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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Substrates Products
Substrates Products on EC 2.1.1.217 - tRNA (adenine22-N1)-methyltransferase
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REACTION DIAGRAM
S-adenosyl-L-methionine + adenine22 in Bacillus subtilis tRNA(Ser)
S-adenosyl-L-homocysteine + N1-methyladenine22 in Bacillus subtilis tRNA(Ser)
crude Escherichia coli tRNA is used, since it does not contain m1A22
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
a methyl group at position N1 prevents Watson-Crick-type base pairing by adenosine and is therefore important for regulation of structure and stability of tRNA molecules
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?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
crude Escherichia coli tRNA is used, since it does not contain m1A22
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-
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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-
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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-
-
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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-
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-
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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-
-
?
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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?
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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?
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
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S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
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S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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additional information
?
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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-
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additional information
?
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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