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Volumn 189, Issue 17, 2007, Pages 6246-6252

Functional characterization by genetic complementation of aroB-encoded dehydroquinate synthase from Mycobacterium tuberculosis H37Rv and its heterologous expression and purification

Author keywords

[No Author keywords available]

Indexed keywords

3 DEHYDROQUINATE SYNTHASE; 3 DEOXY DEXTRO ARABINOHEPTULOSONATE 7 PHOSPHATE; AROMATIC AMINO ACID; AROMATIC COMPOUND; MANNOHEPTULOSE; PHOSPHATE; RECOMBINANT ENZYME; SHIKIMIC ACID; UNCLASSIFIED DRUG;

EID: 34548491616     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00425-07     Document Type: Article
Times cited : (22)

References (39)
  • 1
    • 26444576411 scopus 로고    scopus 로고
    • Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis - an update
    • Basso, L. A., and D. S. Santos. 2005. Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis - an update. Med. Chem. Rev. 2:393-413.
    • (2005) Med. Chem. Rev , vol.2 , pp. 393-413
    • Basso, L.A.1    Santos, D.S.2
  • 3
    • 0024974067 scopus 로고
    • Dehydroquinate synthase: The role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis
    • Bender, S. L., S. Mehdi, and J. R. Knowles. 1989. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28:7555-7560.
    • (1989) Biochemistry , vol.28 , pp. 7555-7560
    • Bender, S.L.1    Mehdi, S.2    Knowles, J.R.3
  • 4
    • 0025581736 scopus 로고
    • The shikimate pathway - a metabolic tree with many branches
    • Bentley, R. 1990. The shikimate pathway - a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 25:307-384.
    • (1990) Crit. Rev. Biochem. Mol. Biol , vol.25 , pp. 307-384
    • Bentley, R.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation 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
  • 6
    • 33645119729 scopus 로고    scopus 로고
    • Emergence of Mycobacterium tuberculosis with extensive resistance to second-line drugs worldwide
    • Centers for Disease Control and Prevention
    • Centers for Disease Control and Prevention. 2006. Emergence of Mycobacterium tuberculosis with extensive resistance to second-line drugs worldwide. Morb. Mortal. Wkly. Rep. 55:301-305.
    • (2006) Morb. Mortal. Wkly. Rep , vol.55 , pp. 301-305
  • 7
    • 17144363589 scopus 로고    scopus 로고
    • Pure but not simple
    • Chapman, T. 2005. Pure but not simple. Nature 434:795-798.
    • (2005) Nature , vol.434 , pp. 795-798
    • Chapman, T.1
  • 8
    • 0031759474 scopus 로고    scopus 로고
    • Characterization of horse kidney metalothionein isoforms by electrospray MS and reversed-phase HPLC-electrospray MS
    • Chassaigne, H., and R. Lobinski. 1998. Characterization of horse kidney metalothionein isoforms by electrospray MS and reversed-phase HPLC-electrospray MS. Analyst 123:2125-2130.
    • (1998) Analyst , vol.123 , pp. 2125-2130
    • Chassaigne, H.1    Lobinski, R.2
  • 9
    • 0032508046 scopus 로고    scopus 로고
    • Cole, S. T., R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S. V. Gordon, K. Eiglmeier, S. Gas, C. E. Barry III, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, A. Krogh, J. McLean, S. Moule, L. Murphy, K. Oliver, J. Osborne, M. A. Quail, M. A. Rajandream, J. Rogers, S. Rutter, K. Seeger, J. Skelton, R. Squares, S. Squares, J. E. Sulston, K. Taylor, S. Whitehead, and B. G. Barrell. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
    • Cole, S. T., R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S. V. Gordon, K. Eiglmeier, S. Gas, C. E. Barry III, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, A. Krogh, J. McLean, S. Moule, L. Murphy, K. Oliver, J. Osborne, M. A. Quail, M. A. Rajandream, J. Rogers, S. Rutter, K. Seeger, J. Skelton, R. Squares, S. Squares, J. E. Sulston, K. Taylor, S. Whitehead, and B. G. Barrell. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
  • 11
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine or vitamin B12
    • Davis, B. D., and E. S. Mingioli. 1950. Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bacteriol. 60:17-28.
    • (1950) J. Bacteriol , vol.60 , pp. 17-28
    • Davis, B.D.1    Mingioli, E.S.2
  • 12
    • 33847719510 scopus 로고    scopus 로고
    • From magic bullets back to the Magic Mountain: The rise of extensively drug-resistant tuberculosis
    • Dorman, S. E., and R. E. Chaisson. 2007. From magic bullets back to the Magic Mountain: the rise of extensively drug-resistant tuberculosis. Nat. Med. 13:295-298.
    • (2007) Nat. Med , vol.13 , pp. 295-298
    • Dorman, S.E.1    Chaisson, R.E.2
  • 14
    • 33847705622 scopus 로고    scopus 로고
    • Mycobacterial shikimate pathway enzymes as targets for drug design
    • Ducati, R. G., L. A. Basso, and D. S. Santos. 2007. Mycobacterial shikimate pathway enzymes as targets for drug design. Curr. Drug Targets 8:423-435.
    • (2007) Curr. Drug Targets , vol.8 , pp. 423-435
    • Ducati, R.G.1    Basso, L.A.2    Santos, D.S.3
  • 15
    • 0023414737 scopus 로고
    • The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains
    • Duncan, K., R. M. Edwards, and J. R. Coggins. 1987. The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Biochem. J. 246:375-386.
    • (1987) Biochem. J , vol.246 , pp. 375-386
    • Duncan, K.1    Edwards, R.M.2    Coggins, J.R.3
  • 16
    • 0021760658 scopus 로고
    • Dehydroquinate synthase from Escherichia coli: Purification, cloning and construction of overproducers of the enzyme
    • Frost, J. W., J. L. Bender, J. T. Kadonaga, and J. R. Knowles. 1984. Dehydroquinate synthase from Escherichia coli: purification, cloning and construction of overproducers of the enzyme. Biochemistry 23:4470-4475.
    • (1984) Biochemistry , vol.23 , pp. 4470-4475
    • Frost, J.W.1    Bender, J.L.2    Kadonaga, J.T.3    Knowles, J.R.4
  • 17
    • 0017352133 scopus 로고
    • A cluster-gene: Evidence for one gene, one polypeptide, five enzymes
    • Gaertner, F. W., and K. W. Cole. 1977. A cluster-gene: evidence for one gene, one polypeptide, five enzymes. Biochem. Biophys. Res. Commun. 75:259-264.
    • (1977) Biochem. Biophys. Res. Commun , vol.75 , pp. 259-264
    • Gaertner, F.W.1    Cole, K.W.2
  • 18
    • 0025742991 scopus 로고
    • The Mycobacterium tuberculosis shikimate pathway genes: Evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases
    • Garbe, T., S. Servos, A. Hawkins, G. Dimitriadis, D. Young, G. Dougan, and I. Charles. 1991. The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases. Mol. Gen. Genet. 228:385-392.
    • (1991) Mol. Gen. Genet , vol.228 , pp. 385-392
    • Garbe, T.1    Servos, S.2    Hawkins, A.3    Dimitriadis, G.4    Young, D.5    Dougan, G.6    Charles, I.7
  • 19
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • Grossman, T. H., E. S. Kawaski, S. R. Punreddy, and M. S. Osburne. 1998. Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209:95-103.
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawaski, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 20
    • 0017810571 scopus 로고
    • Dehydroquinate synthase in Bacillus subtilis. An enzyme associated with chorismate synthase and flavin reductase
    • Hasan, N., and E. W. Nester. 1978. Dehydroquinate synthase in Bacillus subtilis. An enzyme associated with chorismate synthase and flavin reductase. J. Biol. Chem. 253:4999-5004.
    • (1978) J. Biol. Chem , vol.253 , pp. 4999-5004
    • Hasan, N.1    Nester, E.W.2
  • 21
    • 0027787581 scopus 로고
    • The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: Theoretical and practical aspects
    • Hawkins, A. R., H. K. Lamb, J. D. Moore, I. G. Charles, and C. F. Roberts. 1993. The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: theoretical and practical aspects. J. Gen. Microbiol. 139:2891-2899.
    • (1993) J. Gen. Microbiol , vol.139 , pp. 2891-2899
    • Hawkins, A.R.1    Lamb, H.K.2    Moore, J.D.3    Charles, I.G.4    Roberts, C.F.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0036424063 scopus 로고    scopus 로고
    • Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv
    • Magalhães, M. L. B., C. P. Pereira, L. A. Basso, and D. S. Santos. 2002. Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv. Protein Expr. Purif. 26:59-64.
    • (2002) Protein Expr. Purif , vol.26 , pp. 59-64
    • Magalhães, M.L.B.1    Pereira, C.P.2    Basso, L.A.3    Santos, D.S.4
  • 26
    • 4744337641 scopus 로고    scopus 로고
    • Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases
    • Nichols, C. E., J. Ren, K. Leslie, B. Dhaliwal, M. Lockyer, I. Charles, A. R. Hawkins, and D. K. Stammers. 2004. Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases. J. Mol. Biol. 343:533-546.
    • (2004) J. Mol. Biol , vol.343 , pp. 533-546
    • Nichols, C.E.1    Ren, J.2    Leslie, K.3    Dhaliwal, B.4    Lockyer, M.5    Charles, I.6    Hawkins, A.R.7    Stammers, D.K.8
  • 27
    • 0032534786 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase: Its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase
    • Nixon, A. E., J. L. Hunter, G. Bonifacio, J. F. Eccleston, and M. R. Webb. 1998. Purine nucleoside phosphorylase: its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase. Anal. Biochem. 265:299-307.
    • (1998) Anal. Biochem , vol.265 , pp. 299-307
    • Nixon, A.E.1    Hunter, J.L.2    Bonifacio, G.3    Eccleston, J.F.4    Webb, M.R.5
  • 28
    • 0034889953 scopus 로고    scopus 로고
    • Cloning and overexpression in soluble form of functional shikimate kinase and 5-enol-pyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis
    • Oliveira, J. S., C. A. Pinto, L. A. Basso, and D. S. Santos. 2001. Cloning and overexpression in soluble form of functional shikimate kinase and 5-enol-pyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis. Protein Expr. Purif. 22:430-435.
    • (2001) Protein Expr. Purif , vol.22 , pp. 430-435
    • Oliveira, J.S.1    Pinto, C.A.2    Basso, L.A.3    Santos, D.S.4
  • 29
    • 0038057554 scopus 로고    scopus 로고
    • One-step purification of 5-enolpyruvylshikimate-3-phosphate synthase enzyme from Mycobacterium tuberculosis
    • Oliveira, J. S., M. A. Mendes, M. S. Palma, L. A. Basso, and D. S. Santos. 2003. One-step purification of 5-enolpyruvylshikimate-3-phosphate synthase enzyme from Mycobacterium tuberculosis. Protein Expr. Purif. 28:287-292.
    • (2003) Protein Expr. Purif , vol.28 , pp. 287-292
    • Oliveira, J.S.1    Mendes, M.A.2    Palma, M.S.3    Basso, L.A.4    Santos, D.S.5
  • 30
    • 0036773752 scopus 로고    scopus 로고
    • The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis
    • Parish, T., and N. G. Stoker. 2002. The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis. Microbiology 148:3069-3077.
    • (2002) Microbiology , vol.148 , pp. 3069-3077
    • Parish, T.1    Stoker, N.G.2
  • 31
    • 0026089420 scopus 로고
    • Organic solvents as facilitators of a polymerase chain reaction
    • Pomp, D., and J. F. Medrano. 1991. Organic solvents as facilitators of a polymerase chain reaction. BioTechniques 10:58-59.
    • (1991) BioTechniques , vol.10 , pp. 58-59
    • Pomp, D.1    Medrano, J.F.2
  • 34
    • 0001026179 scopus 로고
    • The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate
    • Srinivasan, P. R., J. Rothschild, and D. B. Sprinson. 1963. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238:3176-3182.
    • (1963) J. Biol. Chem , vol.238 , pp. 3176-3182
    • Srinivasan, P.R.1    Rothschild, J.2    Sprinson, D.B.3
  • 35
    • 0026689163 scopus 로고
    • Overproduction in Escherichia coli of the dehydroquinate synthase domain of the Aspergillus nidulans pentafunctional AROM protein
    • van den Hombergh, J. P. T. W., J. D. Moore, I. G. Charles, and A. R. Hawkins. 1992. Overproduction in Escherichia coli of the dehydroquinate synthase domain of the Aspergillus nidulans pentafunctional AROM protein. Biochem. J. 284:861-867.
    • (1992) Biochem. J , vol.284 , pp. 861-867
    • van den Hombergh, J.P.T.W.1    Moore, J.D.2    Charles, I.G.3    Hawkins, A.R.4
  • 37
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M. R. 1992. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. USA 89:4884-4887.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 38
    • 0024600983 scopus 로고
    • An improved method for directly sequencing PCR amplified material using dimethyl sulphoxide
    • Winship, P. R. 1989. An improved method for directly sequencing PCR amplified material using dimethyl sulphoxide. Nucleic Acids Res. 17:1266.
    • (1989) Nucleic Acids Res , vol.17 , pp. 1266
    • Winship, P.R.1
  • 39
    • 0011523808 scopus 로고    scopus 로고
    • Global tuberculosis control: Surveillance, planning, financing
    • World Health Organization, World Health Organization, Geneva, Switzerland
    • World Health Organization. 2006. Global tuberculosis control: surveillance, planning, financing. WHO report 2006. World Health Organization, Geneva, Switzerland.
    • (2006) WHO report 2006


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.