The catalytic site of chloroplastic NADP-dependent malate dehydrogenase contains a His/Asp pair

European Journal of Biochemistry

Volumn 236, Issue 3, 1996, Pages 947-952

  Lemaire, Martine ^a   Miginiac Maslow, Myroslawa ^a   Decottignies, Paulette ^a,b  

^a CNRS   (France)

^b INSTITUTE OF PLANT SCIENCES PARIS SACLAY IPS2   (France)

Author keywords

Active site; His Asp pair; Malate dehydrogenase; Site directed mutagenesis

Indexed keywords

MALATE DEHYDROGENASE (NADP);

AMINO ACID SEQUENCE; ARTICLE; CHLOROPLAST; ENZYME ACTIVE SITE; ENZYME ANALYSIS; MOLECULAR CLONING; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ACID; BASE SEQUENCE; BINDING SITES; CHLOROPLASTS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (NADP+); MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGODEOXYRIBONUCLEOTIDES; PLANTS; POINT MUTATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0029971624     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00947.x     Document Type: Article

References (34)

1. Banaszak, L. J. & Bradshaw, R. A. (1975) Malate dehydrogenases, in The enzymes (Boyer, P. D., ed.) 3rd edn. vol. XIA, pp. 369-396, Academic Press, New York.
2. Coward, C. R. & Nicholls, D. J. (1994) Malate dehydrogenase: A model for structure, evolution, and catalysis, Protein Sci. 3, 1883-1888.
3. Anderton, H. (1970) Identification of an essential, reactive histidine in pig heart mitochondrial malate dehydrogenase, Eur. J. Biochem. 15, 562-567.
4. Foster, M. & Harrison, J. H. (1974) Characterization of porcine malate dehydrogenase II. Amino acid sequence of a peptide containing the active center histidine residue, Biochim. Biophys. Acta 351, 295-300.
5. Holbrook, J. J., Lodola, A. & Illsley, N. P. (1974) Histidine residues and the enzyme activity of pig heart supernatant malate dehydrogenase, Biochem. J. 139, 797-800.
6. Birktoft, J. J. & Banaszak, L. J. (1983) The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase, J. Biol. Chem. 258, 472-482.
7. Roderick, S. L. & Banaszak, L. J. (1986) The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0 Å resolution, J. Biol. Chem. 261, 9461-9464.
8. Hall, M. D., Levin, D. G. & Banaszak, L. J. (1992) Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 Å resolution. J. Mol. Biol. 226, 867-882.
9. 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 32, 3913-3922.
10. 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.
11. Wolosiuk, R. A., Buchanan, B. B. & Crawford, N. A. (1977) Regulation of NADP-malate dehydrogenase by light-activated ferre-doxin/thioredoxin system of chloroplasts, FEBS Lett. 81, 253-258.
12. Lemaire, M., Schmitter, J.-M., Issakidis, E., Miginiac-Maslow, M., Gadal, P. & Decottignies, P. (1994) Essential histidine at the active site of sorghum leaf NADP-dependent malate dehydrogenase, J. Biol Chem. 269, 27291-27296.
13. Thompson, L. M., Higgins, D. G. & Gibson, T. J. (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
14. Crétin, 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.
15. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual. 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
16. Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection, Proc. Natl Acad. Sci. USA 82, 488-492.
17. Issakidis, E., Miginiac-Maslow, M., Decottignies, P., Jacquot, J.-P., Crétin, 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. 267, 21 577-21 583.
18. Jacquot, J.-P., Issakidis, E., Decottignies, P., Lemaire, M. & Miginiac-Maslow, M. (1995) Analysis and manipulation of target enzymes for thioredoxin control, Methods Enzymol. 252, 240-252.
19. de Lamotte-Guéry, F., Miginiac-Maslow, M., Decottignies, P., Stein, M., Minard, P. & Jacquot, J.-P. (1991) Mutation of a negatively charged amino acid in thioredoxin modifies its reactivity with chloroplastic enzymes, Eur. J. Biochem. 196, 287-294.
20. Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
21. Issakidis, E., Saarinen, M., Decottignies, P., Jacquot, J.-P., Crétin, C., Gadal, P. & Miginiac-Maslow, M. (1994) Identification and characterization of the second regulatory disulfide bridge of recombinant sorghum leaf NADP-malate dehydrogenase, J. Biol. Chem. 269, 3511-3517.
22. Johnson, V. G. & Nicholls, P. J. (1994) Histidine 21 does not play a major role in diphteria toxin catalysis. J. Biol. Chem. 269, 4349-4354.
23. Clarke, A. R., Wilks, H. M., Barstow, D. A., Atkinson, T., Chia, W. N. & Holbrook, J. J. (1988) An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase, Biochemistry 27, 1617-1622.
24. Jackson, R. M., Sessions, R. B. & Holbrook, J. J. (1992) A prediction of the three-dimensional structure of maize NADP-dependent malate dehydrogenase which explains aspects of light-dependent regulation unique to plant enzymes, J. Comput. Aided Mol. Des. 6, 1-18.
25. Lodola, A., Parker, D. M., Jeck, R. & Holbrook, J. J. (1978) Malate dehydrogenase of the cytosol. Ionizations of the enzyme-reduced-coenzyme complex and a comparison with lactate dehydrogenase, Biochem. J. 173, 597-605.
26. 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.
27. 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.
28. Cushman, J. C. (1993) Molecular cloning and expression of chloroplast NADP-malate dehydrogenase during crassulacean acid metabolism induction by salt stress, Photosynth. Res. 35, 15-27.
29. Nishiyama, M., Matsubara, N., Yamamoto, K., Iijima, 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.
30. Birktoft, J. T., Rhodes, G. & Banaszak, L. J. (1989) Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution, Biochemistry 28, 6065-6081.
31. Gietl, C., Lehnerer, M. & Olsen, O. (1990) Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein, Plant Mol. Biol. 14, 1019-1030.
32. Gleason, W. B., Fu, Z., Birktoft, J. J. & Banaszak, L. J. (1994) Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases, Biochemistry 33, 2078-2088.
33. McAlister-Henn, L., Blaber, M., Bradshaw, R. A. & Nisco, S. J. (1987) Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase, Nucleic Acids Res. 15, 4993.
34. Cendrin, F., Chroboczek, J. Zaccai, G., Eisenbers, 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 32, 4308-4313.