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Volumn 1854, Issue 9, 2015, Pages 1175-1183

Pyridoxal-phosphate dependent mycobacterial cysteine synthases: Structure, mechanism and potential as drug targets

Author keywords

Abbreviations OAS O acetyl serine; OPS O phosphoserine; PLP pyridoxal 5 phosphate,APS, adenosine 5 phosphosulfate, SAR, structure activity relationships.

Indexed keywords

BACTERIAL ENZYME; CYSK1 ENZYME; CYSK2 ENZYME; CYSM ENZYME; CYSTEINE SYNTHASE; PHOSPHOSERINE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CYSTEINE;

EID: 84937639072     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.11.010     Document Type: Review
Times cited : (28)

References (52)
  • 3
    • 84883668448 scopus 로고    scopus 로고
    • Modeling the Mycobacterium tuberculosis granuloma - the critical battlefield in host immunity and disease
    • E. Guirado, and L.S. Schlesinger Modeling the Mycobacterium tuberculosis granuloma - the critical battlefield in host immunity and disease Front. Immunol. 4 2013 98
    • (2013) Front. Immunol. , vol.4 , pp. 98
    • Guirado, E.1    Schlesinger, L.S.2
  • 4
    • 79951899229 scopus 로고    scopus 로고
    • For better or for worse: the immune response against Mycobacterium tuberculosis balances pathology and protection
    • A. Dorhoi, S.T. Reece, and S.H. Kaufmann For better or for worse: the immune response against Mycobacterium tuberculosis balances pathology and protection Immunol. Rev. 240 2011 235 251
    • (2011) Immunol. Rev. , vol.240 , pp. 235-251
    • Dorhoi, A.1    Reece, S.T.2    Kaufmann, S.H.3
  • 6
  • 7
    • 67650164516 scopus 로고    scopus 로고
    • Mycobacterial survival strategies in the phagosome: defence against host stresses
    • S. Ehrt, and D. Schnappinger Mycobacterial survival strategies in the phagosome: defence against host stresses Cell. Microbiol. 11 2009 1170 1178
    • (2009) Cell. Microbiol. , vol.11 , pp. 1170-1178
    • Ehrt, S.1    Schnappinger, D.2
  • 8
    • 84859645414 scopus 로고    scopus 로고
    • The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species
    • M.I. Voskuil, I.L. Bartek, K. Visconti, and G.K. Schoolnik The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species Front. Microbiol. 2 2011 105
    • (2011) Front. Microbiol. , vol.2 , pp. 105
    • Voskuil, M.I.1    Bartek, I.L.2    Visconti, K.3    Schoolnik, G.K.4
  • 9
    • 3042838120 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy
    • M.I. Voskuil, K.C. Visconti, and G.K. Schoolnik Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy Tuberculosis 84 2004 218 227
    • (2004) Tuberculosis , vol.84 , pp. 218-227
    • Voskuil, M.I.1    Visconti, K.C.2    Schoolnik, G.K.3
  • 10
    • 0242407452 scopus 로고    scopus 로고
    • Mycothiol is essential for growth of Mycobacterium tuberculosis
    • D. Sareen, G.L. Newton, R.C. Fahey, and N.A. Buchmeier Mycothiol is essential for growth of Mycobacterium tuberculosis J. Bacteriol. 185 2003 6736 6740
    • (2003) J. Bacteriol. , vol.185 , pp. 6736-6740
    • Sareen, D.1    Newton, G.L.2    Fahey, R.C.3    Buchmeier, N.A.4
  • 11
    • 33748987070 scopus 로고    scopus 로고
    • A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress
    • N.A. Buchmeier, G.L. Newton, and R.C. Fahey A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress J. Bacteriol. 188 2006 6245 6252
    • (2006) J. Bacteriol. , vol.188 , pp. 6245-6252
    • Buchmeier, N.A.1    Newton, G.L.2    Fahey, R.C.3
  • 12
    • 58949091991 scopus 로고    scopus 로고
    • Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular molecular weight thiol in actinomycetes
    • V.K. Jothivasan, and C.J. Hamilton Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular molecular weight thiol in actinomycetes Nat. Prod. Rep. 25 2008 1091 1117
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 1091-1117
    • Jothivasan, V.K.1    Hamilton, C.J.2
  • 13
    • 0030792817 scopus 로고    scopus 로고
    • Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis
    • C. Bornemann, M.A. Jardine, H.S. Spies, and D.J. Steenkamp 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
  • 14
    • 77952310116 scopus 로고    scopus 로고
    • Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis
    • R. Schnell, and G. Schneider Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis Biochem. Biophys. Res. Commun. 396 2010 33 38
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 33-38
    • Schnell, R.1    Schneider, G.2
  • 15
    • 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
    • R. Schnell, W. Oehlmann, M. Singh, and G. Schneider 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
  • 16
    • 52949126017 scopus 로고    scopus 로고
    • Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis
    • C.T. Jurgenson, K.E. Burns, T.P. Begley, and S.E. Ealick 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
  • 17
    • 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
    • D. Ågren, R. Schnell, D.W. Oehlmann, M. Singh, and G. Schneider 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, D.W.3    Singh, M.4    Schneider, G.5
  • 18
    • 0343851637 scopus 로고    scopus 로고
    • The manifold of vitamin B6 dependent enzymes
    • G. Schneider, H. Käck, and Y. Lindqvist The manifold of vitamin B6 dependent enzymes Structure 8 2000 R1 R6
    • (2000) Structure , vol.8 , pp. R1-R6
    • Schneider, G.1    Käck, H.2    Lindqvist, Y.3
  • 19
    • 84907016411 scopus 로고    scopus 로고
    • CysK2 from Mycobacterium tuberculosis is an O-phospho-L-serine dependent S-sulfocysteine synthase
    • E.M. Steiner, D. Böth, P. Lössl, F. Vilaplana, R. Schnell, and G. Schneider CysK2 from Mycobacterium tuberculosis is an O-phospho-L-serine dependent S-sulfocysteine synthase J. Bacteriol. 196 2014 3410 3420
    • (2014) J. Bacteriol. , vol.196 , pp. 3410-3420
    • Steiner, E.M.1    Böth, D.2    Lössl, P.3    Vilaplana, F.4    Schnell, R.5    Schneider, G.6
  • 20
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • W.M. Rabeh, and P.F. Cook 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
  • 21
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - structural and kinetic properties of the free and bound enzymes
    • M. Droux, M.L. Ruffet, R. Dounce, and D. Job Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - structural and kinetic properties of the free and bound enzymes Eur. J. Biochem. 255 1998 235 245
    • (1998) Eur. J. Biochem. , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.L.2    Dounce, R.3    Job, D.4
  • 22
    • 0034278207 scopus 로고    scopus 로고
    • Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus
    • K. Mino, K. Hiraoka, K. Imamura, T. Sakiyama, N. Eisaki, A. Matsuyama, and K. Nakanishi Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus Biosci. Biotechnol. Biochem. 64 2000 1874 1880
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1874-1880
    • Mino, K.1    Hiraoka, K.2    Imamura, K.3    Sakiyama, T.4    Eisaki, N.5    Matsuyama, A.6    Nakanishi, K.7
  • 23
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • B. Huang, M.W. Vetting, and S.L. Roderick 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
  • 24
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
    • J.A. Francois, S. Kumaran, and J.M. Jez Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex Plant Cell 18 2006 3647 3655
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 25
    • 23644440099 scopus 로고    scopus 로고
    • Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy
    • B. Campanini, F. Speroni, E. Salsi, P.F. Cook, S.L. Roderick, B. Huang, S. Bettati, and A. Mozzarelli Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy Protein Sci. 14 2005 2115 2124
    • (2005) Protein Sci. , vol.14 , pp. 2115-2124
    • Campanini, B.1    Speroni, F.2    Salsi, E.3    Cook, P.F.4    Roderick, S.L.5    Huang, B.6    Bettati, S.7    Mozzarelli, A.8
  • 27
    • 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
    • S.E. O'Leary, C.T. Jurgenson, S.E. Ealick, and T.P. Begley 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
  • 28
    • 58149488752 scopus 로고    scopus 로고
    • The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
    • D. Ågren, R. Schnell, and G. Schneider 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
  • 29
    • 79960957242 scopus 로고    scopus 로고
    • The regulation of sulfur metabolism in Mycobacterium tuberculosis
    • S.K. Hatzios, and C.R. Bertozzi The regulation of sulfur metabolism in Mycobacterium tuberculosis PLoS Pathog. 7 2011 e1002036
    • (2011) PLoS Pathog. , vol.7
    • Hatzios, S.K.1    Bertozzi, C.R.2
  • 30
    • 84876131131 scopus 로고    scopus 로고
    • Identification and characterization of serine acetyltransferase encoded by the Mycobacterium tuberculosis Rv2335 gene
    • J. Qiu, D. Wang, Y. Ma, T. Jiang, and Y. Xin Identification and characterization of serine acetyltransferase encoded by the Mycobacterium tuberculosis Rv2335 gene Int. J. Mol. Med. 31 2013 1229 1233
    • (2013) Int. J. Mol. Med. , vol.31 , pp. 1229-1233
    • Qiu, J.1    Wang, D.2    Ma, Y.3    Jiang, T.4    Xin, Y.5
  • 32
    • 14844303715 scopus 로고    scopus 로고
    • The trifunctional sulfate-activating complex (SAC) of Mycobacterium tuberculosis
    • M. Sun, J.L. Andreassi, S. Liu, R. Pinto, J.A. Triccas, and T.S. Leyh The trifunctional sulfate-activating complex (SAC) of Mycobacterium tuberculosis J. Biol. Chem. 280 2005 7861 7866
    • (2005) J. Biol. Chem. , vol.280 , pp. 7861-7866
    • Sun, M.1    Andreassi, J.L.2    Liu, S.3    Pinto, R.4    Triccas, J.A.5    Leyh, T.S.6
  • 34
    • 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
    • R. Schnell, T. Sandalova, U. Hellman, Y. Lindqvist, and G. Schneider 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
  • 35
    • 84861120403 scopus 로고    scopus 로고
    • Enhancement of thioredoxin/glutaredoxin-mediated L-cysteine synthesis from S-sulfocysteine increases L-cysteine production in Escherichia coli
    • T. Nakatani, I. Ohtsu, G. Nonaka, N. Wiriyathanawudhiwong, S. Morigasaki, and H. Takagi Enhancement of thioredoxin/glutaredoxin-mediated L-cysteine synthesis from S-sulfocysteine increases L-cysteine production in Escherichia coli Microb. Cell Factories 11 2012 62
    • (2012) Microb. Cell Factories , vol.11 , pp. 62
    • Nakatani, T.1    Ohtsu, I.2    Nonaka, G.3    Wiriyathanawudhiwong, N.4    Morigasaki, S.5    Takagi, H.6
  • 36
    • 84874767866 scopus 로고    scopus 로고
    • S-sulfocysteine synthase function in sensing chloroplast redox status
    • C. Gotor, and L.C. Romero S-sulfocysteine synthase function in sensing chloroplast redox status Plant Signal. Behav. 8 2013 e23313
    • (2013) Plant Signal. Behav. , vol.8
    • Gotor, C.1    Romero, L.C.2
  • 39
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • J.C. Betts, P.T. Lukey, L.C. Robb, R.A. McAdam, and K. Duncan Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling Mol. Microbiol. 43 2002 717 731
    • (2002) Mol. Microbiol. , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    Mcadam, R.A.4    Duncan, K.5
  • 40
    • 3042790827 scopus 로고    scopus 로고
    • Stationary phase gene expression of Mycobacterium tuberculosis following a progressive nutrient depletion: a model for persistent organisms
    • T. Hampshire, S. Soneji, J. Bacon, B.W. James, J. Hinds, K. Laing, R.A. Stabler, P.D. Marsh, and P.D. Butcher 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
  • 43
    • 20444419421 scopus 로고    scopus 로고
    • Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • J. Rengarajan, B.R. Bloom, and E.J. Rubin Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages Proc. Natl. Acad. Sci. U. S. A. 102 2005 8327 8332
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 44
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • C.M. Sassetti, and E.J. Rubin Genetic requirements for mycobacterial survival during infection Proc. Natl. Acad. Sci. U. S. A. 100 2003 12989 12994
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 45
    • 62449223765 scopus 로고    scopus 로고
    • targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis
    • K. Raman, K. Yeturu, and N. Chandra targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis BMC Syst. Biol. 2 2008 109
    • (2008) BMC Syst. Biol. , vol.2 , pp. 109
    • Raman, K.1    Yeturu, K.2    Chandra, N.3
  • 46
    • 84882750944 scopus 로고    scopus 로고
    • New targets and inhibitors of mycobacterial sulfur metabolism
    • H. Paritala, and K.S. Carroll New targets and inhibitors of mycobacterial sulfur metabolism Infect. Disord. Drug Targets 13 2013 85 115
    • (2013) Infect. Disord. Drug Targets , vol.13 , pp. 85-115
    • Paritala, H.1    Carroll, K.S.2
  • 47
    • 84873723914 scopus 로고    scopus 로고
    • Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening
    • V.U.J. Kumar, O. Poyraz, S. Saxena, R. Schnell, P. Yogeeswari, G. Schneider, and D. Sriram Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening Bioorg. Med. Chem. Lett. 23 2013 1182 1186
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 1182-1186
    • Kumar, V.U.J.1    Poyraz, O.2    Saxena, S.3    Schnell, R.4    Yogeeswari, P.5    Schneider, G.6    Sriram, D.7
  • 48
  • 50
    • 84865490293 scopus 로고    scopus 로고
    • Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase
    • L. Amori, S. Katkevica, A. Bruno, B. Campanini, P. Felici, A. Mozzarelli, and G. Costantino Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase Med. Chem. Commun. 3 2012 1111 1116
    • (2012) Med. Chem. Commun. , vol.3 , pp. 1111-1116
    • Amori, L.1    Katkevica, S.2    Bruno, A.3    Campanini, B.4    Felici, P.5    Mozzarelli, A.6    Costantino, G.7
  • 52
    • 84857099645 scopus 로고    scopus 로고
    • Virtual screening, identification and in vitro testing of novel inhibitors of O-acetyl-L-serine sulfhydrylase of Entamoeba histolytica
    • I. Nagpal, I. Raj, N. Subbarao, and S. Gourinath Virtual screening, identification and in vitro testing of novel inhibitors of O-acetyl-L-serine sulfhydrylase of Entamoeba histolytica PLoS ONE 7 2012 e30305
    • (2012) PLoS ONE , vol.7
    • Nagpal, I.1    Raj, I.2    Subbarao, N.3    Gourinath, S.4


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