Accepted Name |
multisite-specific tRNA:(cytosine-C(5))-methyltransferase
|
Reaction catalysed |
- cytidine(34) in tRNA precursor + S-adenosyl-L-methionine <=> 5-methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine
- cytidine(40) in tRNA precursor + S-adenosyl-L-methionine <=> 5-methylcytidine(40) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine
- cytidine(48) in tRNA + S-adenosyl-L-methionine <=> 5-methylcytidine(48) in tRNA + H(+) + S-adenosyl-L-homocysteine
- cytidine(49) in tRNA + S-adenosyl-L-methionine <=> 5-methylcytidine(49) in tRNA + H(+) + S-adenosyl-L-homocysteine
|
Comment(s) |
- The enzyme from Saccharomyces cerevisiae is responsible for complete
5-methylcytosine methylations of yeast tRNA.
- The incidence of modification depends on the cytosine position in
tRNA.
- At positions 34 and 40, 5-methylcytosine is found only in two yeast
tRNAs (tRNA(Leu)(CUA) and tRNA(Phe)(GAA), respectively), whereas most
other elongator yeast tRNAs bear either 5-methylcytosine(48) or
5-methylcytosine(49), but never both in the same tRNA molecule.
- The formation of 5-methylcytosine(34) and 5-methylcytosine(40) is a
strictly intron-dependent process, whereas the formation of
5-methylcytosine(48) and 5-methylcytosine(49) is an intron-
independent process.
- Formerly EC 2.1.1.29.
|
Cross-references |
BRENDA | 2.1.1.202 |
EC2PDB | 2.1.1.202 |
ExplorEnz | 2.1.1.202 |
PRIAM enzyme-specific profiles | 2.1.1.202 |
KEGG Ligand Database for Enzyme Nomenclature | 2.1.1.202 |
IUBMB Enzyme Nomenclature | 2.1.1.202 |
IntEnz | 2.1.1.202 |
MEDLINE | Find literature relating to 2.1.1.202 |
MetaCyc | 2.1.1.202 |
Rhea expert-curated reactions | 2.1.1.202 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-