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Volumn 401, Issue 2, 2010, Pages 253-264

Structure and reactivity of bacillus subtilis MenD catalyzing the first committed step in menaquinone biosynthesis

Author keywords

Crystal structure; Enzyme mechanism; Menaquinone biosynthesis; Thiamine diphosphate cofactor

Indexed keywords

ALANINE; ARGININE; CARBOXYLIC ACID; HYDROXYL GROUP; ISOLEUCINE; LEUCINE; LYSINE; MANGANESE; MENAQUINONE; METAL ION DEPENDENT 2 SUCCINYL 5 ENOLPYRUVYL 6 HYDROXY 3 CYCLOHEXADIENE 1 CARBOXYLATE SYNTHASE; PHENYLALANINE; UNCLASSIFIED DRUG;

EID: 77955089175     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.025     Document Type: Article
Times cited : (30)

References (39)
  • 1
    • 0035219809 scopus 로고    scopus 로고
    • 2) and ubiquinone (coenzyme Q): a perspective on enzymatic reactions
    • 2) and ubiquinone (coenzyme Q): a perspective on enzymatic reactions. Vitam. Horm. 2001, 61:173-218.
    • (2001) Vitam. Horm. , vol.61 , pp. 173-218
    • Meganathan, R.1
  • 2
    • 0032843484 scopus 로고    scopus 로고
    • Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management
    • Soballe B., Poole R.K. Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology 1999, 145:1817-1830.
    • (1999) Microbiology , vol.145 , pp. 1817-1830
    • Soballe, B.1    Poole, R.K.2
  • 3
    • 40949087151 scopus 로고    scopus 로고
    • Vitamin K-dependent γ-glutamylcarboxylation: an ancient posttranslational modification
    • Bandyopadhyay P.K. Vitamin K-dependent γ-glutamylcarboxylation: an ancient posttranslational modification. Vitam. Horm. 2008, 78:157-184.
    • (2008) Vitam. Horm. , vol.78 , pp. 157-184
    • Bandyopadhyay, P.K.1
  • 4
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs A.R. The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 2003, 20:119-136.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 119-136
    • Knaggs, A.R.1
  • 7
    • 0345686436 scopus 로고    scopus 로고
    • Steady-state kinetics and molecular evolution of Escherichia coli MenD [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase], an anomalous thiamin diphosphate-dependent decarboxylase-carboligase
    • Bhasin M., Billinsky J.L., Palmer D.R. Steady-state kinetics and molecular evolution of Escherichia coli MenD [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase], an anomalous thiamin diphosphate-dependent decarboxylase-carboligase. Biochemistry 2003, 42:13496-13504.
    • (2003) Biochemistry , vol.42 , pp. 13496-13504
    • Bhasin, M.1    Billinsky, J.L.2    Palmer, D.R.3
  • 8
    • 84982417601 scopus 로고
    • Catalyzed addition of aldehydes to activated double bonds-a new synthetic approach
    • Stetter H. Catalyzed addition of aldehydes to activated double bonds-a new synthetic approach. Angew. Chem., Int. Ed. 1976, 15:639-647.
    • (1976) Angew. Chem., Int. Ed. , vol.15 , pp. 639-647
    • Stetter, H.1
  • 9
    • 34648813427 scopus 로고    scopus 로고
    • Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity
    • Jiang M., Cao Y., Guo Z.F., Chen M., Chen X., Guo Z. Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity. Biochemistry 2007, 46:10979-10989.
    • (2007) Biochemistry , vol.46 , pp. 10979-10989
    • Jiang, M.1    Cao, Y.2    Guo, Z.F.3    Chen, M.4    Chen, X.5    Guo, Z.6
  • 10
    • 40849094350 scopus 로고    scopus 로고
    • Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli
    • Jiang M., Chen X., Guo Z.F., Cao Y., Chen M., Guo Z. Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli. Biochemistry 2008, 47:3426-3434.
    • (2008) Biochemistry , vol.47 , pp. 3426-3434
    • Jiang, M.1    Chen, X.2    Guo, Z.F.3    Cao, Y.4    Chen, M.5    Guo, Z.6
  • 12
    • 0037154255 scopus 로고    scopus 로고
    • A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae
    • Akerley B.J., Rubin E.J., Novick V.L., Amaya K., Judson N., Mekalanos J.J. A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae. Proc. Natl Acad. Sci. USA 2002, 99:966-971.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 966-971
    • Akerley, B.J.1    Rubin, E.J.2    Novick, V.L.3    Amaya, K.4    Judson, N.5    Mekalanos, J.J.6
  • 13
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti C.M., Boyd D.H., Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003, 48:77-84.
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 14
    • 66449089904 scopus 로고    scopus 로고
    • Structure-based ligand design and the promise held for antiprotozoan drug discovery
    • Hunter W.N. Structure-based ligand design and the promise held for antiprotozoan drug discovery. J. Biol. Chem. 2009, 284:11749-11753.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11749-11753
    • Hunter, W.N.1
  • 15
    • 56949084464 scopus 로고    scopus 로고
    • Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase)
    • Dawson A., Fyfe P.K., Hunter W.H. Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase). J. Mol. Biol. 2008, 384:1353-1368.
    • (2008) J. Mol. Biol. , vol.384 , pp. 1353-1368
    • Dawson, A.1    Fyfe, P.K.2    Hunter, W.H.3
  • 20
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60:2256-2268.
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 33748345821 scopus 로고    scopus 로고
    • Domain relationships in thiamine diphosphate-dependent enzymes
    • Duggleby R.G. Domain relationships in thiamine diphosphate-dependent enzymes. Acc. Chem. Res. 2006, 39:550-557.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 550-557
    • Duggleby, R.G.1
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 1242317003 scopus 로고    scopus 로고
    • 2-(2-carboxyethyl)arginine sythase, the first enzyme in the clavulanic acid biosynthesis pathway
    • 2-(2-carboxyethyl)arginine sythase, the first enzyme in the clavulanic acid biosynthesis pathway. J. Biol. Chem. 2004, 279:5685-5692.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5685-5692
    • Caines, M.E.1    Elkins, J.M.2    Hewitson, K.S.3    Schofield, C.J.4
  • 24
    • 47349102781 scopus 로고    scopus 로고
    • Thiamin diposphate catalysis: enzymic and nonenzymic covalent intermediates
    • Kluger R., Tittmann K. Thiamin diposphate catalysis: enzymic and nonenzymic covalent intermediates. Chem. Rev. 2008, 108:1797-1833.
    • (2008) Chem. Rev. , vol.108 , pp. 1797-1833
    • Kluger, R.1    Tittmann, K.2
  • 25
    • 34447260286 scopus 로고    scopus 로고
    • Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases
    • Berthold C.L., Toyota C.G., Moussatche P., Wood M.D., Leeper F., Richards N.G., Lindqvist Y. Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure 2007, 15:853-861.
    • (2007) Structure , vol.15 , pp. 853-861
    • Berthold, C.L.1    Toyota, C.G.2    Moussatche, P.3    Wood, M.D.4    Leeper, F.5    Richards, N.G.6    Lindqvist, Y.7
  • 26
    • 0033559680 scopus 로고    scopus 로고
    • The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli; a novel combination of domain folds
    • Hall D.R., Gourley D.G., Leonard G.A., Duke E.B.H., Anderson L.A., Boxer D.H., Hunter W.N. The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli; a novel combination of domain folds. EMBO J. 1999, 18:1435-1446.
    • (1999) EMBO J. , vol.18 , pp. 1435-1446
    • Hall, D.R.1    Gourley, D.G.2    Leonard, G.A.3    Duke, E.B.H.4    Anderson, L.A.5    Boxer, D.H.6    Hunter, W.N.7
  • 28
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 1993, 26:795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 30
    • 77955086941 scopus 로고    scopus 로고
    • Bruker, Bruker AXS Inc., Madison, WI
    • Bruker XPREP 2004, Bruker AXS Inc., Madison, WI.
    • (2004) XPREP
  • 36
    • 0021863643 scopus 로고
    • A simple procedure for removing contaminating aldehydes and peroxides from aqueous solutions of polyethylene glycols and of nonionic detergents that are based on the polyoxyethylene linkage
    • Ray W.J., Puvathingal J.M. A simple procedure for removing contaminating aldehydes and peroxides from aqueous solutions of polyethylene glycols and of nonionic detergents that are based on the polyoxyethylene linkage. Anal. Biochem. 1985, 146:307-312.
    • (1985) Anal. Biochem. , vol.146 , pp. 307-312
    • Ray, W.J.1    Puvathingal, J.M.2
  • 38
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond C.S., Schuttelkopf A.W. ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2009, 65:510-512.
    • (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.65 , pp. 510-512
    • Bond, C.S.1    Schuttelkopf, A.W.2
  • 39
    • 0025162272 scopus 로고
    • Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization and substrate specificity of isochorismate synthase
    • Rusnak F., Liu J., Quinn N., Berchtold G.A., Walsh C.T. Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization and substrate specificity of isochorismate synthase. Biochemistry 1990, 29:1425-1435.
    • (1990) Biochemistry , vol.29 , pp. 1425-1435
    • Rusnak, F.1    Liu, J.2    Quinn, N.3    Berchtold, G.A.4    Walsh, C.T.5


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