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Methylated-thiol---coenzyme M methyltransferase)
Methylated-thiol-coenzyme M methyltransferase ( EC 2.1.1.251, mtsA (gene)) is an enzyme with systematic name methylated-thiol:coenzyme M methyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction:
| methanethiol + coenzyme M ⇌ methyl-CoM + hydrogen sulfide (overall reaction) | (1) |
| methanethiol + [Co(I) methylated-thiol-specific corrinoid protein] ⇌ [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide | (1a) |
| [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M ⇌ methyl-CoM + [Co(I) methylated-thiol-specific corrinoid protein] | (1b) |
| Methylated-thiol-coenzyme M methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.251 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme involved in methanogenesis from methylated thiols, such as methanethiol, dimethyl sulfide, and 3-S-methylmercaptopropionate.
References
- ^ Paul L, Krzycki JA (November 1996). "Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase". Journal of Bacteriology. 178 (22): 6599–607. doi: 10.1128/jb.178.22.6599-6607.1996. PMC 178547. PMID 8932317.
- ^ Tallant TC, Krzycki JA (November 1997). "Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate". Journal of Bacteriology. 179 (22): 6902–11. doi: 10.1128/jb.179.22.6902-6911.1997. PMC 179627. PMID 9371433.
- ^ Tallant TC, Paul L, Krzycki JA (February 2001). "The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer". The Journal of Biological Chemistry. 276 (6): 4485–93. doi: 10.1074/jbc.m007514200. PMID 11073950.
External links
- Methylated-thiol---coenzyme+M+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
