2.1.1.220: tRNA (adenine58-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (adenine58-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.220
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2.1.1.220
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trnaimet
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1-methyladenosine
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nucleoside
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mtases
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two-subunit
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thermus
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exosome
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polyadenylation
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adomet
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t-loop
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polya
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s-adenosylmethionine
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n1-methylation
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heterotetramer
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homotetrameric
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methionyl-trna
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high-copy-number
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eubacteria
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methyltransferases
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s-adenosyl-l-homocysteine
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two-component
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s-adenosyl-l-methionine-dependent
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l-shaped
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tpsic
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trna-binding
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hypomodified
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drug development
- 2.1.1.220
- trnaimet
- 1-methyladenosine
- nucleoside
- mtases
-
two-subunit
-
thermus
-
exosome
-
polyadenylation
- adomet
-
t-loop
- polya
- s-adenosylmethionine
-
n1-methylation
- heterotetramer
-
homotetrameric
- methionyl-trna
-
high-copy-number
- eubacteria
- methyltransferases
- s-adenosyl-l-homocysteine
-
two-component
-
s-adenosyl-l-methionine-dependent
-
l-shaped
-
tpsic
-
trna-binding
-
hypomodified
- drug development
Reaction
Synonyms
EC 2.1.1.36, Gcd10p, Gcd10p-Gcd14p, Gcd10pyGcd14p complex, Gcd14p, m1A58 MTase, m1A58 tRNA methyl-transferase, m1A58 tRNA methyltransferase, m1A58-methyltransferase, m1A58MTase, Rv2118c, Rv2118p, Trm6, TRM6-TRM61 holoenzyme, Trm61A, Trm61B, TRm61p, TRm6p, TrmI, tRNA (m1A58) methyltransferase, tRNA (m1A58) MTase, tRNA m(1)A58 methyltransferase, tRNA m1A58 methyltransferase, two component m1A58 tRNA methyl-transferase
ECTree
Advanced search results
Engineering
Engineering on EC 2.1.1.220 - tRNA (adenine58-N1)-methyltransferase
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D170A
site-directed mutagenesis, mutation of a conserved active site residue
Y194A
site-directed mutagenesis, crystallization assays of TrmI Y194A lead to poorly diffracting crystals
Y78A
site-directed mutagenesis, mutation of a conserved active site residue. The structure of TrmI Y78A catalytic domain is unmodified regarding the binding of the SAM co-factor and the conformation of residues potentially interacting with the substrate adenine, as compared to the wild-type structure. The structure of the D170A mutant shows a flexible active site with one loop occupying in part the place of the co-factor and the second loop moving at the entrance to the active site
D170A
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site-directed mutagenesis, mutation of a conserved active site residue
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Y194A
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site-directed mutagenesis, crystallization assays of TrmI Y194A lead to poorly diffracting crystals
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Y78A
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site-directed mutagenesis, mutation of a conserved active site residue. The structure of TrmI Y78A catalytic domain is unmodified regarding the binding of the SAM co-factor and the conformation of residues potentially interacting with the substrate adenine, as compared to the wild-type structure. The structure of the D170A mutant shows a flexible active site with one loop occupying in part the place of the co-factor and the second loop moving at the entrance to the active site
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additional information
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siRNA knockdown of m1A58 methyltransferase subunits TRM6 or TRM61
additional information
P46959; P41814
mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
additional information
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mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
additional information
P46959; P41814
the reduced m1A levels observed in vivo and the lack of Mtase activity seen in vitro result from the inability of trm6-416, trm6-420, trm6-504, trm61-255 and trm6-416/trm61-255 mutants to effectively bind their tRNA substrate
additional information
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the reduced m1A levels observed in vivo and the lack of Mtase activity seen in vitro result from the inability of trm6-416, trm6-420, trm6-504, trm61-255 and trm6-416/trm61-255 mutants to effectively bind their tRNA substrate
additional information
P41814; P46959
the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27
additional information
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the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27
additional information
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the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27
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