Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea

Journal of Bacteriology

Volumn 182, Issue 13, 2000, Pages 3688-3692

  Graupner, Marion ^a   Xu, Huimin ^a   White, Robert H ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYACID DEHYDROGENASE; MALATE DEHYDROGENASE; METHANOPTERIN; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARCHAEBACTERIUM; ARTICLE; BACTERIUM IDENTIFICATION; CATALYSIS; COENZYME; DERIVATIZATION; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME SYNTHESIS; METHANOGENESIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; STEREOCHEMISTRY;

ALCOHOL OXIDOREDUCTASES; CATALYSIS; L-LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASES; MALATE DEHYDROGENASE; MESNA; METHANOCOCCACEAE; METHANOCOCCUS;

EID: 0034099657     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.13.3688-3692.2000     Document Type: Article

References (38)

1. Birktoft, J. J., R. T. Fernley, R. A. Bradshaw, and L. J. Banaszak. 1992. Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases from a homologous system with lactate dehydrogenase. Proc. Natl. Acad. Sci. USA 79:6166-6170.
2. Bult, C. J., O. White, G. J. Olsen, L. Zhou, R. D. Fleischmann, G. G. Sutton, J. A. Blake, L. M. FitzGerald, R. A. Clayton, J. D. Gocayne, A. R. Kerlavage, B. A. Dougherty, J.-F. Tomb, M. D. Adams, C. I. Reich, R. Overbeek, E. F. Kirkness, K. G. Weinstock, J. M. Merrick, A. Glodek, J. L. Scott, N. S. M. Geoghagen, J. F. Weidman, J. L. Fuhrmann, D. Nguyen, T. R. Utterback, J. M. Kelley, J. D. Peterson, P. W. Sadow, M. C. Hanna, M. D. Cotton, K. M. Roberts, M. A. Hurst, B. P. Kaine, M. Borodovsky, H.-P. Klenk, C. M. Fraser, H. O. Smith, C. R. Woese, and J. C. Venter. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073.
3. Bur, D., M. A. Lutaen, H. Wynn, L. R. Provencher, J. B. Jones, M. Gold, J. D. Friesen, A. R. Clark, and J. J. Holbrook. 1989. An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillus stearothermophilus. Can. J. Chem. 67:1065-1070.
4. Crane, R. K. 1962. Hexokinases and pentokinases, p. 47-66. In P. D. Boyer, H. Lardy, and K. Myrback (ed.), The enzymes, vol. 6. Academic Press, New York, N.Y.
5. Davies, D., and E. Kun. 1957. Isolation and properties of malic dehydrogenase from ox-heart mitochondria. Biochem. J. 1957:307-316.
6. 420 from Methanobacterium. Biochemistry 17:4583-4593.
7. Gorris, L. G. M., C. van der Drift, and G. D. Vogels. 1988. Separation and quantification of cofactors from methanogenic bacteria by high-performance liquid chromatography: optimum and routine analyses. J. Microbiol. Methods 8:175-190.
8. Gorris, L. G. M., and C. van der Drift. 1994. Cofactor contents of methanogenic bacteria reviewed. Biofactors 4:139-145.
9. Goward, C. R., and D. J. Nicholls. 1994. Malate dehydrogenase: a model for structure, evolution, and catalysis. Protein Sci. 3:1883-1888.
10. Hill, R. K., and T. H. Chan. 1970. The absolute configuration of pantothenic acid. Biochem. Biophys. Res. Commun. 38:181-183.
11. Hohorst, J. J. 1963. L-(-)-Malate determination with malate dehydrogenase and DPN, p. 328-332. In H.-U. Bergmeyer (ed.), Methods of enzymatic analysis. Academic Press, New York, N.Y.
12. Honka, E., S. Fabry, T. Niermann, P. Palm, and R. Hensel. 1990. Properties and primary structure of the L-malate dehydrogenases from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur. J. Biochem. 188:623-632.
13. Howell, D. M., K. Harich, H. Xu, and R. H. White. 1998. The α-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoylthreonine phosphate) in methanogenic Archaea. Biochemistry 37:10108-10117.
14. Kagawa, T., and P. L. Bruno. 1988. NADP-malate dehydrogenase from leaves of Zea mays: purification and physical, chemical and kinetic properties. Arch. Biochem. Biophys. 260:674-695.
15. Kim, M.-J., and G. M. Whitesides. 1988. L-Lactate dehydrogenase: substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids. J. Am. Chem. Soc. 110:2959-2964.
16. Langelandsvik, A. S., I. H. Steen, N. K. Birkeland, and T. Lien. 1997. Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus. Arch. Microbiol. 168:59-67.
17. Leigh, J. A., L. L. Reinhart, Jr., and R. S. Wolfe. 1984. Structure of methanofuran, the carbon dioxide reduction factor of Methanobacterium thermoautotrophicum. J. Am. Chem. Soc. 106:3636-3640.
18. 420 and its γ-monoglutamyl derivative in nonmethanogenic archaebacteria. J. Bacteriol. 168:444-448.
19. Parks, R. E., Jr., and R. P. Agarwal. 1973. Nucleoside diphosphokinases, p. 307-333. In P. D. Boyer (ed.), The enzymes, 3d ed., vol. VIII. Academic Press, New York, N.Y.
20. Pittard, A. J. 1996. Biosynthesis of the aromatic amino acids, p. 458-484. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
21. Smith, D. R., L. A. Doucette-Stamm, C. Deloughery, H. Lee, J. Dubois, T. Aldredge, R. Bashirzadeh, D. Blakely, R. Cook, K. Gilbert, D. Harrison, L. Hoang, P. Keagle, W. Lumm, B. Potheir, D. Qiu, R. Spadafora, R. Vicaire, Y. Wang, J. Wierzbowski, R. Gibson, N. Jiwani, A. Caruso, D. Bush, H. Safer, D. Patwell, S. Prabhakar, S. McDougall, G. Shimer, A. Goyal, S. Pietrokovski, G. M. Church, C. J. Daniels, J. Mao, P. Rice, J. Nöiling, and J. N. Reeve. 1997. Complete genome sequence of Methanobacterium thermoautrophicum. J. Bacteriol. 179:7135-7155.
22. Thompson, H., A. Tersteegen, R. K. Thauer, and R. Hedderich. 1998. Two malate dehydrogenases in Methanobacterium thermoautotrophicum. Arch. Microbiol. 170:38-42.
23. Thurston-Solow, B., and R. H. White. 1997. The absolute stereochemistry of 2-hydroxyglutaric acid present in methanopterin. Chirality 9:678-680.
24. Umbarger, H. E. 1996. Biosynthesis of branched-chain amino acids, p. 442-457. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
25. Van Beelen, P., A. P. M. Strassen, J. W. G. Bosch, G. D. Vogels, W. Guijt, and C. A. G. Haasnoot. 1984. Elucidation of the structure of methanopterin, a coenzyme from Methanobacterium thermoautotrophicum, using two-dimensional nuclear-magnetic-resonance techniques. Eur. J. Biochem. 138:563-571.
26. Van Beelen, P., J. F. A. Labro, J. T. Labro, J. T. Keltjens, W. J. Geerts, G. D. Vogels, W. H. Laarhoven, and C. A. G. Haasnoot. 1984. Derivatives of methanopterin, a coenzyme involved in methanogenesis. Eur. J. Biochem. 139:359-365.
27. Weinstein, C. L., and O. W. Griffith. 1986. β-Sulfopyruvate: chemical and enzymatic syntheses and enzymatic assay. Anal Biochem. 156:154-160.
28. Weinstein, C. L., and O. W. Griffith. 1988. Cysteinesulfonate and β-sulfopyruvate metabolism: partitioning between decarboxylation, transamination, and reduction pathways. J. Biol. Chem. 263:3735-3743.
29. White, R. H. 1985. Biosynthesis of coenzyme M (2-mercaptoethanesulfonic acid). Biochemistry 24:6487-6493.
30. White, R. H. 1986. Intermediates in the biosynthesis of coenzyme M (2-mercaptoethanesulfonic acid). Biochemistry 25:5304-5308.
31. White, R. H. 1988. Characterization of the enzymatic conversion of sulfopyruvate and L-cysteine into coenzyme M (mercaptoethanesulfonic acid). Biochemistry 27:7458-7462.
32. White, R. H. 1988. Structural diversity in the methanofuran from different methanogenic bacteria. J. Bacteriol. 170:4544-4597.
33. White, R. H. 1990. Biosynthesis of methanopterin. Biochemistry 29:5397-5404.
34. White, R. H. 1993. Structure of the modified folates in the thermophilic archaebacteria Pyrococcus furiosus. Biochemistry 32:745-753.
35. White, R. H. 1993. Structures of the modified folates in the extremely thermophilic archaebacteria Thermococcus litoratis. J. Bacteriol. 175:3661-3663.
36. White, R. H. 1996. Biosynthesis of methanopterin. Biochemistry 35:3447-3456.
37. White, R. H. 1997. Structural characterization of modified folates in Archaea. Methods Enzymol. 281:391-401.
38. Wilks, H. M., D. J. Halsall, T. Atkinson, W. N. Chia, A. R. Clarke, and J. J. Hulbook. 1990. Designs for a broad substrate specificity keto acid dehydrogenase. Biochemistry 29:8587-8591.