase from Zea mays seed. Arch. Biochem. Biophys. 158, 213-224
17. Decottignies P., Schmitter J. M., Miginiac-Maslow M., Lemarechal P., Jacquot J. P., Gadal P. (1988): Primary structure of the light-dependent regulatory site of corn NADP-malate dehydrogenase. J. Biol. Chem. 263, 11780-11785
18. Donaldson R. P., Fang T. K. (1987): β-oxidation and glyoxylate cycle coupled to NADH: cytochrome c and ferricyanide reductases in glyoxysomes. Plant. Physiol. 85, 792-795
19. Dry J. B., Dimitriadis E., Ward A. D., Wiskich J. T. (1987): The photorespiration hydrogen shuttle. Synthesis of phthalonic acid and its use in the characterization of the malate/aspartate shuttle in pea (Pisarum sativum) leaf mitochondria. Biochem. J. 245, 669-675
20. Eisenberg H., Mevarech M., Zaccai G. (1992): Biochemical, structural, and molecular genetic aspects of halophilism. Adv. Protein Chem. 43, 1-61
21. Gietl C. (1992): Malate dehydrogenase isoenzymes: cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles. Biochem. Biophys. Acta 1100, 217-234
22. Gleason W., Fu Z., Birtoft J., Banaszak L. (1994): Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. Biochemistry USA 33, 2078-2088
23. Gorisch H., Jany K. (1989): Archaebacterial malate dehydrogenase: the amino-terminal sequence of the enzyme from Sulfolobus acidocalderius is homologous to the eubacterial and eukaryotic malate dehydrogenase. FEBS Lett. 247, 259-262
24. Goward C. R., Nicholls D. J. (1994): Malate dehyrogenase: a model for structure, evolution and catalysis. Protein Sci. 3, 1883-1888
25. Grau U. M., Trommer W. E., Rossman M. G. (1981): Sructure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 Å resolution. J. Mol. Biol. 151, 289-307
26. Hall M. D., Levitt D. G., Banaszak L. J. (1992): Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution. J. Mol. Biol. 226, 867-882
27. Harada K., Wolfe R. G. (1968): Malic dehydrogenase. VII. The catalytic mechanism and possible role of identical protein subunits. J. Biol. Chem. 243, 4131-4137
28. Hartl F. U., Pfanner N., Nicholson D., Neupert W. (1989): Mitochondrial protein import. Biochim. Biophys. Acta 988, 1-45
29. Hatch M. D., Slack C. R. (1969): NADP-specific malate dehydrogenase and glycerate kinase in leaves and evidence for their location in chloroplasts. Biochem. Biophys. Res. Commun. 34, 589-593
30. Hecht K., Wrba A., Jaenicke R. (1989): Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity. Eur. J. Biochem. 183, 69-74
31. Hill E., Tsernoglou D., Webb L., Banaszak L. (1972): Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Angstrom resolution. J. Mol. Biol. 72, 577-591
32. Hochachka P. W., Somero G. N. (1973): Strategies of Biochemical Adaptation, W.B. Saunders Co., p. 358, Philadelphia, London, Toronto
33. Hock B., Gietl C. (1982): Cell-free synthesis of water-melon glyoxysomal malate dehydrogenase: a comparison with the mitochondrial isoenzyme. Ann. NY Acad. Sci. 386, 350-361
34. Honka E., Fabry S., Niermann T., Palm P., Hensel R. (1990): Properties and primary sequence of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur. J. Biochem. 188, 623-632
35. Huang A. H. C. (1987): The Biochemistry of Plants (Ed. P.K.Stumpf) pp. 91-119, Academic Press, London, New York
36. Iijima S., Saiki T., Beppu T. (1980): Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62. Biochim. Biophys. Acta 613, 1-9
37. Iijima S., Saiki T. (1984): Reversibile denaturation of thermophilic malate dehydrogenase by guanidine hydrochloride and acid. J. Biochem. 95, 1273-1281
38. Issakidis E., Migniac-Maslow M., Decottignies P., Jacquot J-P., Cretin C., Gadal P. (1992): Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase. J. Biol. Chem. 26, 21577-21583
39. Issakidis E., Decottignies P., Migniac-Maslow M. (1993): A thioredoxin-independent fully active NADP-malate dehydrogenase obtained by site-directed mut agenesis. FEBS Lett. 321, 55-58
40. Issakidis E., Saarinen M., Decottignies P., Jacquot J-P., Cretin C., Gadal P., Migniac-Maslow M. (1994): Purification and characterization of the second regulatory disulfide site of recombinant sorghum leaf NADP-malate dehydrogenase. J. Biol. Chem. 269, 3511-3517
41. Issakidis E., Lemaire M., Decottignies P., Jacquot J-P., Migniac-Maslow M. (1996): Direct evidence for the different roles of the N- and C-terminal regulatory disulfides of sorghum leaf NADP-malate dehydrogenase in its activation by reduced thioredoxin. FEBS Lett. 392, 121-124
42. Jaenicke R. (1981): Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10, 1-67
43. Jaenicke R. (1988): Stability and self-organization of proteins. Naturwissenschaften 75, 604-610
44. Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y. (1987): Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. J. Biol. Chem. 262, 15127-15131
45. Johnson H. P., Hatch M. D. (1970): Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and "malic" enzyme in plants with the C4-dicarboxylic acid pathway of photosyntesis. Biochem. J. 119, 273-280
46. Kelly C. A., Nishiyama M., Ohnishi Y., Beppu T., Birktoft J. J. (1993): Determinants of protein thermostability observed in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry USA 32, 3913-3922
47. Lemaire M., Miginiac Maslow M., Decottignies P. (1996): The catalytic site of chloroplastic NADP-dependent malate dehydrogenase contains a His/Asp pair. Eur. J. Biochem. 236, 947-952
48. Lorimer G. H., Andrews T. J. (1980): The biochemistry of plants. A comprehensive treatise. In: Photosynthesis (Eds. M. D. Hatch, N. K. Boardman) pp. 329-374, Academic Press, New York
49. MacLachlan L., Haris P., Reid D., White J., Chapman D., Lucy J., Austen B. (1994): A spectroscopic study of the mitochondrial transit peptide of rat malate dehydrogenase. J. Biochem. 303, 657-662
50. McAlister-Henn L. (1988): Evolutionary relationships among the malate dehydrogenases. Trends Biochem. Sci. 13, 178-181
51. McAlister-Henn L., Blaber M., Bradshaw R., Nisco S. (1987): Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase. Nucl. Acids Res. 15, 4993
52. Mernik N., Lewis R., Kollárová M., Mikulášová D., Kadlecová Z. (1998): Characterization and Crystallisation of the Malate Dehydrogenase from Streptomyces aureofaciens. Gen. Physiol. Biophys. 17, Suppl. 1, 49-51
53. Mettler I. J., Beevers H. (1980): Oxidation of NADH in glyoxysomes by a malate/aspartate shuttle. Plant Physiol. 66, 555-560
54. Metzler M. C., Rothermel B. A., Nelson T. (1989): Maize NADP-malate dehydrogenase: cDNA cloning, sequence and mRNA characterization. Plant Mol. Biol. 12, 713-722
55. Mikulášová D., Kollárová M., Migniac-Maslow M., Decottignies P., Jacquot J-P., Kutejová E., Mernik N., Egyudová I., Musrati R., Horecká T. (1998): Purification and characterization of the malate dehydrogenase from Streptomyces aureofaciens. FEMS Lett. 159, 299-305
56. Mullinax T. R., Mock J. N., McEvily A. J., Harrison J. H. (1982): Regulation of mitochondrial malate dehydrogenase. J. Biol, Chem. 257, 13233-13239
57. Muto S., Beevers H. (1974): Lipase activities in castor bean endosperm during germination. Plant Physiol. 54, 23-28
58. Nicholls D. J., Miller J., Scawen M. D., Clarke A. R., Holbrook J. J., Atkinson T., Goward C. R. (1992): The importance of arginine 102 for the substrate specificity of Escherichia coli malate dehydrogenase. Biochem. Biophys. Res. Commun. 189, 1057-1062
59. Nishiyama M., Matsubara N., Yamamoto K., Lijima S., Uozumi T., Beppu T. (1986): Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. J. Biol. Chem. 261, 14178-14183
60. Nishiyama M., Shimada K., Horinouchi S., Beppu T. (1991): Role of threonin 190 in modulating the catalytic function of malate dehydrogenase from a thermophile Thermus flavus, J. Biol. Chem. 266, 14294-14299
61. Parker J. H., Mattoon J. R. (1969): Mutants of yeast with altered oxidative energy metabolism: selection and genetic characterization. J. Bacteriol. 100, 647-657
62. Piontek K., Chakrabarti P., Schar H. P., Rossman M. G., Zuber H. (1990): Structure determination and refinement of Bacillus stearmophilus lactate dehydrogenase. Proteins 7, 74-92
63. Poeydomenge O., Marolda M., Boudet A., Grima-Pettenati J. (1995): Nucleotide sequence of a cDNA encoding mitochondrial malate dehydrogenase from eucalyptus. Plant Physiol. 107, 1455-1456
64. Pundak S., Eisenberg H. (1981): Structure and activity of malate dehydrogenase from extreme halophilic bacteria of Dead Sea. 1. Conformation and interaction with water and salt between 5M and 1M NaCl concentration. Eur. J. Biochem. 118, 463-470
65. Pundak S., Aloni H., Eisenberg H. (1981): Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2M. Salt, salt concentration and temperature dependence of enzyme stability. Eur. J. Biochem. 118, 471-477
66. Rao S. T., Rossmann M.G. (1973): Comparison of super-secondary structures in proteins. J. Mol. Biol. 26, 241-256
67. Rehfeld D. W., Tolbert N. E. (1972): Aminotransferases in peroxisomes from spinach leaves. J. Biol. Chem. 247, 4803-4811
68. Reng W., Riessland R., Scheibe R., Jaenicke R. (1993): Cloning, site-specific mutagenesis expression and characterization of full-length chloroplast NADP-malate dehydrogenase from Pisum sativum. Eur. J. Biochem. 217, 189-197
69. Roderick S. L., Banaszak L. J. (1986): The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0 A resolution. J. Biol. Chem. 261, 9461-9464
70. Schatz G. (1993): The protein import machinery of mitochondria. Protein Sci. 2, 141-146
71. Setoyama C., Ding S. H., Choudhury B. K., Joh T., Takeshima H., Tsuzuki T., Shimada K. (1990): Regulatory regions of the mitochondrial and cytosolic isoenzyme genes participating in the malate-aspartate shuttle. J. Biol. Chem. 265, 1293-1299
72. Somero G. N., Low P. S. (1976): Temperature: a "shaping force" in protein evolution. Biochem. Soc. Symp. 41, 33-42
73. Sutherland P., McAlister -Henn L. (1985): Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase. J. Bacteriol. 163, 1074-1079
74. Tzagoloff A , Akai A., Needleman R. B. (1975): Assembly of the mitochondrial membrane system: isolation of nuclear and cytoplasmic mutants of Saccharomyces cerevisiae with specific defects in mitochondrial functions. J. Bacteriol. 122, 826-831
75. Wigley D. B., Gamblin S. J., Turkenburg J. P., Dodson E. J., Piontek K., Muirhead H., Holbrook J. J. (1992): Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution. J. Mol. Biol. 223, 317-335
76. Wilks H. M., Hart K. N., Feeney R., Dunn C. R., Murhead H., Chia W. N., Barstow D. A., Atkinson T., Clarke A. R., Holbrook J. J. (1988): A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science 242, 1541-1544
77. Wolosiuk R. A., Schurmann P., Buchanan B. B. (1980): Thioredoxin and ferredoxin-thioredoxin reductase of spinach chloroplasts. Methods Enzymol. 69, 382-391
78. Wood D. C., Hodges C. T., Howell S. M., Clary L.- G., Harrison J. H. (1981a): The N-ethylmaleimide-sensitive cysteine residue in the pH-dependent subunite interactions of malate dehydrogenase. J. Biol. Chem. 256, 9895-9900
79. Wood D. C., Jurgensen S. R., Geesin J. C., Harrison J. H. (1981b): Subunit interactions in mitochondrial malate dehydrogenase. Kinetics and mechanisms of reassociation. J. Biol. Chem. 256, 2377-2382
80. Yamazaki R. K., Tolbert N. E. (1969): Malate dehydrogenase in leaf peroxisomes. Biochem. Biophys. Acta 178, 11-20
81. Yancey P, H., Clark M. E., Hand S. C., Bowlus R. D., Somero G. N. (1982): Living with water stress: evolution of osmolyte systems. Science 217, 1214-1222
82. Yueh A. Y., Chung C.-S., Lai Y.-K. (1989): Purification and molecular properties of malate dehydrogenase from the marine diatom Nitzschia alba. J. Biochem. 258, 221-228
83. Zaccai G., Cendrin P., Haik Y., Borochov N., Eisenberg H. (1989): Stabilization of halophilic malate dehydrogenase. J. Mol. Biol. 208, 491-500