메뉴 건너뛰기




Volumn 2, Issue JANUARY, 2012, Pages

Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme

Author keywords

Enzyme kinetics; Mycobacterium tuberculosis; Pentose pathway; Transketolase; X ray crystallography

Indexed keywords

MYCOBACTERIUM TUBERCULOSIS;

EID: 84864196438     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.110026     Document Type: Article
Times cited : (32)

References (64)
  • 1
    • 33644991496 scopus 로고    scopus 로고
    • Global epidemiology of tuberculosis
    • doi:10.1016/S0140-6736 (06)68384-0
    • Dye C. 2006 Global epidemiology of tuberculosis. Lancet 367, 938-940. (doi:10.1016/S0140-6736 (06)68384-0)
    • (2006) Lancet , vol.367 , pp. 938-940
    • Dye, C.1
  • 2
    • 57349144559 scopus 로고    scopus 로고
    • Treatment outcomes and longterm survival in patients with extensively drugresistant tuberculosis
    • doi:10.1164/rccm.200801-132OC
    • Kim DH et al. 2008 Treatment outcomes and longterm survival in patients with extensively drugresistant tuberculosis. Am. J. Respir. Crit. Care Med. 178, 1075-1082. (doi:10.1164/rccm.200801-132OC)
    • (2008) Am. J. Respir. Crit. Care Med. , vol.178 , pp. 1075-1082
    • Kim, D.H.1
  • 4
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Sassetti CM, Boyd DH, Rubin EJ. 2003 Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48, 77-84. (doi:10.1046/j.1365-2958. 2003.03425.x) (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 6
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • doi:10.1074/mcp. M300060-MCP200
    • Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X. 2003 Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2, 1284-1296. (doi:10.1074/mcp. M300060-MCP200)
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 7
    • 34249701192 scopus 로고    scopus 로고
    • Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv
    • DOI 10.1002/pmic.200600853
    • Malen H, Berven FS, Fladmark KE, Wiker HG. 2007 Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7, 1702-1718. (doi:10.1002/pmic.200600853) (Pubitemid 46841830)
    • (2007) Proteomics , vol.7 , Issue.10 , pp. 1702-1718
    • Malen, H.1    Berven, F.S.2    Fladmark, K.E.3    Wiker, H.G.4
  • 8
    • 23044500717 scopus 로고    scopus 로고
    • Mutant kinesin-2 motor subunits increase chromosome loss
    • DOI 10.1091/mbc.
    • Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X. 2005 Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16, 396-404. (doi:10.1091/mbc. E04-04-0329) (Pubitemid 41077089)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.8 , pp. 3810-3820
    • Miller, M.S.1    Esparza, J.M.2    Lippa, A.M.3    Lux III, F.G.4    Cole, D.G.5    Dutcher, S.K.6
  • 9
    • 0033666855 scopus 로고    scopus 로고
    • Towards the proteome of Mycobacterium tuberculosis
    • doi:10.1002/1522-2683(200011)21: 17 3740::AID-ELPS3740.3.0.CO;2-3
    • Rosenkrands I, King A, Weldingh K, Moniatte M, Moertz E, Andersen P. 2000 Towards the proteome of Mycobacterium tuberculosis. Electrophoresis 21, 3740-3756. (doi:10.1002/1522-2683(200011)21: 17, 3740::AID-ELPS3740.3.0.CO;2-3)
    • (2000) Electrophoresis , vol.21 , pp. 3740-3756
    • Rosenkrands, I.1    King, A.2    Weldingh, K.3    Moniatte, M.4    Moertz, E.5    Andersen, P.6
  • 10
    • 0032844939 scopus 로고    scopus 로고
    • Use of fluorescence induction and sucrose counterselection to identify Mycobacterium tuberculosis genes expressed within host cells
    • Triccas JA, Berthet FX, Pelicic V, Gicquel B. 1999 Use of fluorescence induction and sucrose counterselection to identify Mycobacterium tuberculosis genes expressed within host cells. Microbiology 145, 2923-2930. (Pubitemid 29485907)
    • (1999) Microbiology , vol.145 , Issue.10 , pp. 2923-2930
    • Triccas, J.A.1    Berthet, F.-X.2    Pelicic, V.3    Gicquel, B.4
  • 11
    • 77957818235 scopus 로고    scopus 로고
    • The crystal structure of human transketolase and new insights into its mode of action
    • doi:10.1074/jbc.M110.149955
    • Mitschke L, Parthier C, Schroder-Tittmann K, Coy J, Ludtke S, Tittmann K. 2010 The crystal structure of human transketolase and new insights into its mode of action. J. Biol. Chem. 285, 31 559-31 570. (doi:10.1074/jbc.M110.149955)
    • (2010) J. Biol. Chem. , vol.285 , pp. 31559-31570
    • Mitschke, L.1    Parthier, C.2    Schroder-Tittmann, K.3    Coy, J.4    Ludtke, S.5    Tittmann, K.6
  • 13
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution
    • Lindqvist Y, Schneider G, Ermler U, Sundstrom M. 1992 Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. EMBO J. 11, 2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 14
    • 0032537478 scopus 로고    scopus 로고
    • Crystallography and mutagenesis of transketolase: Mechanistic implications for enzymatic thiamin catalysis
    • DOI 10.1016/S0167-4838(98)00082-X, PII S016748389800082X
    • Schneider G, Lindqvist Y. 1998 Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis. Biochim. Biophys. Acta 1385, 387-398. (doi:10.1016/S0167-4838(98) 00082-X) (Pubitemid 28310802)
    • (1998) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1385 , Issue.2 , pp. 387-398
    • Schneider, G.1    Lindqvist, Y.2
  • 15
    • 0031455533 scopus 로고    scopus 로고
    • Identification of catalytically important residues in yeast transketolase
    • DOI 10.1021/bi971606b
    • Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G. 1997 Identification of catalytically important residues in yeast transketolase. Biochemistry 36, 15 643-15 649. (doi:10.1021/bi971606b) (Pubitemid 28027362)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15643-15649
    • Wikner, C.1    Nilsson, U.2    Meshalkina, L.3    Udekwu, C.4    Lindqvist, Y.5    Schneider, G.6
  • 16
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
    • doi:10.1111/j.1432-1033.1995.0525h.x
    • Sprenger GA, Schorken U, Sprenger G, Sahm H. 1995 Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur. J. Biochem. 230, 525-532. (doi:10.1111/j.1432-1033.1995.0525h.x)
    • (1995) Eur. J. Biochem. , vol.230 , pp. 525-532
    • Sprenger, G.A.1    Schorken, U.2    Sprenger, G.3    Sahm, H.4
  • 18
    • 0030294746 scopus 로고    scopus 로고
    • Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts
    • Flechner A, Dressen U, Westhoff P, Henze K, Schnarrenberger C, Martin W. 1996 Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts. Plant Mol. Biol. 32, 475-484. (doi:10.1007/BF00019099) (Pubitemid 27016980)
    • (1996) Plant Molecular Biology , vol.32 , Issue.3 , pp. 475-484
    • Flechner, A.1    Dressen, U.2    Westhoff, P.3    Henze, K.4    Schnarrenberger, C.5    Martin, W.6
  • 19
    • 43749123900 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Plasmodium falciparum transketolase
    • DOI 10.1016/j.molbiopara.2008.03.005, PII S0166685108000686
    • Joshi S, Singh AR, Kumar A, Misra PC, Siddiqi MI, Saxena JK. 2008 Molecular cloning and characterization of Plasmodium falciparum transketolase. Mol. Biochem. Parasitol. 160, 32-41. (doi:10.1016/j.molbiopara. 2008.03.005) (Pubitemid 351694357)
    • (2008) Molecular and Biochemical Parasitology , vol.160 , Issue.1 , pp. 32-41
    • Joshi, S.1    Singh, A.R.2    Kumar, A.3    Misra, P.C.4    Siddiqi, M.I.5    Saxena, J.K.6
  • 20
    • 0035844254 scopus 로고    scopus 로고
    • Examination of donor substrate conversion in yeast transketolase
    • doi:10.1074/jbc.M007936200
    • Fiedler E, Golbik R, Schneider G, Tittmann K, Neef H, Konig S, Hubner G. 2001 Examination of donor substrate conversion in yeast transketolase. J. Biol. Chem. 276, 16 051-16 058. (doi:10.1074/jbc. M007936200)
    • (2001) J. Biol. Chem. , vol.276 , pp. 16051-16058
    • Fiedler, E.1    Golbik, R.2    Schneider, G.3    Tittmann, K.4    Neef, H.5    Konig, S.6    Hubner, G.7
  • 21
    • 0020393767 scopus 로고
    • Transketolase from yeast, rat liver, and pig liver
    • doi:10.1016/S0076-6879(82)90128-8
    • Kochetov GA. 1982 Transketolase from yeast, rat liver, and pig liver. Methods Enzymol. 90, 209-223. (doi:10.1016/S0076-6879(82)90128-8)
    • (1982) Methods Enzymol. , vol.90 , pp. 209-223
    • Kochetov, G.A.1
  • 22
    • 0032423288 scopus 로고    scopus 로고
    • Properties and functions of the thiamin diphosphate dependent enzyme transketolase
    • DOI 10.1016/S1357-2725(98)00095-8, PII S1357272598000958
    • Schenk G, Duggleby RG, Nixon PF. 1998 Properties and functions of the thiamin diphosphate dependent enzyme transketolase. Int. J. Biochem. Cell Biol. 30, 1297-1318. (doi:10.1016/S1357-2725(98)00095-8) (Pubitemid 29002974)
    • (1998) International Journal of Biochemistry and Cell Biology , vol.30 , Issue.12 , pp. 1297-1318
    • Schenk, G.1    Duggleby, R.G.2    Nixon, P.F.3
  • 23
    • 0028131269 scopus 로고
    • 6) as well as the aromatic amino acids and vitamins for growth
    • Zhao G, Winkler ME. 1994 An Escherichia coli K-12 tktA tktB mutant deficient in transketolase activity requires pyridoxine (vitamin B6) as well as the aromatic amino acids and vitamins for growth. J. Bacteriol. 176, 6134-6138. (Pubitemid 24309955)
    • (1994) Journal of Bacteriology , vol.176 , Issue.19 , pp. 6134-6138
    • Zhao, G.1    Winkler, M.E.2
  • 24
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Aresolution
    • DOI 10.1006/jmbi.1994.1299
    • Nikkola M, Lindqvist Y, Schneider G. 1994 Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J. Mol. Biol. 238, 387-404. (doi:10.1006/jmbi.1994.1299) (Pubitemid 24154719)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.3 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 25
    • 35648979411 scopus 로고    scopus 로고
    • Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate
    • DOI 10.1021/bi700844m
    • Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G., Weiss MS, Friedemann R, Wille G, Tittmann K. 2007 Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46, 12 037-12 052. (doi:10.1021/bi700844m) (Pubitemid 350022361)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12037-12052
    • Asztalos, P.1    Parthier, C.2    Golbik, R.3    Kleinschmidt, M.4    Hubner, G.5    Weiss, M.S.6    Friedemann, R.7    Wille, G.8    Tittmann, K.9
  • 26
    • 4544269846 scopus 로고    scopus 로고
    • Transketolase from Leishmania mexicana has a dual subcellular localization
    • DOI 10.1042/BJ20040459
    • Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP. 2004 Transketolase from Leishmania mexicana has a dual subcellular localization. Biochem. J. 382, 759-767. (doi:10.1042/BJ20040459) (Pubitemid 39243943)
    • (2004) Biochemical Journal , vol.382 , Issue.2 , pp. 759-767
    • Veitch, N.J.1    Maugeri, D.A.2    Cazzulo, J.J.3    Lindqvist, Y.4    Barrett, M.P.5
  • 28
    • 38649093031 scopus 로고    scopus 로고
    • Evolutionary analysis of the TPP-dependent enzyme family
    • doi:10.1007/s00239-007-9056-9062
    • Costelloe SJ, Ward JM, Dalby PA. 2008 Evolutionary analysis of the TPP-dependent enzyme family. J. Mol. Evol. 66, 36-49. (doi:10.1007/s00239-007- 9056-2)
    • (2008) J. Mol. Evol. , vol.66 , pp. 36-49
    • Costelloe, S.J.1    Ward, J.M.2    Dalby, P.A.3
  • 29
    • 0020755112 scopus 로고
    • Function of the arginine residue in the active center of baker's yeast transketolase
    • Usmanov RA, Kochetov GA. 1983 Function of the arginine residue in the active center of baker's yeast transketolase. Biokhimiia 48, 772-781.
    • (1983) Biokhimiia , vol.48 , pp. 772-781
    • Usmanov, R.A.1    Kochetov, G.A.2
  • 30
    • 0000288426 scopus 로고
    • Substrate specificity and carbohydrate synthesis using transketolase
    • doi:10.1021/jo00048a023
    • Kobori Y, Myles DC, Whitesides GM. 1992 Substrate specificity and carbohydrate synthesis using transketolase. J. Organ. Chem. 57, 5899-5907. (doi:10.1021/jo00048a023)
    • (1992) J. Organ. Chem. , vol.57 , pp. 5899-5907
    • Kobori, Y.1    Myles, D.C.2    Whitesides, G.M.3
  • 31
    • 43549101762 scopus 로고    scopus 로고
    • Biosynthesis of D-arabinose in mycobacteria - A novel bacterial pathway with implications for antimycobacterial therapy
    • DOI 10.1111/j.1742-4658.2008.06395.x
    • Wolucka BA. 2008 Biosynthesis of D-arabinose in mycobacteria-a novel bacterial pathway with implications for antimycobacterial therapy. FEBS J. 275, 2691-2711. (doi:10.1111/j.1742-4658.2008. 06395.x) (Pubitemid 351678659)
    • (2008) FEBS Journal , vol.275 , Issue.11 , pp. 2691-2711
    • Wolucka, B.A.1
  • 32
    • 1542396974 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site
    • DOI 10.1016/j.jmb.2003.11.021, PII S0022283603014165
    • Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL. 2004 Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site. J. Mol. Biol. 335, 799-809. (doi:10.1016/j. jmb.2003.11.021) (Pubitemid 38352821)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 799-809
    • Roos, A.K.1    Andersson, C.E.2    Bergfors, T.3    Jacobsson, M.4    Karlen, A.5    Unge, T.6    Jones, T.A.7    Mowbray, S.L.8
  • 33
    • 33751583815 scopus 로고    scopus 로고
    • Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis
    • DOI 10.1021/bi061874m
    • Argyrou A, Jin L, Siconilfi-Baez L, Angeletti RH, Blanchard JS. 2006 Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis. Biochemistry 45, 13 947-13 953. (doi:10.1021/bi061874m) (Pubitemid 44846183)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 13947-13953
    • Argyrou, A.1    Jin, L.2    Siconilfi-Baez, L.3    Angeletti, R.H.4    Blanchard, J.S.5
  • 35
    • 0032486197 scopus 로고    scopus 로고
    • Inhibition of a Mycobacterium tuberculosis beta-Ketoacyl ACP synthase by isoniazid
    • DOI 10.1126/science.280.5369.1607
    • Mdluli K, Slayden RA, Zhu Y, Ramaswamy S, Pan X, Mead D, Crane DD, Musser JM, Barry 3rd, CE. 1998 Inhibition of a Mycobacterium tuberculosis betaketoacyl ACP synthase by isoniazid. Science 280, 1607-1610. (doi:10.1126/science.280. 5369.1607) (Pubitemid 28277706)
    • (1998) Science , vol.280 , Issue.5369 , pp. 1607-1610
    • Mdluli, K.1    Slayden, R.A.2    Zhu, Y.3    Ramaswamy, S.4    Pan, X.5    Mead, D.6    Crane, D.D.7    Musser, J.M.8    Barry III, C.E.9
  • 37
    • 0030872573 scopus 로고    scopus 로고
    • Overexpression of the D-alanine racemase gene confers resistance to D- cycloserine in Mycobacterium smegmatis
    • Caceres NE, Harris NB, Wellehan JF, Feng Z, Kapur V, Barletta RG. 1997 Overexpression of the D-alanine racemase gene confers resistance to D-cycloserine in Mycobacterium smegmatis. J. Bacteriol. 179, 5046-5055. (Pubitemid 27340537)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5046-5055
    • Caceres, N.E.1    Harris, N.B.2    Wellehan, J.F.3    Feng, Z.4    Kapur, V.5    Barletta, R.G.6
  • 38
    • 0014589983 scopus 로고
    • Susceptibility of mycobacterial D-alanyl-D-alanine synthetase to D-cycloserine
    • David HL, Takayama K, Goldman DS. 1969 Susceptibility of mycobacterial D-alanyl-D-alanine synthetase to D-cycloserine. Am. Rev. Respir. Dis. 100, 579-581.
    • (1969) Am. Rev. Respir. Dis. , vol.100 , pp. 579-581
    • David, H.L.1    Takayama, K.2    Goldman, D.S.3
  • 39
    • 65649096556 scopus 로고    scopus 로고
    • Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis
    • doi:10.1126/science.1171583
    • Makarov V et al. 2009 Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science 324, 801-804. (doi:10.1126/science. 1171583)
    • (2009) Science , vol.324 , pp. 801-804
    • Makarov, V.1
  • 42
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006 The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. (doi:10.1093/bioinfor matics/bti770) (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 43
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • doi:10.1107/S0108767390010224
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991 Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119. (doi:10.1107/S0108767390010224)
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • DOI 10.1038/nsb0497-269
    • Diederichs K, Karplus PA. 1997 Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275. (doi:10.1038/nsb0497-269) (Pubitemid 27157198)
    • (1997) Nature Structural Biology , vol.4 , Issue.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 48
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • DOI 10.1093/bioinformatics/15.4.305
    • Gouet P, Courcelle E, Stuart DI, Metoz F. 1999 ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308. (doi:10. 1093/bioinformatic//15.4.305) (Pubitemid 29213756)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 49
    • 0020349156 scopus 로고
    • Determination of transketolase activity via ferricyanide reduction
    • doi:10.1016/S0076-6879(82)89009-5
    • Kochetov GA. 1982 Determination of transketolase activity via ferricyanide reduction. Methods Enzymol. 89, 43-44. (doi:10.1016/S0076-6879(82) 89009-5)
    • (1982) Methods Enzymol. , vol.89 , pp. 43-44
    • Kochetov, G.A.1
  • 50
    • 0031001809 scopus 로고    scopus 로고
    • Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme, transketolase
    • DOI 10.1007/PL00006179
    • Schenk G, Layfield R, Candy JM, Duggleby RG, Nixon PF. 1997 Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme, transketolase. J. Mol. Evol. 44, 552-572. (doi:10. 1007/PL00006179) (Pubitemid 27227501)
    • (1997) Journal of Molecular Evolution , vol.44 , Issue.5 , pp. 552-572
    • Schenk, G.1    Layfield, R.2    Candy, J.M.3    Duggleby, R.G.4    Nixon, P.F.5
  • 51
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • doi:10.1016/0022-2836(68)90205-2
    • Matthews BW. 1968 Solvent content of protein crystals. J. Mol. Biol. 33, 491-497. (doi:10.1016/0022-2836(68)90205-2)
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 52
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • doi:10.1093/nar/gkq366
    • Holm L, Rosenstrom P. 2010 Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549. (doi:10.1093/nar/gkq366)
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 53
    • 0032030782 scopus 로고    scopus 로고
    • Purification, properties and in situ localization of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts
    • Teige M, Melzer M, Suss KH. 1998 Purification, properties and in situ localization of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts. Eur. J. Biochem. 252, 237-244. (doi:10.1046/j. 1432-1327.1998.2520237.x) (Pubitemid 28101999)
    • (1998) European Journal of Biochemistry , vol.252 , Issue.2 , pp. 237-244
    • Teige, M.1    Melzer, M.2    Suss, K.-H.3
  • 54
    • 0037154146 scopus 로고    scopus 로고
    • Snapshot of a key intermediate in enzymatic thiamin catalysis: Crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from saccharomyces cerevisiae
    • DOI 10.1073/pnas.022510999
    • Fiedler E, Thorell S, Sandalova T, Golbik R, Konig S, Schneider G. 2002 Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha, beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 99, 591-595. (doi:10.1073/pnas.022510999) (Pubitemid 34106556)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.2 , pp. 591-595
    • Fiedler, E.1    Thorell, S.2    Sandalova, T.3    Golbik, R.4    Konig, S.5    Schneider, G.6
  • 55
    • 0019332362 scopus 로고
    • The active site of transketolase. Two arginine residues are essential for activity
    • Kremer AB, Egan RM, Sable HZ. 1980 The active site of transketolase. Two arginine residues are essential for activity. J. Biol. Chem. 255, 2405-2410.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2405-2410
    • Kremer, A.B.1    Egan, R.M.2    Sable, H.Z.3
  • 56
    • 0031029945 scopus 로고    scopus 로고
    • Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis
    • DOI 10.1074/jbc.272.3.1864
    • Nilsson U, Meshalkina L, Lindqvist Y, Schneider G. 1997 Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis. J. Biol. Chem. 272, 1864-1869. (doi:10.1074/jbc. 272.3.1864) (Pubitemid 27043278)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1864-1869
    • Nilsson, U.1    Meshalkina, L.2    Lindqvist, Y.3    Schneidere, G.4
  • 57
    • 3142640259 scopus 로고
    • On the mechanism of thiamine action. IV. Evidence from studies on model systems
    • doi:10.1021/ja01547a064
    • Breslow R. 1958 On the mechanism of thiamine action. IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80, 3719-3726. (doi:10.1021/ ja01547a064)
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 3719-3726
    • Breslow, R.1
  • 58
    • 0014454512 scopus 로고
    • Catalytic functions of thiamin diphosphate
    • doi:10.1146/annurev.bi.38.070169.001241
    • Krampitz LO. 1969 Catalytic functions of thiamin diphosphate. Annu. Rev. Biochem. 38, 213-240. (doi:10.1146/annurev.bi.38.070169.001241)
    • (1969) Annu. Rev. Biochem. , vol.38 , pp. 213-240
    • Krampitz, L.O.1
  • 60
    • 16644364379 scopus 로고    scopus 로고
    • Identification of novel small-molecule inhibitors for human transketolase by high-throughput screening with fluorescent intensity (FLINT) assay
    • doi:10.1177/1087057104263913
    • Du MX, Sim J, Fang L, Yin Z, Koh S, Stratton J, Pons J, Wang JJ, Carte B. 2004 Identification of novel small-molecule inhibitors for human transketolase by high-throughput screening with fluorescent intensity (FLINT) assay. J. Biomol. Screen 9, 427-433. (doi:10.1177/1087057104263913)
    • (2004) J. Biomol. Screen , vol.9 , pp. 427-433
    • Du, M.X.1    Sim, J.2    Fang, L.3    Yin, Z.4    Koh, S.5    Stratton, J.6    Pons, J.7    Wang, J.J.8    Carte, B.9
  • 61
    • 0028866360 scopus 로고
    • His103 in yeast transketolase is required for substrate recognition and catalysis
    • doi:10.1111/j.1432-1033.1995.750-3.x
    • Wikner C, Meshalkina L, Nilsson U, Backstrom S, Lindqvist Y, Schneider G. 1995 His103 in yeast transketolase is required for substrate recognition and catalysis. Eur. J. Biochem. 233, 750-755. (doi:10.1111/j.1432-1033.1995.750-3.x)
    • (1995) Eur. J. Biochem. , vol.233 , pp. 750-755
    • Wikner, C.1    Meshalkina, L.2    Nilsson, U.3    Backstrom, S.4    Lindqvist, Y.5    Schneider, G.6
  • 62
    • 0027196884 scopus 로고
    • Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 Aresolution
    • DOI 10.1016/0014-5793(93)81779-Y
    • Nilsson U, Lindqvist Y, Kluger R, Schneider G. 1993 Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 A resolution. FEBS Lett. 326, 145-148. (doi:10.1016/0014-5793(93)81779-Y) (Pubitemid 23200265)
    • (1993) FEBS Letters , vol.326 , Issue.1-3 , pp. 145-148
    • Nilsson, U.1    Lindqvist, Y.2    Kluger, R.3    Schneider, G.4
  • 63
    • 0014632067 scopus 로고
    • Transketolase mutants of Escherichia coli
    • Josephson BL, Fraenkel DG. 1969 Transketolase mutants of Escherichia coli. J. Bacteriol. 100, 1289-1295.
    • (1969) J. Bacteriol. , vol.100 , pp. 1289-1295
    • Josephson, B.L.1    Fraenkel, D.G.2
  • 64
    • 0027515306 scopus 로고
    • Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids
    • Sundstrom M, Lindqvist Y, Schneider G, Hellman U, Ronne H. 1993 Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids. J. Biol. Chem. 268, 24 346-24 352. (Pubitemid 23335426)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 24346-24352
    • Sundstrom, M.1    Lindqvist, Y.2    Schneider, G.3    Hellman, U.4    Ronne, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.