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Volumn 97, Issue 24, 2013, Pages 10373-10380

Interaction between DAHP synthase and chorismate mutase endows new regulation on DAHP synthase activity in Corynebacterium glutamicum

Author keywords

3 deoxy D arabino heptulosonate 7 phosphate (DAHP) synthase; Chorismate mutase (CM); Corynebacterium glutamicum; Regulation; Shikimate pathway

Indexed keywords

CHORISMATE MUTASE; CORYNEBACTERIUM GLUTAMICUM; REGULATION; SHIKIMATE PATHWAY; SYNTHASES;

EID: 84892364098     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-4806-0     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0023062219 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli
    • Davidson BE, Hudson GS (1987) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Methods Enzymol 142:440-450
    • (1987) Methods Enzymol , vol.142 , pp. 440-450
    • Davidson, B.E.1    Hudson, G.S.2
  • 3
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • De Lano WL (2002) Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 12:14-20
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 14-20
    • De Lano, W.1
  • 4
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon M (1953) The determination of enzyme inhibitor constants. Biochem J 55:170-171
    • (1953) Biochem J , vol.55 , pp. 170-171
    • Dixon, M.1
  • 5
    • 0028857259 scopus 로고
    • The shikimate pathway: Early steps in the biosynthesis of aromatic compounds
    • Herrmann KM (1995) The shikimate pathway: early steps in the biosynthesis of aromatic compounds. Plant Cell 7:907-919
    • (1995) Plant Cell , vol.7 , pp. 907-919
    • Herrmann, K.M.1
  • 6
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: Features and impacts on biotechnological processes
    • Ikeda M, Nakagawa S (2003) The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl Microbiol Biotechnol 62:99-109
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 7
    • 84856211626 scopus 로고    scopus 로고
    • Dynamic cross-talk among remote binding sites: The molecular basis for unusual synergistic allostery
    • Jiao W, Hutton RD, Cross PJ, Jameson GB, Parker EJ (2012) Dynamic cross-talk among remote binding sites: the molecular basis for unusual synergistic allostery. J Mol Biol 415:716-726
    • (2012) J Mol Biol , vol.415 , pp. 716-726
    • Jiao, W.1    Hutton, R.D.2    Cross, P.J.3    Jameson, G.B.4    Parker, E.J.5
  • 8
    • 0031001311 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase of Escherichia coli
    • Kikuchi Y, Tsujimoto K, Kurahashi O (1997) Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabinoheptulosonate-7- phosphate synthase of Escherichia coli. Appl Environ Microbiol 63:761-762
    • (1997) Appl Environ Microbiol , vol.63 , pp. 761-762
    • Kikuchi, Y.1    Tsujimoto, K.2    Kurahashi, O.3
  • 10
    • 71049121004 scopus 로고    scopus 로고
    • Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum
    • Li PP, Liu YJ, Liu SJ (2009) Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum. Microbiology 155:3382-3391
    • (2009) Microbiology , vol.155 , pp. 3382-3391
    • Li, P.P.1    Liu, Y.J.2    Liu, S.J.3
  • 11
    • 0035165362 scopus 로고    scopus 로고
    • Serine 187 is a crucial residue for allosteric regulation of Corynebacterium glutamicum 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Liao HF, Lin LL, Chien HR, Hsu WH (2001) Serine 187 is a crucial residue for allosteric regulation of Corynebacterium glutamicum 3-deoxy-D-arabino- heptulosonate 7-phosphate synthase. FEMS Microbiol Lett 194:59-64
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 59-64
    • Liao, H.F.1    Lin, L.L.2    Chien, H.R.3    Hsu, W.H.4
  • 12
    • 50949128449 scopus 로고    scopus 로고
    • Corynebacterium glutamicum contains 3-deoxy-D-arabinoheptulosonate 7-phosphate synthases that display novel biochemical features
    • Liu YJ, Li PP, Zhao KX, Wang BJ, Jiang CY, Drake HL, Liu SJ (2008) Corynebacterium glutamicum contains 3-deoxy-D-arabinoheptulosonate 7-phosphate synthases that display novel biochemical features. Appl Environ Microbiol 74:5497-5503
    • (2008) Appl Environ Microbiol , vol.74 , pp. 5497-5503
    • Liu, Y.J.1    Li, P.P.2    Zhao, K.X.3    Wang, B.J.4    Jiang, C.Y.5    Drake, H.L.6    Liu, S.J.7
  • 13
    • 0000605871 scopus 로고    scopus 로고
    • Biosynthesis of aromatic amino acids in Escherichia coli and Salmonella
    • American Society of Microbiology, Washington
    • Pittard AJ (1996) Biosynthesis of aromatic amino acids in Escherichia coli and Salmonella. Cellular and Molecular Biology. American Society of Microbiology, Washington, pp 458-484
    • (1996) Cellular and Molecular Biology , pp. 458-484
    • Pittard, A.J.1
  • 16
    • 67651147947 scopus 로고    scopus 로고
    • Structure and function of a complex between chorismate mutase and DAHP synthase: Efficiency boost for the junior partner
    • Sasso S, Okvist M, Roderer K, Gamper M, Codoni G, Krengel U, Kast P (2009) Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. EMBO J 28:2128-2142
    • (2009) EMBO J , vol.28 , pp. 2128-2142
    • Sasso, S.1    Okvist, M.2    Roderer, K.3    Gamper, M.4    Codoni, G.5    Krengel, U.6    Kast, P.7
  • 17
    • 37549047189 scopus 로고    scopus 로고
    • The two chorismate mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis: Biochemical analysis and limited regulation of promoter activity by aromatic amino acids
    • Schneider CZ, Parish T, Basso LA, Santos DS (2008) The two chorismate mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis: biochemical analysis and limited regulation of promoter activity by aromatic amino acids. J Bacteriol 190:122-134
    • (2008) J Bacteriol , vol.190 , pp. 122-134
    • Schneider, C.Z.1    Parish, T.2    Basso, L.A.3    Santos, D.S.4
  • 18
    • 0017114285 scopus 로고
    • 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli
    • Schoner R, Herrmann KM (1976) 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. J Biol Chem 251:5440-5447
    • (1976) J Biol Chem , vol.251 , pp. 5440-5447
    • Schoner, R.1    Herrmann, K.M.2
  • 19
    • 29344475991 scopus 로고    scopus 로고
    • Inhibitors of EPSP synthase, glutamine synthetase, and histidine synthesis
    • Row RM, Burton JD, Kuhr RJ eds, IOS Press, Amsterdam
    • Siehl DL (1997) Inhibitors of EPSP synthase, glutamine synthetase, and histidine synthesis. In: Row RM, Burton JD, Kuhr RJ (eds) Herbicide Activity: Toxicology, Biochemistry and Molecular Biology. IOS Press, Amsterdam, pp 37-67
    • (1997) Herbicide Activity: Toxicology, Biochemistry and Molecular Biology , pp. 37-67
    • Siehl, D.L.1
  • 20
    • 3342952192 scopus 로고    scopus 로고
    • Crystal structure of the reaction complex of 3-deoxy-D- arabinoheptulosonate-7-phosphate synthase from Thermotoga maritima refines the catalytic mechanism and indicates a new mechanism of allosteric regulation
    • Shumilin IA, Bauerle R, Wu J, Woodard RW, Kretsinger RH (2004) Crystal structure of the reaction complex of 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase from Thermotoga maritima refines the catalytic mechanism and indicates a new mechanism of allosteric regulation. J Mol Biol 341:455-466
    • (2004) J Mol Biol , vol.341 , pp. 455-466
    • Shumilin, I.A.1    Bauerle, R.2    Wu, J.3    Woodard, R.W.4    Kretsinger, R.H.5
  • 21
    • 0029133105 scopus 로고
    • The Corynebacterium xerosis composite transposon Tn5432 consists of two identical insertion sequences, designated IS1249, flanking the erythromycin resistance gene ermCX
    • Tauch A, Kassing F, Kalinowski J, Pühler A (1995) The Corynebacterium xerosis composite transposon Tn5432 consists of two identical insertion sequences, designated IS1249, flanking the erythromycin resistance gene ermCX. Plasmid 34:119-131
    • (1995) Plasmid , vol.34 , pp. 119-131
    • Tauch, A.1    Kassing, F.2    Kalinowski, J.3    Pühler, A.4
  • 22
    • 0036835575 scopus 로고    scopus 로고
    • Efficient electrotransformation of Corynebacterium diphtheriae with a mini-replicon derived from the Corynebacterium glutamicum plasmid pGA1
    • Tauch A, Kirchner O, Loffler B, Gotker S, Pühler A, Kalinowski J (2002) Efficient electrotransformation of Corynebacterium diphtheriae with a mini-replicon derived from the Corynebacterium glutamicum plasmid pGA1. Curr Microbiol 45:362-367
    • (2002) Curr Microbiol , vol.45 , pp. 362-367
    • Tauch, A.1    Kirchner, O.2    Loffler, B.3    Gotker, S.4    Pühler, A.5    Kalinowski, J.6
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 84892364183 scopus 로고    scopus 로고
    • A modified method of QuikChange site-directed mutagenesis
    • Wang RH, Chen RC, Liu RZ (2008) A modified method of QuikChange site-directed mutagenesis. J Xiamen Univ 47:z2
    • (2008) J Xiamen Univ , vol.47
    • Wang, R.H.1    Chen, R.C.2    Liu, R.Z.3
  • 25
    • 28444468809 scopus 로고    scopus 로고
    • The structure of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes
    • Webby CJ, Baker HM, Lott JS, Baker EN, Parker EJ (2005) The structure of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes. J Mol Biol 354:927-939
    • (2005) J Mol Biol , vol.354 , pp. 927-939
    • Webby, C.J.1    Baker, H.M.2    Lott, J.S.3    Baker, E.N.4    Parker, E.J.5
  • 26
    • 77957276754 scopus 로고    scopus 로고
    • Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis
    • Webby CJ, Jiao W, Hutton RD, Blackmore NJ, Baker HM, Baker EN, Jameson GB, Parker EJ (2010) Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis. J Biol Chem 285:30567-30576
    • (2010) J Biol Chem , vol.285 , pp. 30567-30576
    • Webby, C.J.1    Jiao, W.2    Hutton, R.D.3    Blackmore, N.J.4    Baker, H.M.5    Baker, E.N.6    Jameson, G.B.7    Parker, E.J.8
  • 27
    • 25144431811 scopus 로고    scopus 로고
    • Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: Resolution of two long-standing enigmas
    • Wu J, Sheflyan GY, Woodard RW (2005) Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas. Biochem J 390:583-590
    • (2005) Biochem J , vol.390 , pp. 583-590
    • Wu, J.1    Sheflyan, G.Y.2    Woodard, R.W.3


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