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Volumn 61, Issue 6, 2004, Pages 669-681

Glutamate syntliase: A fascinating pathway from L-glutamine to L-glutamate

Author keywords

Ammonia tunnel; Crystal structure; Electrospray ionization mass spectrometry; Glutamate synthase; Glutamine dependent amidotransferase; Multicomponent enzyme; Substrate channeling

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; FERREDOXIN; FLAVOPROTEIN; GLUTAMATE SYNTHASE; GLUTAMIC ACID; GLUTAMINE; IRON SULFUR PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRANSFERASE; LIGAND;

EID: 1842610703     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3316-0     Document Type: Review
Times cited : (82)

References (49)
  • 1
    • 0032951727 scopus 로고    scopus 로고
    • Glutamate synthase: A complex iron-sulfur flavoprotein
    • Vanoni M. A. and Curti B. (1999) Glutamate synthase: a complex iron-sulfur flavoprotein. Cell. Mol. Life Sci. 55: 617-638
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 617-638
    • Vanoni, M.A.1    Curti, B.2
  • 2
    • 0034482639 scopus 로고    scopus 로고
    • Cross-talk and ammonia channeling between active centers in the unexpected domain rearrangement of glutamate synthase
    • Camb.
    • Binda C., Bossi R. T., Wakatsuki S., Arzt S., Coda A., Curti B. et al. (2000) Cross-talk and ammonia channeling between active centers in the unexpected domain rearrangement of glutamate synthase. Structure (Camb.) 8: 1299-1308
    • (2000) Structure , vol.8 , pp. 1299-1308
    • Binda, C.1    Bossi, R.T.2    Wakatsuki, S.3    Arzt, S.4    Coda, A.5    Curti, B.6
  • 5
    • 0037172799 scopus 로고    scopus 로고
    • Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis sp. PCC 6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated a subunit
    • Ravasio S., Dossena L., Martin-Figueroa E., Florencio F. J., Mattevi A., Morandi P. et al. (2002) Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis sp. PCC 6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated a subunit. Biochemistry 41: 8120-8133
    • (2002) Biochemistry , vol.41 , pp. 8120-8133
    • Ravasio, S.1    Dossena, L.2    Martin-Figueroa, E.3    Florencio, F.J.4    Mattevi, A.5    Morandi, P.6
  • 6
    • 0026056062 scopus 로고
    • The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense
    • Vanoni M. A., Nuzzi L., Rescigno M., Zanetti G. and Curti B. (1991) The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense. Eur. J. Biochem. 202: 181-189
    • (1991) Eur. J. Biochem. , vol.202 , pp. 181-189
    • Vanoni, M.A.1    Nuzzi, L.2    Rescigno, M.3    Zanetti, G.4    Curti, B.5
  • 7
    • 0014774708 scopus 로고
    • Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route
    • Tempest D. W., Meers J. L. and Brown C. M. (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
  • 8
    • 84941103141 scopus 로고
    • The enzymology and metabolism of glutamine, glutamate and asparagine
    • Miflin B. J. and Lea P. J. (eds), Academic Press, New York
    • Lea P. J., Robinson S. A. and Stewart G. R. (1990) The enzymology and metabolism of glutamine, glutamate and asparagine. In: The Biochemistry of Plants, vol. 16, pp. 121-159, Miflin B. J. and Lea P. J. (eds), Academic Press, New York
    • (1990) The Biochemistry of Plants , vol.16 , pp. 121-159
    • Lea, P.J.1    Robinson, S.A.2    Stewart, G.R.3
  • 9
    • 0032007276 scopus 로고    scopus 로고
    • Glutamate synthase and nitrogen assimilation
    • Temple S. J., Vance C. P. and Gantt J. S. (1998) Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 3: 51-56
    • (1998) Trends Plant Sci. , vol.3 , pp. 51-56
    • Temple, S.J.1    Vance, C.P.2    Gantt, J.S.3
  • 10
    • 0001870422 scopus 로고    scopus 로고
    • Nitrogen metabolism in higher plants
    • Singh B. K. (ed.), Marcel Dekker, New York
    • Lea P. J. and Ireland R. J. (1999) Nitrogen metabolism in higher plants. In: Plant Amino Acids: Biochemistry and Biotechnology, pp. 1-47, Singh B. K. (ed.), Marcel Dekker, New York
    • (1999) Plant Amino Acids: Biochemistry and Biotechnology , pp. 1-47
    • Lea, P.J.1    Ireland, R.J.2
  • 11
    • 0000060736 scopus 로고    scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine
    • Neidhart F. C. (ed.), ASM Press, Washington, DC
    • Reitzer L. J. (1996) Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine. In: Escherichia coli and Salmonella: Cellular and Molecular Biology, vol. 1, pp. 391-407, Neidhart F. C. (ed.), ASM Press, Washington, DC
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 391-407
    • Reitzer, L.J.1
  • 12
    • 0029889726 scopus 로고    scopus 로고
    • Oxidation-reduction and transient kinetic studies of spinach ferredoxin-dependent glutamate synthase
    • Hirasawa M., Hurley J. K., Salamon Z., Tollin G. and Knaff, D. B. (1996) Oxidation-reduction and transient kinetic studies of spinach ferredoxin-dependent glutamate synthase. Arch. Biochim. Biophys. 330: 209-215
    • (1996) Arch. Biochim. Biophys. , vol.330 , pp. 209-215
    • Hirasawa, M.1    Hurley, J.K.2    Salamon, Z.3    Tollin, G.4    Knaff, D.B.5
  • 13
    • 0343517151 scopus 로고    scopus 로고
    • Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: Expression and assembly in Escherichia coli
    • Navarro F., Martin-Figueroa E., Candau P. and Florencio F. J. (2000) Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: expression and assembly in Escherichia coli. Arch. Biochem. Biophys. 379: 267-276
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 267-276
    • Navarro, F.1    Martin-Figueroa, E.2    Candau, P.3    Florencio, F.J.4
  • 14
    • 0032539513 scopus 로고    scopus 로고
    • The recombinant α subunit of glutamate synthase: Spectroscopic and catalytic properties
    • Vanoni M. A., Fischer F., Ravasio S., Verzotti E., Edmondson D. E., Hagen W. H. et al. (1998) The recombinant α subunit of glutamate synthase: spectroscopic and catalytic properties. Biochemistry 37: 1828-1838
    • (1998) Biochemistry , vol.37 , pp. 1828-1838
    • Vanoni, M.A.1    Fischer, F.2    Ravasio, S.3    Verzotti, E.4    Edmondson, D.E.5    Hagen, W.H.6
  • 15
    • 0029964615 scopus 로고    scopus 로고
    • Properties of the recombinant β subunit of glutamate synthase
    • Vanoni M. A., Verzotti E., Zanetti G. and Curti B. (1996) Properties of the recombinant β subunit of glutamate synthase. Eur. J. Biochem. 236: 937-946
    • (1996) Eur. J. Biochem. , vol.236 , pp. 937-946
    • Vanoni, M.A.1    Verzotti, E.2    Zanetti, G.3    Curti, B.4
  • 16
    • 0015560566 scopus 로고
    • The amidotransferases
    • Buchanan J. M. (1973) The amidotransferases. Adv. Enzymol. 39: 91-183
    • (1973) Adv. Enzymol. , vol.39 , pp. 91-183
    • Buchanan, J.M.1
  • 20
    • 0030613553 scopus 로고    scopus 로고
    • Gln amidotransferase: A novel heterodimeric enzyme required for correct decoding of glutamine codons during translation
    • Gln amidotransferase: a novel heterodimeric enzyme required for correct decoding of glutamine codons during translation. Proc. Natl. Acad. Sci. USA 94: 11819-11826.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11819-11826
    • Curnow, A.W.1    Hong, K.2    Yuan, R.3    Kim, S.4    Martins, O.5    Winkler, W.6
  • 21
    • 0030700490 scopus 로고    scopus 로고
    • Identification of active sites in amidases: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes
    • Kobayashi M., Fujiwara Y., Goda M., Komeda H. and Shimizu S. (1997) Identification of active sites in amidases: evolutionary relationship between amide bond-and peptide bond-cleaving enzymes. Proc. Natl. Acad. Sci. USA 94: 11986-11991
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11986-11991
    • Kobayashi, M.1    Fujiwara, Y.2    Goda, M.3    Komeda, H.4    Shimizu, S.5
  • 22
    • 0035106010 scopus 로고    scopus 로고
    • Phylogenetic analyses of two 'archaeal' genes in Thermotoga maritima reveal multiple transfers between archaea and bacteria
    • Nesbo C. L., L'Haridon S., Stetter K. O. and Doolittle W. F. (2001) Phylogenetic analyses of two 'archaeal' genes in Thermotoga maritima reveal multiple transfers between archaea and bacteria. Mol. Biol. Evol. 18: 362-375
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 362-375
    • Nesbo, C.L.1    L'Haridon, S.2    Stetter, K.O.3    Doolittle, W.F.4
  • 23
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
    • Krahn J. M., Kim J. H., Burns M. R., Parry R. J., Zalkin H. and Smith J. L. (1997) Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36: 11061-11068
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6
  • 25
    • 0033534161 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli asparagine synthetase B: A short journey from substrate to product
    • Larsen T. M., Boehlein S. K., Schuster S. M., Richards N. G., Thoden J. B., Holden H. M. et al. (1999) Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38: 16146-16157
    • (1999) Biochemistry , vol.38 , pp. 16146-16157
    • Larsen, T.M.1    Boehlein, S.K.2    Schuster, S.M.3    Richards, N.G.4    Thoden, J.B.5    Holden, H.M.6
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L. and Sander C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233: 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 0025278264 scopus 로고
    • Molecular structure of flavocytochrome b2 at 2.4 Å resolution
    • Xia Z. X. and Mathews F. S. (1990) Molecular structure of flavocytochrome b2 at 2.4 Å resolution. J. Mol. Biol. 212: 837-863
    • (1990) J. Mol. Biol. , vol.212 , pp. 837-863
    • Xia, Z.X.1    Mathews, F.S.2
  • 28
    • 0024962365 scopus 로고
    • Refined structure of spinach glycolate oxidase at 2 Å resolution
    • Lindqvist Y. (1989) Refined structure of spinach glycolate oxidase at 2 Å resolution. J. Mol. Biol. 209: 151-166
    • (1989) J. Mol. Biol. , vol.209 , pp. 151-166
    • Lindqvist, Y.1
  • 29
    • 0031568812 scopus 로고    scopus 로고
    • The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis
    • Camb.
    • Rowland P., Nielsen F. S., Jensen K. F. and Larsen S. (1997) The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis. Structure (Camb.) 5: 239-252
    • (1997) Structure , vol.5 , pp. 239-252
    • Rowland, P.1    Nielsen, F.S.2    Jensen, K.F.3    Larsen, S.4
  • 32
    • 0032544357 scopus 로고    scopus 로고
    • Crystal structure of polygalacturonase fcom Erwinia carotovora ssp. carotovora
    • Pickersgill R., Smith D., Worboys K. and Jenkins J. (1998) Crystal structure of polygalacturonase fcom Erwinia carotovora ssp. carotovora. J. Biol. Chem. 273: 24660-24664
    • (1998) J. Biol. Chem. , vol.273 , pp. 24660-24664
    • Pickersgill, R.1    Smith, D.2    Worboys, K.3    Jenkins, J.4
  • 34
    • 0041529609 scopus 로고    scopus 로고
    • Quaternary structure of Azospirillum brasilense NADPH-dependent glutamate synthase in solution as revealed by synchrotron radiation X-ray scattering
    • Petoukhov M. V., Svergun D. I., Kornarev P. V., Ravasio S., van den Heuvel R. H. H., Curti B. and Vanoni M. A. (2003) Quaternary structure of Azospirillum brasilense NADPH-dependent glutamate synthase in solution as revealed by synchrotron radiation X-ray scattering. J. Biol. Chem. 278: 29933-29939
    • (2003) J. Biol. Chem. , vol.278 , pp. 29933-29939
    • Petoukhov, M.V.1    Svergun, D.I.2    Kornarev, P.V.3    Ravasio, S.4    Van Den Heuvel, R.H.H.5    Curti, B.6    Vanoni, M.A.7
  • 35
    • 1842468172 scopus 로고    scopus 로고
    • Reference removed in proof
    • Reference removed in proof
  • 36
    • 0003887281 scopus 로고    scopus 로고
    • Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein
    • Stabile H., Curti B. and Vanoni M. A. (2000) Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein. Eur. J. Biochem. 267: 2720-2730
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2720-2730
    • Stabile, H.1    Curti, B.2    Vanoni, M.A.3
  • 37
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan J. A., Dodson G., Duggleby H. J., Moody P. C., Smith J. L., Tomchick D. R. et al. (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378: 416-419
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3    Moody, P.C.4    Smith, J.L.5    Tomchick, D.R.6
  • 38
    • 0030772416 scopus 로고    scopus 로고
    • Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosyl-pyrophosphate amidotransferase by nucleotides
    • Chen S., Tomchick D. R., Wolle D., Hu P., Smith J. L., Switzer R. L. et al. (1997) Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosyl-pyrophosphate amidotransferase by nucleotides. Biochemistry 36: 10718-10726
    • (1997) Biochemistry , vol.36 , pp. 10718-10726
    • Chen, S.1    Tomchick, D.R.2    Wolle, D.3    Hu, P.4    Smith, J.L.5    Switzer, R.L.6
  • 39
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim J. H., Krahn J. M., Tomchick D. R., Smith J. L. and Zalkin H. (1996) Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271, 15549-15557
    • (1996) J. Biol. Chem. , vol.271 , pp. 15549-15557
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 40
    • 0031941411 scopus 로고    scopus 로고
    • Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
    • Muchmore C. R. A., Krahn J. M., Kim J. H., Zalkin H. and Smith J. L. (1998) Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci. 7: 39-51
    • (1998) Protein Sci. , vol.7 , pp. 39-51
    • Muchmore, C.R.A.1    Krahn, J.M.2    Kim, J.H.3    Zalkin, H.4    Smith, J.L.5
  • 41
    • 0028762844 scopus 로고
    • Structure of the allosteric regulatory enzyme of purine biosynthesis
    • Smith J. L., Zaluzec E. J., Wery J.-P., Niu L., Switzer R., Zalkin H. et al. (1994) Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264: 1427-1433
    • (1994) Science , vol.264 , pp. 1427-1433
    • Smith, J.L.1    Zaluzec, E.J.2    Wery, J.-P.3    Niu, L.4    Switzer, R.5    Zalkin, H.6
  • 42
    • 0030586024 scopus 로고    scopus 로고
    • Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: Evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase
    • Camb.
    • Isupov M. N., Obmolova G., Butterworth S., Badet-Denisot M. A., Badet B., Polikarpov I. et al. (1996) Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure (Camb.) 4: 801-810
    • (1996) Structure , vol.4 , pp. 801-810
    • Isupov, M.N.1    Obmolova, G.2    Butterworth, S.3    Badet-Denisot, M.A.4    Badet, B.5    Polikarpov, I.6
  • 43
    • 0015944894 scopus 로고
    • 2 from bakers' yeast (L-lactate dehydrogenase). A double-headed enzyme
    • 2 from bakers' yeast (L-lactate dehydrogenase). A double-headed enzyme. Eur. J. Biochem. 41: 311-320
    • (1974) Eur. J. Biochem. , vol.41 , pp. 311-320
    • Jacq, C.1    Lederer, F.2
  • 44
  • 46
    • 0036175240 scopus 로고    scopus 로고
    • Structural evidence for ammonia tunneling across the (β/α)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex
    • Camb.
    • Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M. C., Sterner R. and Wilmanns M. (2002) Structural evidence for ammonia tunneling across the (β/α)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure (Camb.) 10: 185-93
    • (2002) Structure , vol.10 , pp. 185-193
    • Douangamath, A.1    Walker, M.2    Beismann-Driemeyer, S.3    Vega-Fernandez, M.C.4    Sterner, R.5    Wilmanns, M.6
  • 47
    • 0034503620 scopus 로고    scopus 로고
    • CONSCRIPT: A program for generating electron density isosurfaces from Fourier syntheses in protein crystallography
    • Lawrence M. C. and Bourke P. (2000) CONSCRIPT: a program for generating electron density isosurfaces from Fourier syntheses in protein crystallography. J. Appl. Cryst. 33: 990-991
    • (2000) J. Appl. Cryst. , vol.33 , pp. 990-991
    • Lawrence, M.C.1    Bourke, P.2
  • 48
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E. A. and Bacon D. J. (1997) Raster3D: photorealistic molecular graphics. Methods Enzymol. 277: 505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 49
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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