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Pathway Description
Hydrogen Sulfide Biosynthesis I
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-10-09
Last Updated: 2019-08-13
Many bacteria can produce hydrogen sulfide, which can be used as defense system against antibiotics and oxidative stress. This pathway is one of the hydrogen sulfide biosynthesis pathways (totally two). L-Cysteine is transported by L-cysteine ABC transporter and convert to 3-mercaptopyruvic acid by facilitation of aspartate aminotransferase. 3-Mercaptopyruvic acid is later catalyzed to form pyruvic acid and hydrogen sulfide by 3-mercaptopyruvate sulfurtransferase.
References
Hydrogen Sulfide Biosynthesis I References
Barrett EL, Clark MA: Tetrathionate reduction and production of hydrogen sulfide from thiosulfate. Microbiol Rev. 1987 Jun;51(2):192-205.
Pubmed: 3299028
Kuramitsu S, Okuno S, Ogawa T, Ogawa H, Kagamiyama H: Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene. J Biochem. 1985 Apr;97(4):1259-62. doi: 10.1093/oxfordjournals.jbchem.a135173.
Pubmed: 3897210
Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, Primrose SB, Parker DM, Edwards RM: The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem J. 1986 Mar 15;234(3):593-604. doi: 10.1042/bj2340593.
Pubmed: 3521591
Kondo K, Wakabayashi S, Yagi T, Kagamiyama H: The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. Biochem Biophys Res Commun. 1984 Jul 18;122(1):62-7. doi: 10.1016/0006-291x(84)90439-x.
Pubmed: 6378205
Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D: The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli. J Mol Biol. 2004 Jan 9;335(2):583-93. doi: 10.1016/j.jmb.2003.10.072.
Pubmed: 14672665
Hama H, Kayahara T, Ogawa W, Tsuda M, Tsuchiya T: Enhancement of serine-sensitivity by a gene encoding rhodanese-like protein in Escherichia coli. J Biochem. 1994 Jun;115(6):1135-40. doi: 10.1093/oxfordjournals.jbchem.a124469.
Pubmed: 7982894
Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
Pubmed: 9205837
Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. doi: 10.1093/dnares/3.6.379.
Pubmed: 9097040
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Mytelka DS, Chamberlin MJ: Escherichia coli fliAZY operon. J Bacteriol. 1996 Jan;178(1):24-34. doi: 10.1128/jb.178.1.24-34.1996.
Pubmed: 8550423
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