Tellurite methyltransferase
Tellurite methyltransferase (EC 2.1.1.265, TehB) is an enzyme with systematic name S-adenosyl-L-methionine:tellurite methyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + tellurite S-adenosyl-L-homocysteine + methanetelluronate
| Tellurite methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.265 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The enzyme is involved in the detoxification of tellurite.
References
- Liu M, Turner RJ, Winstone TL, Saetre A, Dyllick-Brenzinger M, Jickling G, Tari LW, Weiner JH, Taylor DE (November 2000). "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance". Journal of Bacteriology. 182 (22): 6509–13. doi:10.1128/JB.182.22.6509-6513.2000. PMC 94800. PMID 11053398.
- Choudhury HG, Cameron AD, Iwata S, Beis K (April 2011). "Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli". The Biochemical Journal. 435 (1): 85–91. doi:10.1042/BJ20102014. PMID 21244361.
External links
- Tellurite+methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.