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Tellurite methyltransferase

From Wikipedia, the free encyclopedia
Tellurite methyltransferase
Identifiers
EC no.2.1.1.265
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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

The enzyme is involved in the detoxification of tellurite.

References

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  1. ^ 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.
  2. ^ Choudhury HG, Cameron AD, Iwata S, Beis K (April 2011). "Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli" (PDF). The Biochemical Journal. 435 (1): 85–91. doi:10.1042/BJ20102014. PMID 21244361.
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