2.1.1.214: tRNA (guanine10-N2)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanine10-N2)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.214
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2.1.1.214
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methyltransferases
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nucleoside
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mtases
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anticodons
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1-methyladenosine
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s-adenosylmethionine-dependent
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methylase
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zinc-finger
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two-subunit
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archaeon
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rrna
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decoding
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zinc-binding
- 2.1.1.214
- methyltransferases
- nucleoside
- mtases
-
anticodons
- 1-methyladenosine
-
s-adenosylmethionine-dependent
-
methylase
-
zinc-finger
-
two-subunit
- archaeon
- rrna
-
decoding
-
zinc-binding
Reaction
Synonyms
(m2G10) methyltransferase, archaeal Trm11, EC 2.1.1.32, eukaryotic m2G10 tRNA methyltransferase, eukaryotic Trm11, N2, N2-dimethylguanosine tRNA methyltransferase, N2,N2-dimethylguanosine tRNA methyltransferase, Tk0981, Trm-G10, Trm-m22G10, Trm11, Trm11-Trm112 complex, Trm11p, Trmp112p, tRNA m2G10/m22G10 methyltransferase, tRNA MTase, YOL124c
ECTree
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Activating Compound
Activating Compound on EC 2.1.1.214 - tRNA (guanine10-N2)-methyltransferase
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TRM112
dependent on, Trm11 proves to be completely inactive alone. This lack of activity cannot be attributed to protein unfolding as the circular dichroism (CD) spectrum recorded on this protein is typical of well-folded proteins containing alpha-helices and beta-strands. Trm112 stimulates SAM binding to Trm11 and contributes to tRNA binding. Analysis of the activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112. Yeast Trm112 has a calculated molecular weight of 15067.6 Da. A zinc atom is attached to its Zn-binding domain. The Trm112-Trm11 interaction mode is reminiscent of the other Trm112-MTase complexes. Three-dimensional Trm11-Trm112 complex structrue analysis, and thermodynamics of interaction at 10°C, overview
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