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EC Tree
IUBMB Comments Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, 1,4-dithiane and many other thioethers.
The enzyme appears in viruses and cellular organisms
Synonyms
thioether s-methyltransferase, thioether methyltransferase,
more
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S-adenosyl-L-methionine:thioether S-methyltransferase
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thioether methyltransferase
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S-adenosyl-L-methionine + dimethyl sulfide + H+ = S-adenosyl-L-homocysteine + trimethylsulfonium
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methyl group transfer
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S-adenosyl-L-methionine:dimethyl-sulfide S-methyltransferase
Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, 1,4-dithiane and many other thioethers.
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S-adenosyl-L-methionine + 1,4-dithiane
S-adenosyl-L-homocysteine + methyl-1,4-dithiane
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?
S-adenosyl-L-methionine + 2-methylthioethanol
S-adenosyl-L-homocysteine + 2,2-dimethylthioethanol
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S-adenosyl-L-methionine + 2-methylthioethylamine
S-adenosyl-L-homocysteine + 2,2-dimethylthioethylamine
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S-adenosyl-L-methionine + 3-methylthiopropionaldehyde
S-adenosyl-L-homocysteine + 3,3-dimethylthiopropionaldehyde
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?
S-adenosyl-L-methionine + benzyl methyl sulfide
S-adenosyl-L-homocysteine + benzyl dimethyl sulfonium
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?
S-adenosyl-L-methionine + diethyl sulfide
S-adenosyl-L-homocysteine + diethylmethylsulfonium
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?
S-adenosyl-L-methionine + dimethyl selenide
S-adenosyl-L-homocysteine + trimethylselenonium
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?
S-adenosyl-L-methionine + dimethyl sulfide
S-adenosyl-L-homocysteine + trimethylsulfonium
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?
S-adenosyl-L-methionine + dimethyl telluride
S-adenosyl-L-homocysteine + trimethyltelluronium
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S-adenosyl-L-methionine + ethyl vinyl sulfide
S-adenosyl-L-homocysteine + methyl ethyl vinyl sulfonium
S-adenosyl-L-methionine + methyl n-propyl sulfide
S-adenosyl-L-homocysteine + dimethyl n-propyl sulfonium
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?
S-adenosyl-L-methionine + pentamethylene sulfide
S-adenosyl-L-homocysteine + pentamethylenemethylsulfonium
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?
S-adenosyl-L-methionine + selenium
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + sulfur
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + tellurium
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + tetrahydrothiophene
S-adenosyl-L-homocysteine + methyltetrahydrothiophene
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?
S-adenosyl-L-methionine + thiomorpholine
S-adenosyl-L-homocysteine + methylthiomorpholine
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additional information
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strain- and infection-related alterations in sleep may be influenced by Temt expression and perhaps by subsequent effects on prostaglandin metabolism, mice treated with the Temt-inhibitor sinefungin develop enhanced sleep
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S-adenosyl-L-methionine + ethyl vinyl sulfide
S-adenosyl-L-homocysteine + methyl ethyl vinyl sulfonium
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S-adenosyl-L-methionine + ethyl vinyl sulfide
S-adenosyl-L-homocysteine + methyl ethyl vinyl sulfonium
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suicide substrate leading to inactivation
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S-adenosyl-L-methionine + selenium
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + sulfur
S-adenosyl-L-homocysteine + ?
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S-adenosyl-L-methionine + tellurium
S-adenosyl-L-homocysteine + ?
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additional information
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strain- and infection-related alterations in sleep may be influenced by Temt expression and perhaps by subsequent effects on prostaglandin metabolism, mice treated with the Temt-inhibitor sinefungin develop enhanced sleep
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ethyl vinyl sulfide
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suicide substrate, inactivation rate constant: 0.05/min, dimethyl sulfide protects
methyl ethyl vinyl sulfonium
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product of ethyl vinyl sulfide methylation inactivates
S-adenosyl-L-homocysteine
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0.04 mM, 50% inhibition
sinefungin
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0.025 mM, 50% inhibition
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0.0004
dimethyl selenide
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0.001
Dimethyl sulfide
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0.001
S-adenosylmethionine
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0.275
ethyl vinyl sulfide
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suicide substrate
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6.3
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sharp drop in activity below
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SwissProt
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male C57BL/6J and BALB/cByJ mice, mice infected with influenza virus for experiments, enzyme mRNA levels in influenza infected mice are different from healthy mice
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INMT_HUMAN
263
0
28891
Swiss-Prot
other Location (Reliability: 2 )
INMT_MOUSE
264
0
29460
Swiss-Prot
other Location (Reliability: 1 )
INMT_PONAB
263
0
28848
Swiss-Prot
other Location (Reliability: 1 )
INMT_RABIT
263
0
28955
Swiss-Prot
other Location (Reliability: 1 )
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29460
1 * 29460, deduced from nucleotide sequence
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monomer
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1 * 28000, SDS-PAGE
monomer
1 * 29460, deduced from nucleotide sequence
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DEAE, gel filtration, chromatofocusing
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upon exposure of pregnant mice to sodium arsenate in drinking water and subsequent injection of offspring on postpartum days 1-5 with diethylstilbestrol, transcripts for homocysteine cycling genes betaine-homocysteine methyltransferase and thioether S-methyltransferase and developmental marker genes alpha-fetoprotein, insulin-like growth factor 2 and IGF binding protein-1 are higher than with either treatment alone
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medicine
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exposure of the mouse to arsenic during a critical period of fetal development may potentially alter adrenal genetic programming, leading to endocrine disruption and potentially enhancing tumor formation together with diethylstilbestrol at other sites much later in life
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Mozier, N.M.; McConnel, K.P.; Hoffman, J.L.
S-Adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism
J. Biol. Chem.
263
4527-4531
1988
Mus musculus
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Warner, D.R.; Mozier, N.M.; Pearson, J.D.; Hoffman, J.L.
Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase
Biochim. Biophys. Acta
1246
160-166
1995
Mus musculus (P40936), Mus musculus
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Warner, D.R.; Hoffman, J.L.
Suicide inactivation of thioether S-methyltransferase by ethyl vinyl sulfide
Biochemistry
35
4480-4484
1996
Mus musculus
brenda
Ding, M.; Toth, L.A.
mRNA expression in mouse hypothalamus and basal forebrain during influenza infection: a novel model for sleep regulation
Physiol. Genomics
24
225-234
2006
Mus musculus
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Liu, J.; Yu, L.; Coppin, J.F.; Tokar, E.J.; Diwan, B.A.; Waalkes, M.P.
Fetal arsenic exposure appears to facilitate endocrine disruption by postnatal diethylstilbestrol in neonatal mouse adrenal
Chem. Biol. Interact.
182
253-258
2009
Mus musculus
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