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Volumn 396, Issue 1, 2010, Pages 33-38

Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis

Author keywords

Cysteine biosynthesis; Enzyme structure; Enzymology; Inhibition; Tuberculosis

Indexed keywords

CYSTEINE; CYSTEINE SYNTHASE; PROTEIN CYSK1; PROTEIN NIRA; SULFITE REDUCTASE; SULFUR; UNCLASSIFIED DRUG;

EID: 77952310116     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.02.118     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0032773119 scopus 로고    scopus 로고
    • The death and resurrection of tuberculosis
    • Bloom B.R., and McKinney R.D. The death and resurrection of tuberculosis. Nat. Med. 5 (1999) 872-874
    • (1999) Nat. Med. , vol.5 , pp. 872-874
    • Bloom, B.R.1    McKinney, R.D.2
  • 2
    • 0028024035 scopus 로고
    • Metronidazole is bactericidal to dormant cells of Mycobacterium tuberculosis
    • Wayne L.G., and Sramek H.A. Metronidazole is bactericidal to dormant cells of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 38 (1994) 807-811
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 807-811
    • Wayne, L.G.1    Sramek, H.A.2
  • 4
    • 17044384970 scopus 로고    scopus 로고
    • The DOTS strategy for controlling the global tuberculosis epidemic
    • Frieden T.R., and Munsiff S.S. The DOTS strategy for controlling the global tuberculosis epidemic. Clin. Chest Med. 26 (2005) 197-205
    • (2005) Clin. Chest Med. , vol.26 , pp. 197-205
    • Frieden, T.R.1    Munsiff, S.S.2
  • 5
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • Wayne L.G., and Sohaskey C.D. Nonreplicating persistence of Mycobacterium tuberculosis. Annu. Rev. Microbiol. 55 (2001) 139-163
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 7
    • 12244293660 scopus 로고    scopus 로고
    • S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense
    • Rhee K.Y., Erdjument-Bromage H., Tempst P., and Nathan C.F. S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense. Proc. Natl. Acad. Sci. USA 102 (2005) 467-472
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 8
    • 0030792817 scopus 로고    scopus 로고
    • Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis
    • Bornemann C., Jardine M.A., Spies H.S., and Steenkamp D.J. Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis. Biochem. J. 325 (1997) 623-629
    • (1997) Biochem. J. , vol.325 , pp. 623-629
    • Bornemann, C.1    Jardine, M.A.2    Spies, H.S.3    Steenkamp, D.J.4
  • 9
    • 0035822573 scopus 로고    scopus 로고
    • Increased levels of sigJ mRNA in late stationary phase cultures of Mycobacterium tuberculosis detected by DNA array hybridisation
    • Hu Y., and Coates A.R.M. Increased levels of sigJ mRNA in late stationary phase cultures of Mycobacterium tuberculosis detected by DNA array hybridisation. FEMS Microbiol. Lett. 202 (2001) 59-65
    • (2001) FEMS Microbiol. Lett. , vol.202 , pp. 59-65
    • Hu, Y.1    Coates, A.R.M.2
  • 11
    • 3042790827 scopus 로고    scopus 로고
    • Stationary phase gene expression of Mycobacterium tuberculosis following a progressive nutrient depletion: a model for persistent organisms?
    • Hampshire T., Soneji S., Bacon J., James B.W., Hinds J., Laing K., Stabler R.A., Marsh P.D., and Butcher P.D. Stationary phase gene expression of Mycobacterium tuberculosis following a progressive nutrient depletion: a model for persistent organisms?. Tuberculosis 84 (2004) 228-238
    • (2004) Tuberculosis , vol.84 , pp. 228-238
    • Hampshire, T.1    Soneji, S.2    Bacon, J.3    James, B.W.4    Hinds, J.5    Laing, K.6    Stabler, R.A.7    Marsh, P.D.8    Butcher, P.D.9
  • 12
    • 9144263752 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions
    • Starck J., Källenius G., Marklund B.I., Andersson D.I., and Akerlund T. Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions. Microbiology 150 (2004) 3821-3829
    • (2004) Microbiology , vol.150 , pp. 3821-3829
    • Starck, J.1    Källenius, G.2    Marklund, B.I.3    Andersson, D.I.4    Akerlund, T.5
  • 17
    • 20444419421 scopus 로고    scopus 로고
    • Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • Rengarajan J., Bloom B.R., and Rubin E.J. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc. Natl. Acad. Sci. USA 102 (2005) 8327-8332
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 18
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti C.M., and Rubin E.J. Genetic requirements for mycobacterial survival during infection. Proc. Natl. Acad. Sci. USA 100 (2003) 12989-12994
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 19
    • 57349131909 scopus 로고    scopus 로고
    • 1.9 A structure of the signal receiver domain of the putative response regulator NarL from Mycobacterium tuberculosis
    • Schnell R., Ågren D., and Schneider G. 1.9 A structure of the signal receiver domain of the putative response regulator NarL from Mycobacterium tuberculosis. Acta Crystallogr. F 64 (2008) 1096-1100
    • (2008) Acta Crystallogr. F , vol.64 , pp. 1096-1100
    • Schnell, R.1    Ågren, D.2    Schneider, G.3
  • 20
    • 40849117861 scopus 로고    scopus 로고
    • Three-dimensional structures of apo- and holo-l-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme binding
    • Ågren D., Stehr M., Berthold C.L., Kapoor S., Oehlmann W., Singh M., and Schneider G. Three-dimensional structures of apo- and holo-l-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme binding. J. Mol. Biol. 377 (2008) 1161-1173
    • (2008) J. Mol. Biol. , vol.377 , pp. 1161-1173
    • Ågren, D.1    Stehr, M.2    Berthold, C.L.3    Kapoor, S.4    Oehlmann, W.5    Singh, M.6    Schneider, G.7
  • 21
    • 0033231207 scopus 로고    scopus 로고
    • Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional l-alanine dehydrogenase
    • Hutter B., and Singh M. Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional l-alanine dehydrogenase. Biochem. J. 343 (1999) 669-672
    • (1999) Biochem. J. , vol.343 , pp. 669-672
    • Hutter, B.1    Singh, M.2
  • 22
    • 22844435319 scopus 로고    scopus 로고
    • Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site
    • Schnell R., Sandalova T., Hellman U., Lindqvist Y., and Schneider G. Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site. J. Biol. Chem. 280 (2005) 27319-27328
    • (2005) J. Biol. Chem. , vol.280 , pp. 27319-27328
    • Schnell, R.1    Sandalova, T.2    Hellman, U.3    Lindqvist, Y.4    Schneider, G.5
  • 23
    • 55249100956 scopus 로고    scopus 로고
    • O-phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis
    • O'Leary S.E., Jurgenson C.T., Ealick S.E., and Begley T.P. O-phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis. Biochemistry 47 (2008) 11606-11615
    • (2008) Biochemistry , vol.47 , pp. 11606-11615
    • O'Leary, S.E.1    Jurgenson, C.T.2    Ealick, S.E.3    Begley, T.P.4
  • 24
    • 57649136751 scopus 로고    scopus 로고
    • Cysteine synthase (CYSM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria
    • Ågren D., Schnell R., Oehlmann W., Singh M., and Schneider G. Cysteine synthase (CYSM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J. Biol. Chem. 283 (2008) 31567-31574
    • (2008) J. Biol. Chem. , vol.283 , pp. 31567-31574
    • Ågren, D.1    Schnell, R.2    Oehlmann, W.3    Singh, M.4    Schneider, G.5
  • 25
    • 58149488752 scopus 로고    scopus 로고
    • The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
    • Ågren D., Schnell R., and Schneider G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity. FEBS Lett. 583 (2009) 330-336
    • (2009) FEBS Lett. , vol.583 , pp. 330-336
    • Ågren, D.1    Schnell, R.2    Schneider, G.3
  • 26
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • Rabeh W.M., and Cook P.F. Structure and mechanism of O-acetylserine sulfhydrylase. J. Biol. Chem. 279 (2004) 26803-26806
    • (2004) J. Biol. Chem. , vol.279 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 27
    • 34548188995 scopus 로고    scopus 로고
    • Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex
    • Schnell R., Oehlmann W., Singh M., and Schneider G. Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex. J. Biol. Chem. 282 (2007) 23473-23481
    • (2007) J. Biol. Chem. , vol.282 , pp. 23473-23481
    • Schnell, R.1    Oehlmann, W.2    Singh, M.3    Schneider, G.4
  • 30
    • 0030472457 scopus 로고    scopus 로고
    • The relationship between structure and function for the sulfite reductases
    • Crane B.R., and Getzoff E.D. The relationship between structure and function for the sulfite reductases. Curr. Opin. Struct. Biol. 6 (1996) 744-756
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 744-756
    • Crane, B.R.1    Getzoff, E.D.2
  • 31
    • 0034535502 scopus 로고    scopus 로고
    • A simplified functional version of the Escherichia coli sulfite reductase
    • Zeghouf M., Fontecave M., and Coves J. A simplified functional version of the Escherichia coli sulfite reductase. J. Biol. Chem. 275 (2000) 37651-37656
    • (2000) J. Biol. Chem. , vol.275 , pp. 37651-37656
    • Zeghouf, M.1    Fontecave, M.2    Coves, J.3
  • 32
    • 0026097297 scopus 로고
    • Ferredoxin-dependent chloroplast enzymes
    • Knaff D.B., and Hirasawa M. Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta 1056 (1991) 93-125
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 93-125
    • Knaff, D.B.1    Hirasawa, M.2
  • 33
    • 0028809514 scopus 로고
    • Sulfite reductase structure at 1.6 Å: evolution and catalysis for reduction of inorganic anions
    • Crane B.R., Siegel L.M., and Getzoff E.D. Sulfite reductase structure at 1.6 Å: evolution and catalysis for reduction of inorganic anions. Science 270 (1995) 59-67
    • (1995) Science , vol.270 , pp. 59-67
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3
  • 35
    • 0037385630 scopus 로고    scopus 로고
    • Semisynthetic production of unnatural l-alpha-amino acids by metabolic engineering of the cysteine-biosynthetic pathway
    • Maier T.H. Semisynthetic production of unnatural l-alpha-amino acids by metabolic engineering of the cysteine-biosynthetic pathway. Nat. Biotechnol. 21 (2003) 422-427
    • (2003) Nat. Biotechnol. , vol.21 , pp. 422-427
    • Maier, T.H.1
  • 37
    • 0029844625 scopus 로고    scopus 로고
    • A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst
    • Rege V.D., Kredich N.M., Tai C.H., Karsten W.E., Schnackerz K.D., and Cook P.F. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry 35 (1996) 13485-13493
    • (1996) Biochemistry , vol.35 , pp. 13485-13493
    • Rege, V.D.1    Kredich, N.M.2    Tai, C.H.3    Karsten, W.E.4    Schnackerz, K.D.5    Cook, P.F.6
  • 38
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • Huang B., Vetting M.W., and Roderick S.L. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. J. Bacteriol. 187 (2005) 3201-3205
    • (2005) J. Bacteriol. , vol.187 , pp. 3201-3205
    • Huang, B.1    Vetting, M.W.2    Roderick, S.L.3
  • 39
    • 52949126017 scopus 로고    scopus 로고
    • Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis
    • Jurgenson C.T., Burns K.E., Begley T.P., and Ealick S.E. Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis. Biochemistry 47 (2008) 10354-10364
    • (2008) Biochemistry , vol.47 , pp. 10354-10364
    • Jurgenson, C.T.1    Burns, K.E.2    Begley, T.P.3    Ealick, S.E.4
  • 40
    • 0142134254 scopus 로고    scopus 로고
    • A novel O-phospho-l-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1
    • Mino K., and Ishikawa K. A novel O-phospho-l-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1. FEBS Lett. 551 (2003) 133-138
    • (2003) FEBS Lett. , vol.551 , pp. 133-138
    • Mino, K.1    Ishikawa, K.2


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