Coenzyme M

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

Identifiers

CAS Number

* 3375-50-6 (sulfonic acid form) Y
* 40292-31-7 (sulfonate form)

3D model (JSmol)

* Interactive image

ChEBI |

* CHEBI:58319 Y

ChemSpider |

* 3935 Y

PubChem CID

* 4077

UNII |

* VHD28S0H7F (sulfonic acid form) Y

InChI

* InChI=1S/C2H6O3S2/c3-7(4,5)2-1-6/h6H,1-2H2,(H,3,4,5)/p-1 Y

Key: ZNEWHQLOPFWXOF-UHFFFAOYSA-M Y

SMILES

* [O-]S(=O)(=O)CCS

Properties

Chemical formula

| 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).

Infobox references

Tracking categories (test):

* SizeSet

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] It is also a necessary cofactor in the metabolic pathway of alkene-oxidizing bacteria. CoM helps eliminate the toxic epoxides formed from the oxidation of alkenes such as propylene.[4] The structure of this coenzyme was discovered by CD Taylor and RS Wolfe in 1974 while they were studying methanogenesis, the process by which carbon dioxide is transformed into methane in some archaea.[5] The coenzyme is an anion with the formula HSCH2CH2SO−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.

## Contents

* 1 Biochemical role
* 1.1 Methanogenesis
* 1.2 Alkene metabolism
* 2 Biosynthesis
* 3 See also
* 4 References

## Biochemical role

### Methanogenesis

The coenzyme is the C1 donor in methanogenesis. It is converted to methyl-coenzyme M thioether, the thioether CH3SCH2CH2SO−3, in the penultimate step to methane formation.[6] Methyl-coenzyme M reacts with coenzyme B, 7-thioheptanoylthreoninephosphate, to give a heterodisulfide, releasing methane:

CH3–S–CoM + HS–CoB → CH4 \+ CoB–S–S–CoM

This induction is catalyzed by the enzyme methyl-coenzyme M reductase, which restricts cofactor F430 as the prosthetic group.

CH3-S-CoM is produced by the MtaA-catalyzed reaction between a methylated version of monomethylamine corrinoid protein MtmC and HS-CoM. The methylated version of MtmC is in turn produced by a cobamide-dependent methyltransferase that uses trimethylamine (TMA), dimethylamine (DMA), or monomethylamine (MMA) as the methyl donor.[7]

### Alkene metabolism

Coenzyme M is also used to make acetoacetate from CO2 and propylene or ethylene in aerobic bacteria. Specifically, in bacteria that oxidize alkenes into epoxides. After the propylene (or other alkene) undergoes epoxidation and becomes epoxypropane it becomes electrophilic and toxic. These epoxides react with DNA and proteins, affecting cell function. Alkene-oxidizing bacteria like Xanthobacter autotrophicus[4] use a metabolic pathway in which CoM is conjugated with an aliphatic epoxide. This step creates a nucleophilic compound which can react with CO2. The eventual carboxylation produces acetoacetate, breaking down the propylene.[4]

## Biosynthesis

Bacteria and archaea use different synthetic routes, albeit both starting with phosphoenolpyruvate.[8]

## See also

* Mesna – a cancer chemotherapy adjuvant with the same structure

## References

1. ↑ "Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid)". J. Bacteriol. 137 (1): 256–63. 1979. doi:10.1128/JB.137.1.256-263.1979. PMID 104960.
2. ↑ "Structure and methylation of coenzyme M(HSCH2CH2SO3)". J. Biol. Chem. 249 (15): 4879–85. 10 August 1974. doi:10.1016/S0021-9258(19)42403-4. PMID 4367810.HSCH2CH2SO3)&rft.jtitle=J.+Biol.+Chem.&rft.date=10+August+1974&rft.volume=249&rft.issue=15&rft.pages=4879–85&rft_id=info:doi/10.1016/S0021-9258(19)42403-4&rft_id=info:pmid/4367810&rfr_id=info:sid/en.wikibooks.org:Chemistry:Coenzyme_M">
3. ↑ Partovi, Sarah E.; Mus, Florence; Gutknecht, Andrew E.; Martinez, Hunter A.; Tripet, Brian P.; Lange, Bernd Markus; DuBois, Jennifer L.; Peters, John W. (2018-04-06). "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. PMID 29414784.
4. ↑ 4.0 4.1 4.2 Krishnakumar, Arathi M.; Sliwa, Darius; Endrizzi, James A.; Boyd, Eric S.; Ensign, Scott A.; Peters, John W. (September 2008). "Getting a Handle on the Role of Coenzyme M in Alkene Metabolism". Microbiology and Molecular Biology Reviews 72 (3): 445–456. doi:10.1128/MMBR.00005-08. ISSN 1092-2172. PMID 18772284.
5. ↑ Parry, Ronald J. (1999-01-01), Barton, Sir Derek; Nakanishi, Koji; Meth-Cohn, Otto, eds., "1.29 - Biosynthesis of Sulfur-containing Natural Products" (in en), Comprehensive Natural Products Chemistry (Oxford: Pergamon): pp. 825–863, doi:10.1016/b978-0-08-091283-7.00031-x, ISBN 978-0-08-091283-7, https://www.sciencedirect.com/science/article/pii/B978008091283700031X, retrieved 2022-05-10
6. ↑ Thauer, Rudolf K. (1998-09-01). "Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture" (in en). Microbiology 144 (9): 2377–2406. doi:10.1099/00221287-144-9-2377. ISSN 1350-0872. PMID 9782487.
7. ↑ Ferguson, Tsuneo; Soares, Jitesh A.; Lienard, Tanja; Gottschalk, Gerhard; Krzycki, Joseph A. (January 2009). "RamA, a Protein Required for Reductive Activation of Corrinoid-dependent Methylamine Methyltransferase Reactions in Methanogenic Archaea". Journal of Biological Chemistry 284 (4): 2285–2295. doi:10.1074/jbc.M807392200. PMID 19043046.
8. ↑ Wu, Hsin-Hua; Pun, Michael D.; Wise, Courtney E.; Streit, Bennett R.; Mus, Florence; Berim, Anna; Kincannon, William M.; Islam, Abdullah et al. (6 September 2022). "The pathway for coenzyme M biosynthesis in bacteria". Proceedings of the National Academy of Sciences 119 (36). doi:10.1073/pnas.2207190119. PMID 36037354. Bibcode: 2022PNAS..11907190W.

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Enzyme cofactors

Active forms|

| vitamins|

* TPP / ThDP (B1)
* FMN, FAD (B2)
* NAD+, NADH, NADP+, NADPH (B3)
* Coenzyme A (B5)
* PLP / P5P (B6)
* Biotin (B7)
* THFA / H4FA, DHFA / H2FA, MTHF (B9)
* AdoCbl, MeCbl (B12)
* Ascorbic acid (C)
* Phylloquinone (K1), Menaquinone (K2)
* Coenzyme F420

|

non-vitamins|

* ATP
* CTP
* SAMe
* PAPS
* GSH
* Coenzyme B
* Cofactor F430
* Coenzyme M
* Coenzyme Q
* Heme / Haem (A, B, C, O)
* Lipoic Acid
* Methanofuran
* Molybdopterin/Molybdenum cofactor
* PQQ
* THB / BH4
* THMPT / H4MPT

metal ions|

* Ca2+
* Cu2+
* Fe2+, Fe3+
* Mg2+
* Mn2+
* Mo
* Ni2+
* Zn2+

Base forms|

* vitamins: see vitamins

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