Sulfur compound metabolism
Mehra S, Kaushal D. Functional Genomics Reveals Extended Roles of the Mycobacterium tuberculosis Stress Response Factor s H. J Bacteriol. 2009 Jun 15;191(12):3965–80. doi: 10.1128/jb.00064-09.; Agren D, Schnell R, Oehlmann W, Singh M, 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. 2008 Nov 14;283(46):31567–74. doi: 10.1074/jbc.m804877200. PMID: 18799456.; O’Leary SE, Jurgenson CT, Ealick SE, Begley TP. O-Phospho-l-serine and the Thiocarboxylated Sulfur Carrier Protein CysO-COSH Are Substrates for CysM, a Cysteine Synthase from Mycobacterium tuberculosis. Biochemistry. 2008 Oct 09;47(44):11606–15. doi: 10.1021/bi8013664.; Hatzios SK, Iavarone AT, Bertozzi CR. Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase. Biochemistry. 2008 May 27;47(21):5823–31. PMID: 18454554; PMCID: PMC2711008.; Pinto R, Harrison JS, Hsu T, Jacobs WR, Leyh TS. Sulfite reduction in mycobacteria. J Bacteriol. 2007 Sep;189(18):6714–22. PMID: 17644602; PMCID: PMC2045171.; Schnell R, Oehlmann W, Singh M, 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. 2007 Aug 10;282(32):23473–81. doi: 10.1074/jbc.m703518200. PMID: 17567578.; Devayani P. Bhave, Wilson B. Muse III, Kate S. Carroll. Drug Targets in Mycobacterial Sulfur Metabolism. IDDT. 2007 Jun 01;7(2):140–58. doi: 10.2174/187152607781001772.; Haitani Y, Awano N, Yamazaki M, Wada M, Nakamori S, Takagi H. Functional analysis of L-serine O-acetyltransferase from Corynebacterium glutamicum. FEMS Microbiol Lett. 2006 Feb;255(1):156–63. doi: 10.1111/j.1574-6968.2005.00068.x. PMID: 16436075.; Burns KE, Baumgart S, Dorrestein PC, Zhai H, McLafferty FW, Begley TP. Reconstitution of a New Cysteine Biosynthetic Pathway inMycobacteriumtuberculosis. J. Am. Chem. Soc. 2005 Aug 02;127(33):11602–3. doi: 10.1021/ja053476x.; Schnell R, Sandalova T, Hellman U, Lindqvist Y, 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. Journal of Biological Chemistry. 2005 Jul;280(29):27319–28. doi: 10.1074/jbc.m502560200.; Carroll KS, Gao H, Chen H, Stout CD, Leary JA, Bertozzi CR. A Conserved Mechanism for Sulfonucleotide Reduction. PLoS Biol. 2005 Jul 19;3(8):e250. doi: 10.1371/journal.pbio.0030250.; Wheeler PR, Coldham NG, Keating L, Gordon SV, Wooff EE, Parish T, Hewinson RG. Functional Demonstration of Reverse Transsulfuration in the Mycobacterium tuberculosis Complex Reveals That Methionine Is the Preferred Sulfur Source for Pathogenic Mycobacteria. Journal of Biological Chemistry. 2005 Mar;280(9):8069–78. doi: 10.1074/jbc.m412540200.; Sun M, Andreassi JL, Liu S, Pinto R, Triccas JA, Leyh TS. The Trifunctional Sulfate-activating Complex (SAC) of Mycobacterium tuberculosis. Journal of Biological Chemistry. 2005 Mar;280(9):7861–6. doi: 10.1074/jbc.m409613200.; Pinto R, Tang QX, Britton WJ, Leyh TS, Triccas JA. The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex. Microbiology (Reading). 2004 Jun;150(Pt 6):1681–6. doi: 10.1099/mic.0.26894-0. PMID: 15184554.; Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR. 5'-Adenosinephosphosulfate Lies at a Metabolic Branch Point in Mycobacteria. Journal of Biological Chemistry. 2002 Sep;277(36):32606–15. doi: 10.1074/jbc.m204613200.; Wooff E, Michell SL, Gordon SV, Chambers MA, Bardarov S, Jacobs WR, Hewinson RG, Wheeler PR. Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Molecular Microbiology. 2002 Feb;43(3):653–63. doi: 10.1046/j.1365-2958.2002.02771.x.