2.1.1.34: tRNA (guanosine18-2'-O)-methyltransferase
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For detailed information about tRNA (guanosine18-2'-O)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.34
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2.1.1.34
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thermophilus
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thermus
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d-loops
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ribose
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methyltransferases
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trnaphe
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adomet
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2'-o-methyltransferases
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2'-o-methylguanosine
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analysis
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s-adenosyl-l-homocysteine
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medicine
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methyl-transfer
- 2.1.1.34
- thermophilus
-
thermus
-
d-loops
- ribose
- methyltransferases
- trnaphe
- adomet
-
2'-o-methyltransferases
- 2'-o-methylguanosine
- analysis
- s-adenosyl-l-homocysteine
- medicine
-
methyl-transfer
Reaction
Synonyms
methyltransferase, transfer ribonucleate guanosine 2'-, S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase, SpoU, TARBP1, transfer ribonucleate guanosine 2'-methyltransferase, transfer RNA (Gm18) methyltransferase, TrmH, tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, tRNA (guanosine-2'-O-)-methyltransferase, tRNA Gm18 methyltransferase, tRNA guanosine 2'-methyltransferase
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Application on EC 2.1.1.34 - tRNA (guanosine18-2'-O)-methyltransferase
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analysis
medicine
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Arg-41 is the catalytic center, Lys-90, Arg-166, Arg-168, and Arg-176 are the initial sites of tRNA binding, Arg-8, Arg-19, and Lys-32 are required in the tRNA binding site for continuation the catalytic cycle, Arg-11-His-71-Met-147 interaction is involved in the structural element in release of S-adenosyl-L-homocysteine, His-34 plays a role in the assisted phosphate binding site, Arg-109 has an unknown function
analysis
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dissociation of tRNA from the tRNA-enzyme complex after the methyl-transfer reaction is caused by the dissociation of enzyme subunits
analysis
reveals a fold typical of members of the SpoU clan of proteins, a subfamily of the alpha/beta-knot superfamily, with alpha-helical extensions at the N- and C-termini that are likely to be involved in tRNA binding
analysis
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through the log phase, the content of the TrmH protein is not changed obviously, but in the stationary phase, the content of the TrmH protein is slowly reduced
analysis
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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dissociation of tRNA from the tRNA-enzyme complex after the methyl-transfer reaction is caused by the dissociation of enzyme subunits
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analysis
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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through the log phase, the content of the TrmH protein is not changed obviously, but in the stationary phase, the content of the TrmH protein is slowly reduced
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an RNA preparation of an Escherichia coli trmH mutant that lacks Gm18 2'-O-methyltransferase activity is significantly more immunostimulatory in human peripheral blood mononuclear cells than the wild-type sample. The single methyl group on the 2'-oxygen of Gm18 is a natural modification in native tRNA that, beyond its primary structural role, has acquired a secondary function as an antagonist of toll-like receptor TLR7
medicine
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bacterial tRNA induces type I interferon and inflammatory cytokines in mouse dendritic cells and human peripheral blood mononuclear cells. tRNA from an Escherichia coli knockout strain for tRNA (Gm18)-2'-O-methyltransferase regained immunostimulatory potential. In vitro methylation of this immunostimulatory Gm18-negative tRNA with recombinant trmH from Thermus thermophilus abolishes its interferon-alpha-inducing potential. Gm18-modified tRNA acts as toll-like receptor TLR7 antagonist and blocks IFN-alpha induction of influenza A virus-infected peripheral blood mononuclear cells
medicine
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in vitro methylation of immunostimulatory Gm18-negative tRNA with recombinant trmH from Thermus thermophilus abolishes its interferon-alpha-inducing potential