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| Names | |
|---|---|
| IUPAC name 2-Sulfanylethanesulfonate | |
| Systematic IUPAC name 2-Sulfanylethanesulfonate | |
| Other names 2-mercaptoethylsulfonate; 2-mercaptoethanesulfonate; coenzyme M anion; H-S-CoM; AC1L1HCY; 2-sulfanylethane-1-sulfonate; CTK8A8912 | |
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3D model (JSmol) | |
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| Properties | |
| C2H5O3S2 | |
| Molar mass | 141.18 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens,[1][2] and in the metabolism of other substrates in bacteria.[3] The coenzyme is an anion with the formula HSCH
2CH
2SO−
3. It is named 2-mercaptoethanesulfonate and abbreviated HS–CoM. The cation is unimportant, but the sodium salt is most available. Mercaptoethanesulfonate contains both a thiol, which is the main site of reactivity, and a sulfonate group, which confers solubility in aqueous media.
Biochemical role
The coenzyme is the C1 donor in methanogenesis. It is converted to methyl-coenzyme M thioether, the thioether CH
3SCH
2CH
2SO−
3, in the penultimate step to methane formation.[4] Methyl-coenzyme M reacts with coenzyme B, 7-thioheptanoylthreoninephosphate, to give a heterodisulfide, releasing methane:
- CH
3–S–CoM + HS–CoB → CH
4 + CoB–S–S–CoM
This induction is catalyzed by the enzyme methyl-coenzyme M reductase, which restricts cofactor F430 as the prosthetic group.
See also
- Mesna – a cancer chemotherapy adjuvant with the same structure
References
- ^ Balch WE, Wolfe RS (1979). "Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid)". J. Bacteriol. 137 (1): 256–63. doi:10.1128/JB.137.1.256-263.1979. PMC 218444. PMID 104960.
- ^ Taylor CD, Wolfe RS (10 August 1974). "Structure and methylation of coenzyme M(HSCH
2CH
2SO
3)". J. Biol. Chem. 249 (15): 4879–85. PMID 4367810. - ^ Partovi, Sarah E.; Mus, Florence; Gutknecht, Andrew E.; Martinez, Hunter A.; Tripet, Brian P.; Lange, Bernd Markus; DuBois, Jennifer L.; Peters, John W. (04 06, 2018). "Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily". The Journal of Biological Chemistry. 293 (14): 5236–5246. doi:10.1074/jbc.RA117.001234. ISSN 1083-351X. PMC 5892593. PMID 29414784.
- ^ Thauer RK (1998). "Biochemistry of Methanogenesis: a Tribute to Marjory Stephenson". Microbiology. 144 (9): 2377–2406. doi:10.1099/00221287-144-9-2377. PMID 9782487.