2.1.1.217: tRNA (adenine22-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (adenine22-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.217
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2.1.1.217
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mtases
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methyltransferases
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adomet
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rna-binding
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groove
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sam-dependent
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class-i
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ligand-free
- 2.1.1.217
- mtases
- methyltransferases
- adomet
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rna-binding
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groove
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sam-dependent
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class-i
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ligand-free
Reaction
Synonyms
BsTrmK, Class I MTase, EC 2.1.1.36, m1A22 MTase, m1A22 tRNA methyltransferase, Sp1610, TrmK, tRNA: m1A22 methyltransferase, yqfN
ECTree
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Subunits
Subunits on EC 2.1.1.217 - tRNA (adenine22-N1)-methyltransferase
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monomer
additional information
BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
monomer
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BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
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monomer
Sp1610 exists as a monomer both in solution and in the P212121 crystal
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
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backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
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BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
-
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
-
additional information
-
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
-