Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaealmethanogens,[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 anaerobic bacteria.[5] 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.
The coenzyme is the C1 donor in methanogenesis. It is converted to methyl-coenzyme M thioether, the thioetherCH 3SCH 2CH 2SO− 3, in the penultimate step to methane formation.[6] Methyl-coenzyme M reacts with coenzyme B, 7-thioheptanoylthreoninephosphate, to give a heterodisulfide, releasing methane:
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]
See alsoedit
Mesna – a cancer chemotherapy adjuvant with the same structure
Referencesedit
^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. PMC218444. 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. doi:10.1016/S0021-9258(19)42403-4. 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. (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. PMC5892593. PMID 29414784.
^ abcKrishnakumar, 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. PMC2546864. PMID 18772284.
^Parry, Ronald J. (1999-01-01), Barton, Sir Derek; Nakanishi, Koji; Meth-Cohn, Otto (eds.), "1.29 - Biosynthesis of Sulfur-containing Natural Products", Comprehensive Natural Products Chemistry, Oxford: Pergamon, pp. 825–863, doi:10.1016/b978-0-08-091283-7.00031-x, ISBN978-0-08-091283-7, retrieved 2022-05-10
^Thauer, Rudolf K. (1998-09-01). "Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture". Microbiology. 144 (9): 2377–2406. doi:10.1099/00221287-144-9-2377. ISSN 1350-0872. PMID 9782487.
This biochemistry article is a stub. You can help Wikipedia by expanding it.
coenzyme, coenzyme, required, methyl, transfer, reactions, metabolism, archaeal, methanogens, metabolism, other, substrates, bacteria, also, necessary, cofactor, metabolic, pathway, alkene, oxidizing, bacteria, helps, eliminate, toxic, epoxides, formed, from, . 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 anaerobic bacteria 5 The coenzyme is an anion with the formula HSCH2 CH2 SO 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 Coenzyme M NamesIUPAC name 2 SulfanylethanesulfonateSystematic IUPAC name 2 SulfanylethanesulfonateOther names 2 mercaptoethylsulfonate 2 mercaptoethanesulfonate coenzyme M anion H S CoM AC1L1HCY 2 sulfanylethane 1 sulfonate CTK8A8912IdentifiersCAS Number 3375 50 6 sulfonic acid form Y40292 31 7 sulfonate form 3D model JSmol Interactive imageChEBI CHEBI 58319 YChemSpider 3935 YPubChem CID 4077UNII VHD28S0H7F sulfonic acid form YInChI InChI 1S C2H6O3S2 c3 7 4 5 2 1 6 h6H 1 2H2 H 3 4 5 p 1 YKey ZNEWHQLOPFWXOF UHFFFAOYSA M YSMILES O S O O CCSPropertiesChemical formula C 2H 5O 3S 2Molar mass 141 18 g mol 1Except where otherwise noted data are given for materials in their standard state at 25 C 77 F 100 kPa Infobox references Contents 1 Biochemical role 1 1 Methanogenesis 1 2 Alkene metabolism 2 See also 3 ReferencesBiochemical role editMethanogenesis edit The coenzyme is the C1 donor in methanogenesis It is converted to methyl coenzyme M thioether the thioether CH3 SCH2 CH2 SO 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 CoMThis induction is catalyzed by the enzyme methyl coenzyme M reductase which restricts cofactor F430 as the prosthetic group Alkene metabolism edit 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 See also editMesna a cancer chemotherapy adjuvant with the same structureReferences edit 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 HSCH2 CH2 SO3 J Biol Chem 249 15 4879 85 doi 10 1016 S0021 9258 19 42403 4 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 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 PMC 5892593 PMID 29414784 a b c 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 PMC 2546864 PMID 18772284 Parry Ronald J 1999 01 01 Barton Sir Derek Nakanishi Koji Meth Cohn Otto eds 1 29 Biosynthesis of Sulfur containing Natural Products 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 retrieved 2022 05 10 Thauer Rudolf K 1998 09 01 Biochemistry of methanogenesis a tribute to Marjory Stephenson 1998 Marjory Stephenson Prize Lecture Microbiology 144 9 2377 2406 doi 10 1099 00221287 144 9 2377 ISSN 1350 0872 PMID 9782487 nbsp This biochemistry article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Coenzyme M amp oldid 1139773758, wikipedia, wiki, book, books, library,
