2.1.1.200: tRNA (cytidine32/uridine32-2'-O)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (cytidine32/uridine32-2'-O)-methyltransferase, go to the full flat file.
Reaction
Synonyms
2'-O-tRNA methyltransferase, PA14 14690, Saci_0621, TrMet(Xm32), TrmJ, tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase, tRNA:Cm32/Um32 methyltransferase, tRNA:Cm32/Um32/Am32 methyltransferase, YfhQ
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 2.1.1.200 - tRNA (cytidine32/uridine32-2'-O)-methyltransferase
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REACTION DIAGRAM
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
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S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
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S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
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S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
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S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
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S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
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bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
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additional information
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bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
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