Tellurite methyltransferase

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Tellurite methyltransferase
Identifiers
EC no. 2.1.1.265
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PRIAM profile
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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.

Related Research Articles

<span class="mw-page-title-main">Dimethyl telluride</span> Chemical compound

Dimethyl telluride is an organotelluride compound, formula (CH3)2Te, also known by the abbreviation DMTe.

In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Uroporphyrinogen-III C-methyltransferase</span> Class of enzymes

Uroporphyrinogen-III C-methyltransferase, uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase. This enzyme catalyses the following chemical reaction

Demethylmenaquinone methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:demethylmenaquinone methyltransferase. This enzyme catalyses the following chemical reaction

Methyl halide transferase is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1207-N2)-methyltransferase (EC 2.1.1.172, m2G1207 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1207-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine2445-N2)-methyltransferase (EC 2.1.1.173, ycbY (gene), rlmL (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2445-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine967-C5)-methyltransferase (EC 2.1.1.176, rsmB (gene), fmu (gene), 16S rRNA m5C967 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine967-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (EC 2.1.1.182, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanosine2251-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (cytosine1962-C5)-methyltransferase (EC 2.1.1.191, RlmI, rRNA large subunit methyltransferase I, YccW) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytosine1962-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

Malonyl-CoA O-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:malonyl-CoA O-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (cytidine32/uridine32-2'-O)-methyltransferase (EC 2.1.1.200, YfhQ, tRNA:Cm32/Um32 methyltransferase, TrMet(Xm32), TrmJ) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine32/uridine32-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (cytidine34-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

2-polyprenyl-6-hydroxyphenol methylase is an enzyme with systematic name S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (guanine37-N1)-methyltransferase (EC 2.1.1.228, TrmD, tRNA (m1G37) methyltransferase, transfer RNA (m1G37) methyltransferase, Trm5p, TRMT5, tRNA-(N1G37) methyltransferase, MJ0883 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

Erythromycin 3''-O-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:erythromycin C 3''-O-methyltransferase. This enzyme catalyses the following chemical reaction

References

  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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