메뉴 건너뛰기




Volumn 254, Issue 6, 1997, Pages 635-642

Gene cloning, sequencing and enzymatic properties of glutamate synthase from the hyperthermophilic archaeon Pyrococcus sp. KOD1

Author keywords

Gene expression; Glutamate synthase; Hyperthermophilic archaea; Nitrogen assimilation; Pyrococcus

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; GLUTAMATE SYNTHASE; GLUTAMIC ACID;

EID: 0030919815     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050461     Document Type: Article
Times cited : (29)

References (35)
  • 1
    • 0000322050 scopus 로고
    • Purification and characterization of NADH-glutamate synthase from alfalfa root nodules
    • Anderson MP, Vance CP, Heichel GH, Miller SS (1989) Purification and characterization of NADH-glutamate synthase from alfalfa root nodules. Plant Physiol 90:351-358
    • (1989) Plant Physiol , vol.90 , pp. 351-358
    • Anderson, M.P.1    Vance, C.P.2    Heichel, G.H.3    Miller, S.S.4
  • 2
    • 0023957787 scopus 로고
    • Ammonium assimilation in Rhizobium phaseoli by the glutamine synthetase-alutamate synthase pathway
    • Bravo A, Mora J (1988) Ammonium assimilation in Rhizobium phaseoli by the glutamine synthetase-alutamate synthase pathway. J Bacteriol 170:980-984
    • (1988) J Bacteriol , vol.170 , pp. 980-984
    • Bravo, A.1    Mora, J.2
  • 4
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans: Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink G, Engel H, Vriend, G, Terpstra P, Witholt B (1990) Rubredoxin reductase of Pseudomonas oleovorans: structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J Mol Biol 212:135-142
    • (1990) J Mol Biol , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 5
    • 0030574267 scopus 로고    scopus 로고
    • The world of archaea: Genome analysis, evolution and thermostable enzymes
    • Fujiwara S, Okuyama S, Imanaka T (1996) The world of archaea: genome analysis, evolution and thermostable enzymes. Gene 179:165-170
    • (1996) Gene , vol.179 , pp. 165-170
    • Fujiwara, S.1    Okuyama, S.2    Imanaka, T.3
  • 7
    • 0019336813 scopus 로고
    • Regulation and function of glutamate synthase in Neurospora crassa
    • Hummelt G, Mora J (1980) Regulation and function of glutamate synthase in Neurospora crassa. Biochem Biophys Res Commun 96:1688-1694
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 1688-1694
    • Hummelt, G.1    Mora, J.2
  • 8
    • 0019838194 scopus 로고
    • Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis
    • Imanaka T, Tanaka T, Tsunekawa H, Aiba S (1981) Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis. J Bacteriol 147:776-786
    • (1981) J Bacteriol , vol.147 , pp. 776-786
    • Imanaka, T.1    Tanaka, T.2    Tsunekawa, H.3    Aiba, S.4
  • 9
    • 0028784140 scopus 로고
    • Aspartyl-tRNA synthetase of hyperthermophilic archaeon Pyrococcus sp. KOD1 has a chimerical structure of eukaryotic and bacterial enzymes
    • Imanaka T, Lee S, Takagi M, Fujiwara S (1995) Aspartyl-tRNA synthetase of hyperthermophilic archaeon Pyrococcus sp. KOD1 has a chimerical structure of eukaryotic and bacterial enzymes. Gene 164:153-156
    • (1995) Gene , vol.164 , pp. 153-156
    • Imanaka, T.1    Lee, S.2    Takagi, M.3    Fujiwara, S.4
  • 10
    • 0024358140 scopus 로고
    • Evolutionary relationship of archaebacteria, eubacteria and eukaryotes inferred from phylogenetic trees of duplicated genes
    • Iwabe N, Kuma K, Hasegawa M, Osawa S, Miyata T (1989) Evolutionary relationship of archaebacteria, eubacteria and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc Natl Acad Sci USA 86:9355-9359
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 11
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: prototype for a structurally novel flavoenzyme family. Science 251:60-66
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 12
    • 0025874679 scopus 로고
    • Spectroscopic evidence for a [3Fe-4S] cluster in spinach alulamate synthase
    • Knaff DB, Hirasawa M, Ameyibor E, Fu W, Johnson MK (1991) Spectroscopic evidence for a [3Fe-4S] cluster in spinach alulamate synthase. J Biol Chem 266:15080-15084
    • (1991) J Biol Chem , vol.266 , pp. 15080-15084
    • Knaff, D.B.1    Hirasawa, M.2    Ameyibor, E.3    Fu, W.4    Johnson, M.K.5
  • 13
    • 0026060723 scopus 로고
    • Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes
    • McKie JH, Douglas KT (1991) Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett 279:5-8
    • (1991) FEBS Lett , vol.279 , pp. 5-8
    • McKie, J.H.1    Douglas, K.T.2
  • 14
    • 0014909964 scopus 로고
    • Glutamine (amide): 2-oxoglutarate amino transferase oxido-reductase (NADP), an enzyme involved in the synthesis of glutamate by some bacteria
    • Meers JL, Tempest DW, Brown CM (1970) Glutamine (amide): 2-oxoglutarate amino transferase oxido-reductase (NADP), an enzyme involved in the synthesis of glutamate by some bacteria. J Gen Microbiol 64:187-194
    • (1970) J Gen Microbiol , vol.64 , pp. 187-194
    • Meers, J.L.1    Tempest, D.W.2    Brown, C.M.3
  • 15
    • 0022272463 scopus 로고
    • Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae
    • Meister A (1985) Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae. Methods Enzymol 113:327-337
    • (1985) Methods Enzymol , vol.113 , pp. 327-337
    • Meister, A.1
  • 16
    • 0042830094 scopus 로고
    • The role of glutamine in ammonium assimilation and reassimilation in plants
    • Mora J, Palacios R (eds) Academic Press. New York
    • Miflin BJ, Lea PJ, Wallsgrove RM (1980) The role of glutamine in ammonium assimilation and reassimilation in plants. In: Mora J, Palacios R (eds) Glutamine: metabolism, enzymology and regulation. Academic Press. New York, pp 213-234
    • (1980) Glutamine: Metabolism, Enzymology and Regulation , pp. 213-234
    • Miflin, B.J.1    Lea, P.J.2    Wallsgrove, R.M.3
  • 17
    • 0027946790 scopus 로고
    • Purification and characterization of a thermostable thiolprotease from a newly isolated hyperthermophilic Pyrococcus sp.
    • Morikawa M, Izawa Y, Rashid N, Hoaki T, Imanaka T (1994) Purification and characterization of a thermostable thiolprotease from a newly isolated hyperthermophilic Pyrococcus sp. Appl Environ Microbiol 60:4559-4566
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4559-4566
    • Morikawa, M.1    Izawa, Y.2    Rashid, N.3    Hoaki, T.4    Imanaka, T.5
  • 18
    • 0015186294 scopus 로고
    • The mechanism of ammonia assimilation in nitrogen-fixing bacteria
    • Nagatani H, Shimizu M, Valentine RC (1971) The mechanism of ammonia assimilation in nitrogen-fixing bacteria. Arch Microbiol 79:164-175
    • (1971) Arch Microbiol , vol.79 , pp. 164-175
    • Nagatani, H.1    Shimizu, M.2    Valentine, R.C.3
  • 20
    • 0027412184 scopus 로고
    • Glutamate synthase gene of the diazotroph Azospirillum brasilense: Cloning, sequencing, and analysis of functional domains
    • Pelanda R, Vanoni MA, Perego M, Piubelli L, Galizzi A, Curti B, Zanetti G (1993) Glutamate synthase gene of the diazotroph Azospirillum brasilense: cloning, sequencing, and analysis of functional domains. J Biol Chem 268:3099-3106
    • (1993) J Biol Chem , vol.268 , pp. 3099-3106
    • Pelanda, R.1    Vanoni, M.A.2    Perego, M.3    Piubelli, L.4    Galizzi, A.5    Curti, B.6    Zanetti, G.7
  • 21
    • 0026684272 scopus 로고
    • Evidence that eukaryotes and eocyte prokaryotes are immediate relatives
    • Rivera M, Lake JA (1992) Evidence that eukaryotes and eocyte prokaryotes are immediate relatives. Science 257:74-76
    • (1992) Science , vol.257 , pp. 74-76
    • Rivera, M.1    Lake, J.A.2
  • 23
    • 0025768404 scopus 로고
    • Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf
    • Sakakibara H, Watanabe M, Hase T, Sugiyama T (1991) Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf. J Biol Chem 266:2028-2035
    • (1991) J Biol Chem , vol.266 , pp. 2028-2035
    • Sakakibara, H.1    Watanabe, M.2    Hase, T.3    Sugiyama, T.4
  • 26
    • 0016744341 scopus 로고
    • Regulation of nitrogen metabolism in Escherichia coli and Klebsiella acrogenes: Studies with the continuous-culture technique
    • Senior PJ (1975) Regulation of nitrogen metabolism in Escherichia coli and Klebsiella acrogenes: studies with the continuous-culture technique. J Bacteriol 123:407-418
    • (1975) J Bacteriol , vol.123 , pp. 407-418
    • Senior, P.J.1
  • 27
    • 0001047421 scopus 로고
    • Glutamate synthase
    • Milling BJ (ed) Academic Press, New York
    • Stewart GR, Mann AF, Fentem PA (1980) Glutamate synthase. In: Milling BJ (ed) The biochemistry of plants, vol 5. Academic Press, New York, pp 309-327
    • (1980) The Biochemistry of Plants , vol.5 , pp. 309-327
    • Stewart, G.R.1    Mann, A.F.2    Fentem, P.A.3
  • 28
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW, Mollau BA (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Mollau, B.A.2
  • 29
    • 0000130160 scopus 로고
    • Glutamate synthase: Physiochemical and functional properties of different forms in higher plants and in other organisms
    • Suzuki A, Gadal P (1984) Glutamate synthase: physiochemical and functional properties of different forms in higher plants and in other organisms. Phys Veg 22:471-486
    • (1984) Phys Veg , vol.22 , pp. 471-486
    • Suzuki, A.1    Gadal, P.2
  • 30
    • 0014774708 scopus 로고
    • Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route
    • Tempest DW, Meers JL, Brown CM (1970) Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route. Biochem J 117:405-407
    • (1970) Biochem J , vol.117 , pp. 405-407
    • Tempest, D.W.1    Meers, J.L.2    Brown, C.M.3
  • 31
    • 0016293208 scopus 로고
    • Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase
    • Trotta PP, Platzer KEB, Haschemeyer RH, Meister A (1974) Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase. Proc Natl Acad Sci USA 71:4607-4611
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4607-4611
    • Trotta, P.P.1    Platzer, K.E.B.2    Haschemeyer, R.H.3    Meister, A.4
  • 32
    • 0026659227 scopus 로고
    • Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospririllum brasilense by absorption, circulation dichroism, and electron paramagnetic resonance spectroscopies
    • Vanoni MA, Edmondson DE, Zanetti G, Curti B (1992) Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospririllum brasilense by absorption, circulation dichroism, and electron paramagnetic resonance spectroscopies. Biochemistry 31:4613-4623
    • (1992) Biochemistry , vol.31 , pp. 4613-4623
    • Vanoni, M.A.1    Edmondson, D.E.2    Zanetti, G.3    Curti, B.4
  • 33
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins
    • Wierenga RK, De Maeyer MCH, Hol WGJ (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins. Biochemistry 24:1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 34
    • 0001271789 scopus 로고
    • Phylogenetic structure of the prokaryotic domain: The primary kingdoms
    • Woese CR, Fox GE (1977) Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proc Natl Acad Sci USA 74:5088-5090
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 35
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese CR, Kandler O, Wheelis ML (1990) Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci USA 87:4576-4579
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.