Hetero-oligomeric glutamate dehydrogenase from Thermus thermophilus

Microbiology

Volumn 156, Issue 12, 2010, Pages 3801-3813

  Tomita, Takeo ^a   Miyazaki, Takashi ^a   Miyazaki, Junichi ^a   Kuzuyama, Tomohisa ^a   Nishiyama, Makoto ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b RIKEN SPring 8 Center   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GENE PRODUCT; GLUTAMATE DEHYDROGENASE; GLUTAMATE DEHYDROGENASE GDHA; GLUTAMATE DEHYDROGENASE GDHB; LEUCINE; OXIDOREDUCTASE; POLYHISTIDINE TAG; UNCLASSIFIED DRUG;

ALLOSTERISM; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BACTERIAL STRAIN; CATALYSIS; COMPLEX FORMATION; DEAMINATION; ENZYME ACTIVITY; ENZYME METABOLISM; GENE EXPRESSION; GENE FUNCTION; HYDROPHOBICITY; KINETICS; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; OXIDATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; REGULATOR GENE; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DIMERIZATION; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTAMATE DEHYDROGENASE; KINETICS; SEQUENCE HOMOLOGY, AMINO ACID; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 78650043632     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.042721-0     Document Type: Article

References (43)

1. +-specific glutamate dehydrogenase from Archaeoglobus fulgidus. Arch Microbiol 168, 536-539.
2. Abramoff, M. D., Magelhaes, P. J. & Ram, S. J. (2004). Image processing with ImageJ. Biophotonics International 11, 36-42.
3. Baggio, L. & Morrison, M. (1996). The NAD(P)H-utilizing glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by trans-acting gene(s) positioned downstream of gdhA. J Bacteriol 178, 7212-7220. (Pubitemid 26424636)
4. Baker, P. J., Britton, K. L., Rice, D. W., Rob, A. & Stillman, T. J. (1992). Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity. J Mol Biol 228, 662-671. (Pubitemid 23007582)
5. Barnes, L. D., Kuehn, G. D. & Atkinson, D. E. (1971). Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties. Biochemistry 10, 3939-3944.
6. Bolivar, J. M., Cava, F., Mateo, C., Rocha-Martin, J., Guisan, J. M., Berenguer, J. & Fernandez-Lafuente, R. (2008). Immobilization- stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus. Appl Microbiol Biotechnol 80, 49-58.
7. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
8. +-dependent enzyme. Comp Biochem Physiol A Mol Integr Physiol 131, 559-567.
9. +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae. J Biol Chem 267, 16417-16423.
10. + -isocitrate dehydrogenase with altered isocitrate binding sites: contribution of IDH1 and IDH2 subunits to regulation and catalysis. Biochemistry 32, 9323-9328.
11. Fang, J., Hsu, B. Y., MacMullen, C. M., Poncz, M., Smith, T. J. & Stanley, C. A. (2002). Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J 363, 81-87. (Pubitemid 34280615)
12. Gabriel, J. L., Zervos, P. R. & Plaut, G. W. (1986). Activity of purified NAD-specific isocitrate dehydrogenase at modulator and substrate concentrations approximating conditions in mitochondria. Metabolism 35, 661-667.
13. Goldenberg, D. P. (1989). Analysis of protein conformation by gel electrophoresis. In Protein Structure: a Practical Approach, pp. 225- 250. Edited by T. Creighton. Oxford: IRL Press.
14. +? FEBS Lett 582, 1816-1820.
15. Henne, A., Bruggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Lienard, T., Gohl, O. & other authors (2004). The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol 22, 547-553.
16. Hoseki, J., Okamoto, A., Takada, N., Suenaga, A., Futatsugi, N., Konagaya, A., Taiji, M., Yano, T., Kuramitsu, S. & Kagamiyama, H. (2003). Increased rigidity of domain structures enhances the stability of a mutant enzyme created by directed evolution. Biochemistry 42, 14469-14475.
17. +-specific isocitrate dehydrogenase. J Biol Chem 281, 16935-16942.
18. Hudson, R. C. & Daniel, R. M. (1993). L-Glutamate dehydrogenases: distribution, properties and mechanism. Comp Biochem Physiol B 106, 767-792. (Pubitemid 2016322)
19. Kawakami, R., Sakuraba, H. & Ohshima, T. (2007). Gene cloning and characterization of the very large NAD-dependent L-glutamate dehydrogenase from the psychrophile Janthinobacterium lividum, isolated from cold soil. J Bacteriol 189, 5626-5633. (Pubitemid 47206409)
20. Kobayashi, T., Higuchi, S., Kimura, K., Kudo, T. & Horikoshi, K. (1995). Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus. J Biochem 118, 587-592.
21. Koyama, Y., Hoshino, T., Tomizuka, N. & Furukawa, K. (1986). Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J Bacteriol 166, 338-340. (Pubitemid 16043323)
22. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
23. +-dependent glutamate dehydrogenase which is subject to allosteric regulation. J Bacteriol 183, 490-499.
24. Miñambres, B., Olivera, E. R., Jensen, R. A. & Luengo, J. M. (2000). A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. J Biol Chem 275, 39529-39542. (Pubitemid 32058980)
25. Mountain, A., McPherson, M. J., Baron, A. J. & Wootton, J. C. (1985). The Klebsiella aerogenes glutamate dehydrogenase (gdhA) gene: cloning, high-level expression and hybrid enzyme formation in Escherichia coli. Mol Gen Genet 199, 141-145.
26. Noor, S. & Punekar, N. S. (2005). Allosteric NADP-glutamate dehydrogenase from aspergilli: purification, characterization and implications for metabolic regulation at the carbon-nitrogen interface. Microbiology 151, 1409-1419.
27. Rice, D. W., Baker, P. J., Farrants, G. W. & Hornby, D. P. (1987). The crystal structure of glutamate dehydrogenase from Clostridium symbiosum at 0.6 nm resolution. Biochem J 242, 789-795.
28. Ruiz, J. L., Ferrer, J., Camacho, M. & Bonete, M. J. (1998). NAD-specific glutamate dehydrogenase from Thermus thermophilus HB8: purification and enzymatic properties. FEMS Microbiol Lett 159, 15-20.
29. +-glutamate dehydrogenase from Thermus thermophilus HB8. J Protein Chem 22, 295-301.
30. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
31. Smith, E. L., Austin, B. M., Blumenthal, K. M. & Nyc, J. F. (1975). Glutamate dehydrogenase. In The Enzymes, pp. 293-367. Edited by E. D. Boyer. New York: Academic Press.
32. Smith, T. J., Schmidt, T., Fang, J., Wu, J., Siuzdak, G. & Stanley, C. A. (2002). The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318, 765-777.
33. Stanley, C. A., Lieu, Y. K., Hsu, B. Y., Burlina, A. B., Greenberg, C. R., Hopwood, N. J., Perlman, K., Rich, B. H., Zammarchi, E. & Poncz, M. (1998). Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med 338, 1352-1357.
34. Stillman, T. J., Baker, P. J., Britton, K. L. & Rice, D. W. (1993). Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol 234, 1131-1139. (Pubitemid 24027242)
35. Syed, S. E. & Engel, P. C. (1984). Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits. Biochem J 222, 621-626.
36. Tanaka, T., Kawano, N. & Oshima, T. (1981). Cloning of 3- isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product. J Biochem 89, 677-682. (Pubitemid 11107972)
37. +-specific isocitrate dehydrogenase. J Biol Chem 283, 10872-10880.
38. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680.
39. Turano, F. J., Thakkar, S. S., Fang, T. & Weisemann, J. M. (1997). Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. Plant Physiol 113, 1329-1341. (Pubitemid 27210628)
40. Veronese, F. M., Nyc, J. F., Degani, Y., Brown, D. M. & Smith, E. L. (1974). Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. I. Purification and molecular properties. J Biol Chem 249, 7922-7928.
41. Watson, D. H. & Wootton, J. C. (1978). Subunit ratios of separated hybrid hexamers of Neurospora NADP-specific glutamate dehydrogenase containing complementing mutationally modified monomers. Biochem J 175, 1125-1133.
42. Wen, Z. & Morrison, M. (1996). The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B14 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth. Appl Environ Microbiol 62, 3826-3833.
43. West, D. J., Tuveson, R. W., Barratt, R. W. & Fincham, J. R. (1967). Allosteric effects in nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Neurospora. J Biol Chem 242, 2134-2138.