Tellurite methyltransferase

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

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

  1. Liu, M.; Turner, R.J.; Winstone, T.L.; Saetre, A.; Dyllick-Brenzinger, M.; Jickling, G.; Tari, L.W.; Weiner, J.H.; Taylor, D.E. (2000). "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance". J. Bacteriol. 182: 6509–6513. doi:10.1128/JB.182.22.6509-6513.2000. PMC 94800Freely accessible. PMID 11053398.
  2. Choudhury, H.G.; Cameron, A.D.; Iwata, S.; Beis, K. (2011). "Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli". Biochem. J. 435 (1): 85–91. doi:10.1042/BJ20102014. PMID 21244361.
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