메뉴 건너뛰기




Volumn 78, Issue 16, 2010, Pages 3292-3303

Potential anti-bacterial drug target: Structural characterization of 3,4-dihydroxy-2-butanone-4-phosphate synthase from Salmonella typhimurium LT2

Author keywords

Antimicrobial target; Crystal structure; DHBPS; Flavin adenine dinucleotide; Flavin mono nucleotide; Riboflavin biosynthesis; Ribulose 5 phosphate

Indexed keywords

3,4 DIHYDROXY 2 BUTANONE 4 PHOSPHATE SYNTHASE; ACID; ANTIINFECTIVE AGENT; BASE; MAGNESIUM ION; RIBULOSE PHOSPHATE; SULFATE; UNCLASSIFIED DRUG; ZINC ION;

EID: 78349236903     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22837     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 33947129778 scopus 로고    scopus 로고
    • Salmonella, the host and disease: a brief review
    • Coburn B, Grassl GA, Finlay BB. Salmonella, the host and disease: a brief review. Immunol Cell Biol 2007; 85: 112-118.
    • (2007) Immunol Cell Biol , vol.85 , pp. 112-118
    • Coburn, B.1    Grassl, G.A.2    Finlay, B.B.3
  • 2
    • 36549040131 scopus 로고    scopus 로고
    • Pathogenesis of enteric Salmonella infections
    • Grassl GA, Finlay BB. Pathogenesis of enteric Salmonella infections. Curr Opin Gastroenterol 2008; 24: 22-26.
    • (2008) Curr Opin Gastroenterol , vol.24 , pp. 22-26
    • Grassl, G.A.1    Finlay, B.B.2
  • 3
    • 78349256458 scopus 로고    scopus 로고
    • FAO/OIE/WHO Expert Workshop on Non-Human Antimicrobial Usage and Antimicrobial Resistance
    • WHO report on 1st Joint., Scientific assessment, Geneva, December 1-5
    • WHO report on 1st Joint. FAO/OIE/WHO Expert Workshop on Non-Human Antimicrobial Usage and Antimicrobial Resistance: Scientific assessment, Geneva, December 1-5, 2003.
    • (2003)
  • 4
    • 0003796783 scopus 로고    scopus 로고
    • Escherichia coli and Salmonella: cellular and molecular biology
    • In, Neidhardt FC,Ingraham JL,Low KB,Magasanik B,Schaechter M,Umbarger HE, editors., Washington, DC, ASM Press
    • Bacher A, Eberhardt S, Richter G. Biosynthesis of riboflavin. In: Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE, editors. Escherichia coli and Salmonella: cellular and molecular biology. Washington, DC: ASM Press; 1996.
    • (1996) Biosynthesis of riboflavin
    • Bacher, A.1    Eberhardt, S.2    Richter, G.3
  • 5
    • 0025720052 scopus 로고
    • Biosynthesis of riboflavin. Studies on the mechanism of L-3,4-dihydroxy-2-butanone 4-phosphate synthase
    • Volk R, Bacher A. Biosynthesis of riboflavin. Studies on the mechanism of L-3, 4-dihydroxy-2-butanone 4-phosphate synthase. J Biol Chem 1991; 266: 20610-20618.
    • (1991) J Biol Chem , vol.266 , pp. 20610-20618
    • Volk, R.1    Bacher, A.2
  • 6
    • 0016789502 scopus 로고
    • Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli
    • Foor F, Brown GM. Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J Biol Chem 1975; 250: 3545-3551.
    • (1975) J Biol Chem , vol.250 , pp. 3545-3551
    • Foor, F.1    Brown, G.M.2
  • 7
    • 0018087061 scopus 로고
    • Presence in Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
    • Burrows RB, Brown GM. Presence in Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J Bacteriol 1978; 136: 657-667.
    • (1978) J Bacteriol , vol.136 , pp. 657-667
    • Burrows, R.B.1    Brown, G.M.2
  • 8
    • 0019807080 scopus 로고
    • Biosynthesis of riboflavin. Characterization of the product of the deaminase
    • Nielsen P, Bacher A. Biosynthesis of riboflavin. Characterization of the product of the deaminase. Biochim Biophys Acta 1981; 662: 312-317.
    • (1981) Biochim Biophys Acta , vol.662 , pp. 312-317
    • Nielsen, P.1    Bacher, A.2
  • 9
    • 0027236679 scopus 로고
    • Biosynthesis of riboflavin: cloning, sequencing, mapping and expression of the gene coding for GTP cyclohydrolase II in E. coli
    • Richter G, Ritz H, Katzenmeier G, Volk R, Kohnle A, Lottspeich F. Biosynthesis of riboflavin: cloning, sequencing, mapping and expression of the gene coding for GTP cyclohydrolase II in E. coli. J Bacteriol 1993; 175: 4045-4051.
    • (1993) J Bacteriol , vol.175 , pp. 4045-4051
    • Richter, G.1    Ritz, H.2    Katzenmeier, G.3    Volk, R.4    Kohnle, A.5    Lottspeich, F.6
  • 10
    • 0030946770 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Characterization of the bifunctional deaminase/reductase of Escherichia coli and Bacillus subtilis
    • Richter G, Fischer M, Krieger C, Eberhardt S, Lüttgen H, Gerstenschläger I, Bacher A. Biosynthesis of riboflavin. Characterization of the bifunctional deaminase/reductase of Escherichia coli and Bacillus subtilis. J Bacteriol 1997; 179: 2022-2028.
    • (1997) J Bacteriol , vol.179 , pp. 2022-2028
    • Richter, G.1    Fischer, M.2    Krieger, C.3    Eberhardt, S.4    Lüttgen, H.5    Gerstenschläger, I.6    Bacher, A.7
  • 11
    • 0001976613 scopus 로고
    • Studies on the stoichiometry of the enzymatic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin
    • Plaut GWE. Studies on the stoichiometry of the enzymatic conversion of 6, 7-dimethyl-8-ribityllumazine to riboflavin. J Biol Chem 1960; 235: 41-42.
    • (1960) J Biol Chem , vol.235 , pp. 41-42
    • Plaut, G.W.E.1
  • 12
    • 0001653222 scopus 로고
    • Studies on the nature of the enzymatic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin
    • Plaut GWE. Studies on the nature of the enzymatic conversion of 6, 7-dimethyl-8-ribityllumazine to riboflavin. J Biol Chem 1963; 238: 2225-2243.
    • (1963) J Biol Chem , vol.238 , pp. 2225-2243
    • Plaut, G.W.E.1
  • 13
    • 0014952520 scopus 로고
    • Studies on the mechanism ofelimination of protons from the methyl groups of 6,7-dimethyl-8-ribityllumazine by riboflavin synthetase
    • Plaut GWE, Beach RL, Aogaichi T. Studies on the mechanism ofelimination of protons from the methyl groups of 6, 7-dimethyl-8-ribityllumazine by riboflavin synthetase. Biochemistry 1970; 9: 771-785.
    • (1970) Biochemistry , vol.9 , pp. 771-785
    • Plaut, G.W.E.1    Beach, R.L.2    Aogaichi, T.3
  • 14
    • 0001376922 scopus 로고
    • The enzymatic synthesis of riboflavin
    • Plaut GWE, Harvey RA. The enzymatic synthesis of riboflavin. Methods Enzymol 1971; 18: 515-538.
    • (1971) Methods Enzymol , vol.18 , pp. 515-538
    • Plaut, G.W.E.1    Harvey, R.A.2
  • 15
    • 0023059813 scopus 로고
    • Biosynthesis of riboflavin. Enzymatic formation of 6,7-dimethyl-8-ribityllumazine by heavy riboflavin synthase from Bacillus subtilis
    • Neuberger G, Bacher A. Biosynthesis of riboflavin. Enzymatic formation of 6, 7-dimethyl-8-ribityllumazine by heavy riboflavin synthase from Bacillus subtilis. Biochem Biophys Res Commun 1986; 139: 1111-1116.
    • (1986) Biochem Biophys Res Commun , vol.139 , pp. 1111-1116
    • Neuberger, G.1    Bacher, A.2
  • 16
    • 0029054040 scopus 로고
    • Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis
    • Kis K, Bacher A. Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis. J Biol Chem 1995; 270: 16788-16795.
    • (1995) J Biol Chem , vol.270 , pp. 16788-16795
    • Kis, K.1    Bacher, A.2
  • 17
    • 0028925952 scopus 로고
    • Biosynthesis of riboflavin. Studies on the reaction mechanism of 6,7-dimethyl-8-ribityllumazine synthase
    • Kis K, Volk R, Bacher A. Biosynthesis of riboflavin. Studies on the reaction mechanism of 6, 7-dimethyl-8-ribityllumazine synthase. Biochemistry 1995; 34: 2883-2892.
    • (1995) Biochemistry , vol.34 , pp. 2883-2892
    • Kis, K.1    Volk, R.2    Bacher, A.3
  • 18
    • 0004255912 scopus 로고
    • Chemistry and biochemistry of flavoenzymes
    • In, Muller F, editor., London, CRC press;
    • Bacher, A. Riboflavin kinase and FAD synthetase. In: Muller F, editor. Chemistry and biochemistry of flavoenzymes. London: CRC press; 1991. pp 349-370.
    • (1991) Riboflavin kinase and FAD synthetase , pp. 349-370
    • Bacher, A.1
  • 19
    • 0025203677 scopus 로고
    • Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2-butanone-4-phosphate synthase
    • Volk R, Bacher A. Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3, 4-dihydroxy-2-butanone-4-phosphate synthase. J Biol Chem 1990; 265: 19479-19485.
    • (1990) J Biol Chem , vol.265 , pp. 19479-19485
    • Volk, R.1    Bacher, A.2
  • 20
    • 0033119631 scopus 로고    scopus 로고
    • NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling
    • Richter G, Kelly M, Krieger C, Yu Y, Bermel W, Karlsson G. NMR studies on the 46-kDa dimeric protein, 3, 4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling. Eur J Biochem 1999; 261: 57-65.
    • (1999) Eur J Biochem , vol.261 , pp. 57-65
    • Richter, G.1    Kelly, M.2    Krieger, C.3    Yu, Y.4    Bermel, W.5    Karlsson, G.6
  • 21
    • 0035155856 scopus 로고    scopus 로고
    • Crystal structure of 3,4-diyhdroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis
    • Liao DI, Calabrese JC, Wawrzak Z, Viitanen PV, Jordan DB. Crystal structure of 3, 4-diyhdroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis. Structure 2001; 9: 11-18.
    • (2001) Structure , vol.9 , pp. 11-18
    • Liao, D.I.1    Calabrese, J.C.2    Wawrzak, Z.3    Viitanen, P.V.4    Jordan, D.B.5
  • 22
    • 0037065733 scopus 로고    scopus 로고
    • Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone 4-phosphate synthase
    • Liao DI, Zheng YJ, Viitanen PV, Jordan DB. Structural definition of the active site and catalytic mechanism of 3, 4-dihydroxy-2-butanone 4-phosphate synthase. Biochemistry 2002; 41: 1795-1806.
    • (2002) Biochemistry , vol.41 , pp. 1795-1806
    • Liao, D.I.1    Zheng, Y.J.2    Viitanen, P.V.3    Jordan, D.B.4
  • 23
    • 0142242191 scopus 로고    scopus 로고
    • Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate
    • Steinbacher S, Schiffmann S, Richter G, Huber R, Bacher A, Fischer M. Structure of 3, 4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate. J Biol Chem 2003; 278: 42256-42265.
    • (2003) J Biol Chem , vol.278 , pp. 42256-42265
    • Steinbacher, S.1    Schiffmann, S.2    Richter, G.3    Huber, R.4    Bacher, A.5    Fischer, M.6
  • 24
    • 3843086171 scopus 로고    scopus 로고
    • Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans
    • Echt S, Bauer S, Steinbacher S, Huber R, Bacher A, Fischer M. Potential anti-infective targets in pathogenic yeasts: structure and properties of 3, 4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans. J Mol Biol 2004; 341: 1085-1096.
    • (2004) J Mol Biol , vol.341 , pp. 1085-1096
    • Echt, S.1    Bauer, S.2    Steinbacher, S.3    Huber, R.4    Bacher, A.5    Fischer, M.6
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0034672113 scopus 로고    scopus 로고
    • Spectrophotometric determination of 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
    • Picollelli MA, Viitanen PV, Jordan DB. Spectrophotometric determination of 3, 4-dihydroxy-2-butanone-4-phosphate synthase activity. Anal Biochem 2000; 287: 347-349.
    • (2000) Anal Biochem , vol.287 , pp. 347-349
    • Picollelli, M.A.1    Viitanen, P.V.2    Jordan, D.B.3
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D 1994; 50: 760-763
    • (1994) Acta Crystallogr Sect D , vol.50 , pp. 760-763
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr Sect D 1997; 53: 240-255.
    • (1997) Acta Crystallogr Sect D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr Sect D 2004; 60: 2126-2132.
    • (2004) Acta Crystallogr Sect D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 35
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • Palo Alto, CA, DeLano Scientific
    • DeLano WL. The PyMOL molecular graphics system. Palo Alto, CA: DeLano Scientific; 2002.
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.