serine biosynthesis
Accession ID: BioCyc:LEISH_SERSYN-PWY |
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Opperdoes FR, Coombs GH. Metabolism of Leishmania: proven and predicted. Trends Parasitol. 2007 Apr;23(4):149–58. doi: 10.1016/j.pt.2007.02.004. PMID: 17320480. |
superpathway of serine and glycine biosynthesis I
Accession ID: BioCyc:LEISH_SER-GLYSYN-PWY |
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Mycobacterium tuberculosis biological processes
Accession ID: Reactome:R-MTU-870392 |
10.1006/jmbi.1999.298010.1006/prep.2001.145710.1007/s00203-002-0462-y10.1016/j.abb.2004.02.01410.1016/j.jmb.2005.09.09310.1016/j.pep.2004.06.04010.1016/j.pep.2005.10.00410.1016/s0969-2126(02)00718-910.1016/s1046-5928(02)00509-010.1021/bi012212u10.1021/bi030080u10.1021/bi702453s10.1021/bi801366410.1021/bi991025h10.1021/ja053476x10.1042/bj2003064210.1042/bj287017310.1046/j.1365-2958.2002.02771.x10.1046/j.1365-2958.2003.03900.x10.1046/j.1432-1033.2002.03327.x10.1074/jbc.m20461320010.1074/jbc.m30891420010.1074/jbc.m40961320010.1074/jbc.m41254020010.1074/jbc.m50256020010.1074/jbc.m60472420010.1074/jbc.m70351820010.1074/jbc.m80101720010.1074/jbc.m80487720010.1099/00221287-146-1-19910.1099/00221287-148-10-296710.1099/mic.0.26894-010.1111/j.1574-6968.2005.00068.x10.1111/j.1574-6976.2006.00062.x10.1128/jb.00064-0910.1128/jb.00425-0710.1128/jb.00487-0710.1128/jb.172.12.6774-6782.199010.1128/jb.182.24.6958-6963.200010.1128/mmbr.00008-0810.1186/1471-2091-9-1310.1186/1471-2180-10-5010.1371/journal.pbio.003025010.1586/eri.10.60
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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.; Newton GL, Buchmeier N, Fahey RC. Biosynthesis and Functions of Mycothiol, the Unique Protective Thiol of Actinobacteria. Microbiol Mol Biol Rev. 2008 Sep;72(3):471–94. doi: 10.1128/mmbr.00008-08.; Vetting MW, Frantom PA, Blanchard JS. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J Biol Chem. 2008 Jun 06;283(23):15834–44. PMID: 18390549; PMCID: PMC2414306.; 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.; Ely F, Nunes JE, Schroeder EK, Frazzon J, Palma MS, Santos DS, Basso LA. The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase. BMC Molecular and Cell Biology. 2008 Apr 29;9(1):13. doi: 10.1186/1471-2091-9-13.; 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.; de Mendonc¸a JD, Ely F, Palma MS, Frazzon J, Basso LA, Santos DS. Functional Characterization by Genetic Complementation of aroB -Encoded Dehydroquinate Synthase from Mycobacterium tuberculosis H37Rv and Its Heterologous Expression and Purification. J Bacteriol. 2007 Sep;189(17):6246–52. doi: 10.1128/jb.00425-07.; 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.; Rawat M, Av-Gay Y. Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol Rev. 2007 Apr;31(3):278–92. doi: 10.1111/j.1574-6976.2006.00062.x. PMID: 17286835.; Newton GL, Ta P, Bzymek KP, Fahey RC. Biochemistry of the Initial Steps of Mycothiol Biosynthesis. Journal of Biological Chemistry. 2006 Nov;281(45):33910–20. doi: 10.1074/jbc.m604724200.; Fonseca IO, Magalhães MLB, Oliveira JS, Silva RG, Mendes MA, Palma MS, Santos DS, Basso LA. Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: Purification and characterization. Protein Expression and Purification. 2006 Apr;46(2):429–37. doi: 10.1016/j.pep.2005.10.004.; 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.; Webby CJ, Baker HM, Lott JS, Baker EN, Parker EJ. The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes. J Mol Biol. 2005 Dec 09;354(4):927–39. doi: 10.1016/j.jmb.2005.09.093. PMID: 16288916.; 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.; Rizzi C, Frazzon J, Ely F, Weber PG, da Fonseca IO, Gallas M, Oliveira JS, Mendes MA, de Souza BM, Palma MS, Santos DS, Basso LA. DAHP synthase from Mycobacterium tuberculosis H37Rv: cloning, expression, and purification of functional enzyme. Protein Expression and Purification. 2005 Mar;40(1):23–30. doi: 10.1016/j.pep.2004.06.040.; Edavana VK, Pastuszak I, Carroll JD, Thampi P, Abraham EC, Elbein AD. Cloning and expression of the trehalose-phosphate phosphatase of Mycobacterium tuberculosis: comparison to the enzyme from Mycobacterium smegmatis. Archives of Biochemistry and Biophysics. 2004 Jun;426(2):250–7. doi: 10.1016/j.abb.2004.02.014.; 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.; Movahedzadeh F, Smith DA, Norman RA, Dinadayala P, Murray-Rust J, Russell DG, Kendall SL, Rison SCG, McAlister MSB, Bancroft GJ, McDonald NQ, Daffe M, Av-Gay Y, Stoker NG. The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence. Molecular Microbiology. 2003 Dec 23;51(4):1003–14. doi: 10.1046/j.1365-2958.2003.03900.x.; Maynes JT, Garen C, Cherney MM, Newton G, Arad D, Av-Gay Y, Fahey RC, James MN. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J Biol Chem. 2003 Nov 21;278(47):47166–70. doi: 10.1074/jbc.m308914200. PMID: 12958317.; Steffek M, Newton GL, Av-Gay Y, Fahey RC. Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. Biochemistry. 2003 Oct 21;42(41):12067–76. doi: 10.1021/bi030080u. PMID: 14556638.; Vogt RN, Steenkamp DJ, Zheng R, Blanchard JS. The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem J. 2003 Sep 15;374(Pt 3):657–66. PMID: 12809551; PMCID: PMC1223637.; Pan YT, Carroll JD, Elbein AD. Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur J Biochem. 2002 Dec;269(24):6091–100. doi: 10.1046/j.1432-1033.2002.03327.x. PMID: 12473104.; Koledin T, Newton GL, Fahey RC. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch Microbiol. 2002 Nov;178(5):331–7. doi: 10.1007/s00203-002-0462-y. PMID: 12375100.; Camus JC, Pryor MJ, Médigue C, Cole ST. Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Microbiology (Reading). 2002 Oct;148(Pt 10):2967–73. doi: 10.1099/00221287-148-10-2967. PMID: 12368430.; Magalhães MLB, Pereira CP, Basso LA, Santos DS. Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv. Protein Expression and Purification. 2002 Oct;26(1):59–64. doi: 10.1016/s1046-5928(02)00509-0.; 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.; Sareen D, Steffek M, Newton GL, Fahey RC. ATP-Dependent l-Cysteine:1d-myo-Inosityl 2-Amino-2-deoxy-a-d-glucopyranoside Ligase, Mycothiol Biosynthesis Enzyme MshC, Is Related to Class I Cysteinyl-tRNA Synthetases. Biochemistry. 2002 May 10;41(22):6885–90. doi: 10.1021/bi012212u.; Norman RA, McAlister MS, Murray-Rust J, Movahedzadeh F, Stoker NG, McDonald NQ. Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis. Structure. 2002 Mar;10(3):393–402. doi: 10.1016/s0969-2126(02)00718-9. PMID: 12005437.; 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.; Oliveira JS, Pinto CA, Basso LA, Santos DS. Cloning and Overexpression in Soluble Form of Functional Shikimate Kinase and 5-Enolpyruvylshikimate 3-Phosphate Synthase Enzymes from Mycobacterium tuberculosis. Protein Expression and Purification. 2001 Aug;22(3):430–5. doi: 10.1006/prep.2001.1457.; Newton GL, Av-gay Y, Fahey RC. N -Acetyl-1- d - myo -Inosityl-2-Amino-2-Deoxy-a- d -Glucopyranoside Deacetylase (MshB) Is a Key Enzyme in Mycothiol Biosynthesis. J Bacteriol. 2000 Dec 15;182(24):6958–63. doi: 10.1128/jb.182.24.6958-6963.2000.; De Smet KAL, Weston A, Brown IN, Young DB, Robertson BD. Three pathways for trehalose biosynthesis in mycobacteria. Microbiology (Reading). 2000 Jan;146 ( Pt 1)():199–208. doi: 10.1099/00221287-146-1-199. PMID: 10658666.; Bachhawat N, Mande SC. Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme 1 1Edited by M. Yaniv. Journal of Molecular Biology. 1999 Aug;291(3):531–6. doi: 10.1006/jmbi.1999.2980.; Patel MP, Blanchard JS. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry. 1999 Sep 07;38(36):11827–33. doi: 10.1021/bi991025h. PMID: 10512639.; Moore JD, Lamb HK, Garbe T, Servos S, Dougan G, Charles IG, Hawkins AR. Inducible overproduction of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dehydroquinases from Salmonella typhi and Mycobacterium tuberculosis. Biochem J. 1992 Oct 01;287 ( Pt 1)():173–81. PMID: 1329726; PMCID: PMC1133140.; Garbe T, Jones C, Charles I, Dougan G, Young D. Cloning and characterization of the aroA gene from Mycobacterium tuberculosis. J Bacteriol. 1990 Dec;172(12):6774–82. doi: 10.1128/jb.172.12.6774-6782.1990. |
Sulfur amino acid metabolism
Accession ID: Reactome:R-MTU-937250 |
10.1016/j.bbrc.2010.02.11810.1021/bi801366410.1021/ja053476x10.1074/jbc.m20461320010.1074/jbc.m41254020010.1074/jbc.m50256020010.1074/jbc.m70351820010.1074/jbc.m80487720010.1111/j.1574-6968.2005.00068.x10.1128/jb.00064-0910.1128/jb.00487-0710.1371/journal.pbio.0030250
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Schnell R, Schneider G. Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis. Biochemical and Biophysical Research Communications. 2010 May;396(1):33–8. doi: 10.1016/j.bbrc.2010.02.118.; 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.; 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.; 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.; 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. |
Sulfur compound metabolism
Accession ID: Reactome:R-MTU-936621 |
10.1021/bi702453s10.1021/bi801366410.1021/ja053476x10.1046/j.1365-2958.2002.02771.x10.1074/jbc.m20461320010.1074/jbc.m40961320010.1074/jbc.m41254020010.1074/jbc.m50256020010.1074/jbc.m70351820010.1074/jbc.m80487720010.1099/mic.0.26894-010.1111/j.1574-6968.2005.00068.x10.1128/jb.00064-0910.1128/jb.00487-0710.1371/journal.pbio.003025010.2174/187152607781001772
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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. |
Cysteine synthesis from O-phosphoserine
Accession ID: Reactome:R-MTU-936654 |
10.1021/bi801366410.1021/ja053476x10.1074/jbc.m804877200
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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.; 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. |
Serine biosynthesis
Accession ID: WikiPathways:WP459 |
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Trans-sulfuration, one-carbon metabolism and related pathways
Accession ID: WikiPathways:WP2525 |
10.1016/j.cmet.2016.08.009
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Ducker GS, Rabinowitz JD. One-Carbon Metabolism in Health and Disease. Cell Metabolism. 2017 Jan;25(1):27–42. doi: 10.1016/j.cmet.2016.08.009. |
Biochemical pathways: part I
Accession ID: WikiPathways:WP3604 |
10.1016/s0303-2647(98)00019-7
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Michal G. On representation of metabolic pathways. Biosystems. 1998 Jun;47(1-2):1–7. doi: 10.1016/s0303-2647(98)00019-7. PMID: 9715748. |
Amino acid metabolism in triple-negative breast cancer cells
Accession ID: WikiPathways:WP5213 |
10.1158/0008-5472.can-14-3745
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Bhutia YD, Babu E, Ramachandran S, Ganapathy V. Amino Acid transporters in cancer and their relevance to 'glutamine addiction': novel targets for the design of a new class of anticancer drugs. Cancer Res. 2015 May 01;75(9):1782–8. doi: 10.1158/0008-5472.can-14-3745. PMID: 25855379. |
Metabolic Epileptic Disorders
Accession ID: WikiPathways:WP5355 |
10.1038/s41418-020-0491-6
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Tan M, Mosaoa R, Graham GT, Kasprzyk-Pawelec A, Gadre S, Parasido E, Catalina-Rodriguez O, Foley P, Giaccone G, Cheema A, Kallakury B, Albanese C, Yi C, Avantaggiati ML. Inhibition of the mitochondrial citrate carrier, Slc25a1, reverts steatosis, glucose intolerance, and inflammation in preclinical models of NAFLD/NASH. Cell Death & Differentiation. 2020 Jan 20;27(7):2143–57. doi: 10.1038/s41418-020-0491-6. |
Trans-sulfuration and one-carbon metabolism
Accession ID: WikiPathways:WP3135 |
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