EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  2.1.1.200 | more |
no methylation of cytosine 34 in tRNALeu(CAA) |
Escherichia coli |
? |
- |
? |
| 2.1.1.200 | more |
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 |
Escherichia coli |
? |
- |
? |
| 2.1.1.200 | more |
PA14 TrmJ catalyzes 2'-O-methylation of C, U and A at position 32 in the tRNA anticodon loop. tRNA substrates for reaction with PA14 TrmJ are prepared by in vitro T7 transcription. Substrate specificity, overview. No or poor activity with tRNASer(UGA) and tRNAHis(GUG). Structure analysis of TrmJ-NTD tRNA binding |
Pseudomonas aeruginosa |
? |
- |
- |
| 2.1.1.200 | more |
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 |
Escherichia coli K-12 MG1655 |
? |
- |
? |
| 2.1.1.200 | more |
PA14 TrmJ catalyzes 2'-O-methylation of C, U and A at position 32 in the tRNA anticodon loop. tRNA substrates for reaction with PA14 TrmJ are prepared by in vitro T7 transcription. Substrate specificity, overview. No or poor activity with tRNASer(UGA) and tRNAHis(GUG). Structure analysis of TrmJ-NTD tRNA binding |
Pseudomonas aeruginosa UCBPP-PA14 |
? |
- |
- |
| 2.1.1.200 | S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG) |
tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates |
Pseudomonas aeruginosa |
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG) |
- |
? |
| 2.1.1.200 | S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG) |
tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates |
Pseudomonas aeruginosa UCBPP-PA14 |
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG) |
- |
? |
| 2.1.1.200 | S-adenosyl-L-methionine + cytidine32 in tRNA |
- |
Pseudomonas aeruginosa |
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA |
- |
? |
| 2.1.1.200 | S-adenosyl-L-methionine + cytidine32 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 |
Escherichia coli |
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA |
- |
? |
| 2.1.1.200 | S-adenosyl-L-methionine + cytidine32 in tRNA |
2'-O-methylation of cytidine34 in tRNAGln2(CUG). Total crude tRNA extracted from the wild-type strain MC1061 was not a substrate for the purified YfhQ enzyme, while tRNA from the yfhQ K.O. strain is an excellent substrate for this enzyme |
Escherichia coli |
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA |
- |
? |
