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Volumn 17, Issue 3, 2013, Pages 379-389

Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis

Author keywords

Biochemical characterization; Hyperthermophilic archaeon; l Glutamate dehydrogenases; Pyrobaculum calidifontis; Thermophilic enzyme

Indexed keywords

ARCHAEA; ESCHERICHIA COLI; PYROBACULUM; PYROBACULUM CALIDIFONTIS;

EID: 84876686889     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-013-0527-7     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100 degrees C
    • Adams MW (1993) Enzymes and proteins from organisms that grow near and above 100 degrees C. Annu Rev Microbiol 47: 627-658.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 627-658
    • Adams, M.W.1
  • 2
    • 0141939275 scopus 로고    scopus 로고
    • Pyrobaculum calidifontis sp. nov., a novel hyperthermophilic archaeon that grows in atmospheric air
    • Amo T, Paje ML, Inagaki A, Ezaki S, Atomi H, Imanaka T (2002) Pyrobaculum calidifontis sp. nov., a novel hyperthermophilic archaeon that grows in atmospheric air. Archaea 1: 113-121.
    • (2002) Archaea , vol.1 , pp. 113-121
    • Amo, T.1    Paje, M.L.2    Inagaki, A.3    Ezaki, S.4    Atomi, H.5    Imanaka, T.6
  • 3
    • 0036547771 scopus 로고    scopus 로고
    • Temperature dependence of kinetic parameters for hyperthermophilic glutamate dehydrogenase from Aeropyrum pernix K1
    • Bhuiya MW, Sakuraba H, Ohshima T (2002) Temperature dependence of kinetic parameters for hyperthermophilic glutamate dehydrogenase from Aeropyrum pernix K1. Biosci Biotechnol Biochem 66: 873-876.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 873-876
    • Bhuiya, M.W.1    Sakuraba, H.2    Ohshima, T.3
  • 4
    • 9644294199 scopus 로고    scopus 로고
    • The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum
    • Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H (2005) The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J Mol Biol 345: 325-337.
    • (2005) J Mol Biol , vol.345 , pp. 325-337
    • Bhuiya, M.W.1    Sakuraba, H.2    Ohshima, T.3    Imagawa, T.4    Katunuma, N.5    Tsuge, H.6
  • 5
  • 6
    • 0001259670 scopus 로고
    • A new glutamate dehydrogenase from Halobacterium halobium with different coenzyme specificity
    • Bonete MJ, Camacho ML, Cadenas E (1987) A new glutamate dehydrogenase from Halobacterium halobium with different coenzyme specificity. Int J Biochem 19: 1149-1155.
    • (1987) Int J Biochem , vol.19 , pp. 1149-1155
    • Bonete, M.J.1    Camacho, M.L.2    Cadenas, E.3
  • 7
    • 0029869306 scopus 로고    scopus 로고
    • NAD-glutamate dehydrogenase from Halobacterium halobium: inhibition and activation by TCA intermediates and amino acids
    • Bonete MJ, Perez-Pomares F, Ferrer J, Camacho ML (1996) NAD-glutamate dehydrogenase from Halobacterium halobium: inhibition and activation by TCA intermediates and amino acids. Biochim Biophys Acta 1289: 14-24.
    • (1996) Biochim Biophys Acta , vol.1289 , pp. 14-24
    • Bonete, M.J.1    Perez-Pomares, F.2    Ferrer, J.3    Camacho, M.L.4
  • 8
    • 0642369572 scopus 로고    scopus 로고
    • Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber
    • Bonete MJ, Pérez-Pomares F, Díaz S, Ferrer J, Oren A (2003) Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber. FEMS Microbiol Lett 226: 181-186.
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 181-186
    • Bonete, M.J.1    Pérez-Pomares, F.2    Díaz, S.3    Ferrer, J.4    Oren, A.5
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0026335162 scopus 로고
    • Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Consalvi V, Chiaraluce R, Politi L, Vaccaro R, De Rosa M, Scandurra R (1991b) Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Eur J Biochem 202: 1189-1196.
    • (1991) Eur J Biochem , vol.202 , pp. 1189-1196
    • Consalvi, V.1    Chiaraluce, R.2    Politi, L.3    Vaccaro, R.4    de Rosa, M.5    Scandurra, R.6
  • 14
    • 33645978366 scopus 로고    scopus 로고
    • Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei
    • Díaz S, Pérez-Pomares F, Pire C, Ferrer J, Bonete MJ (2006) Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei. Extremophiles 10: 105-115.
    • (2006) Extremophiles , vol.10 , pp. 105-115
    • Díaz, S.1    Pérez-Pomares, F.2    Pire, C.3    Ferrer, J.4    Bonete, M.J.5
  • 15
    • 0015181329 scopus 로고
    • Inactivation in vivo of glutamine synthetase and NAD-specific glutamate dehydrogenase: its role in the regulation of glutamine synthesis in yeasts
    • Ferguson AR, Sims AP (1971) Inactivation in vivo of glutamine synthetase and NAD-specific glutamate dehydrogenase: its role in the regulation of glutamine synthesis in yeasts. J Gen Microbiol 69: 423-427.
    • (1971) J Gen Microbiol , vol.69 , pp. 423-427
    • Ferguson, A.R.1    Sims, A.P.2
  • 16
    • 0030586251 scopus 로고    scopus 로고
    • NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability
    • Ferrer J, Pérez-Pomares F, Bonete MJ (1996) NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability. FEMS Microbiol Lett 141: 59-63.
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 59-63
    • Ferrer, J.1    Pérez-Pomares, F.2    Bonete, M.J.3
  • 17
    • 0024252148 scopus 로고
    • +-glutamate dehydrogenase in Clostridium botulinum 113B
    • +-glutamate dehydrogenase in Clostridium botulinum 113B. Arch Microbiol 150: 460-464.
    • (1988) Arch Microbiol , vol.150 , pp. 460-464
    • Hammer, B.A.1    Johnson, E.A.2
  • 20
    • 0036036621 scopus 로고    scopus 로고
    • Expression of two kinds of recombinant glutamate dehydrogenase from Aeropyrum pernix with different N-terminal sequence length in Escherichia coli
    • Helianti I, Morita Y, Murakami Y, Yokoyama K, Tamiya E (2002) Expression of two kinds of recombinant glutamate dehydrogenase from Aeropyrum pernix with different N-terminal sequence length in Escherichia coli. Appl Microbiol Biotechnol 59: 462-466.
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 462-466
    • Helianti, I.1    Morita, Y.2    Murakami, Y.3    Yokoyama, K.4    Tamiya, E.5
  • 21
    • 17044371911 scopus 로고    scopus 로고
    • The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum
    • Ingoldsby LM, Geoghegan KF, Hayden BM, Engel PC (2005) The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum. Gene 349: 237-244.
    • (2005) Gene , vol.349 , pp. 237-244
    • Ingoldsby, L.M.1    Geoghegan, K.F.2    Hayden, B.M.3    Engel, P.C.4
  • 22
    • 34547627159 scopus 로고    scopus 로고
    • Gene cloning and characterization of the very large NAD-dependent l-glutamate dehydrogenase from the psychrophile Janthinobacterium lividum, isolated from cold soil
    • 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.
    • (2007) J Bacteriol , vol.189 , pp. 5626-5633
    • Kawakami, R.1    Sakuraba, H.2    Ohshima, T.3
  • 23
    • 0017616447 scopus 로고
    • Glutamate dehydrogenase from Bacillus subtilis PCI 219. I. Purification and properties
    • Kimura K, Miyakawa A, Imai T, Sasakawa T (1977) Glutamate dehydrogenase from Bacillus subtilis PCI 219. I. Purification and properties. J Biochem 81: 467-476.
    • (1977) J Biochem , vol.81 , pp. 467-476
    • Kimura, K.1    Miyakawa, A.2    Imai, T.3    Sasakawa, T.4
  • 24
    • 0014719188 scopus 로고
    • NAD and NADP-dependent glutamate dehydrogenase in Hydrogenomonas H16
    • Krämer J (1970) NAD and NADP-dependent glutamate dehydrogenase in Hydrogenomonas H16. Arch Mikrobiol 71: 226-234.
    • (1970) Arch Mikrobiol , vol.71 , pp. 226-234
    • Krämer, J.1
  • 25
    • 0031744984 scopus 로고    scopus 로고
    • Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents
    • Kujo C, Ohshima T (1998) Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents. Appl Environ Microbiol 64: 2152-2157.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2152-2157
    • Kujo, C.1    Ohshima, T.2
  • 26
    • 0036549657 scopus 로고    scopus 로고
    • Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis: cloning and comparison with two marine hyperthermophilic GDHs
    • Lee MK, González JM, Robb F (2002) Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis: cloning and comparison with two marine hyperthermophilic GDHs. Extremophiles 6: 151-159.
    • (2002) Extremophiles , vol.6 , pp. 151-159
    • Lee, M.K.1    González, J.M.2    Robb, F.3
  • 27
    • 0014232647 scopus 로고
    • Evidence for two species of glutamate dehydrogenases in Thiobacillus novellus
    • LéJohn HB, McCrea BE (1968) Evidence for two species of glutamate dehydrogenases in Thiobacillus novellus. J Bacteriol 95: 87-94.
    • (1968) J Bacteriol , vol.95 , pp. 87-94
    • LéJohn, H.B.1    McCrea, B.E.2
  • 28
    • 84857804808 scopus 로고    scopus 로고
    • The structure and allosteric regulation of mammalian glutamate dehydrogenase
    • Li M, Li C, Allen A, Stanley CA, Smith TJ (2012) The structure and allosteric regulation of mammalian glutamate dehydrogenase. Arch Biochem Biophys 519: 69-80.
    • (2012) Arch Biochem Biophys , vol.519 , pp. 69-80
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 31
    • 0035156804 scopus 로고    scopus 로고
    • +-dependent glutamate dehydrogenase which is subject to allosteric regulation
    • +-dependent glutamate dehydrogenase which is subject to allosteric regulation. J Bacteriol 183: 490-499.
    • (2001) J Bacteriol , vol.183 , pp. 490-499
    • Lu, C.D.1    Abdelal, A.T.2
  • 32
    • 0028069713 scopus 로고
    • Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
    • Ma K, Robb FT, Adams MW (1994) Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis. Appl Environ Microbiol 60: 562-568.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 562-568
    • Ma, K.1    Robb, F.T.2    Adams, M.W.3
  • 33
    • 0034671553 scopus 로고    scopus 로고
    • A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus
    • Miñambres B, Olivera ER, Jensen RA, Luengo JM (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.
    • (2000) J Biol Chem , vol.275 , pp. 39529-39542
    • Miñambres, B.1    Olivera, E.R.2    Jensen, R.A.3    Luengo, J.M.4
  • 34
    • 84860834514 scopus 로고    scopus 로고
    • +-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014
    • +-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014. Extremophiles 16: 463-476.
    • (2012) Extremophiles , vol.16 , pp. 463-476
    • Munawar, N.1    Engel, P.C.2
  • 35
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: an on-line retrieval system for biological sequence banks
    • Perrière G, Gouy M (1996) WWW-query: an on-line retrieval system for biological sequence banks. Biochimie 78: 364-369.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 36
    • 0016697801 scopus 로고
    • Glutamate dehydrogenase from Escherichia coli: purification and properties
    • Sakamoto N, Kotre AM, Savageau MA (1975) Glutamate dehydrogenase from Escherichia coli: purification and properties. J Bacteriol 124: 775-783.
    • (1975) J Bacteriol , vol.124 , pp. 775-783
    • Sakamoto, N.1    Kotre, A.M.2    Savageau, M.A.3
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (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.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 80054814738 scopus 로고    scopus 로고
    • Structural basis for leucine-induced allosteric activation of glutamate dehydrogenase
    • Tomita T, Kuzuyama T, Nishiyama M (2011) Structural basis for leucine-induced allosteric activation of glutamate dehydrogenase. J Biol Chem 286: 37406-37413.
    • (2011) J Biol Chem , vol.286 , pp. 37406-37413
    • Tomita, T.1    Kuzuyama, T.2    Nishiyama, M.3
  • 41
    • 0037373480 scopus 로고    scopus 로고
    • Heat effect on the structure and activity of the recombinant glutamate dehydrogenase from a hyperthermophilic archaeon Pyrococcus horikoshii
    • Wang S, Feng Y, Zhang Z, Zheng B, Li N, Cao S, Matsui I, Kosugi Y (2003) Heat effect on the structure and activity of the recombinant glutamate dehydrogenase from a hyperthermophilic archaeon Pyrococcus horikoshii. Arch Biochem Biophys 411: 56-62.
    • (2003) Arch Biochem Biophys , vol.411 , pp. 56-62
    • Wang, S.1    Feng, Y.2    Zhang, Z.3    Zheng, B.4    Li, N.5    Cao, S.6    Matsui, I.7    Kosugi, Y.8


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