TRNA (cytosine38-C5)-methyltransferase
Appearance
TRNA (cytosine38-C5)-methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.204 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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TRNA (cytosine38-C5)-methyltransferase (EC 2.1.1.204, hDNMT2 (gene), DNMT2 (gene), TRDMT1 (gene)) is an enzyme with the systematic name S-adenosyl-L-methionine:tRNA (cytosine38-C5)-methyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction:
- S-adenosyl-L-methionine + cytosine38 in tRNA S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
The eukaryotic enzyme catalyses methylation of cytosine38 in the anti-codon loop of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC).
See also
[edit]References
[edit]- ^ Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH (January 2006). "Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2". Science. 311 (5759): 395–8. doi:10.1126/science.1120976. PMID 16424344.
- ^ Jurkowski TP, Meusburger M, Phalke S, Helm M, Nellen W, Reuter G, Jeltsch A (August 2008). "Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism". RNA. 14 (8): 1663–70. doi:10.1261/rna.970408. PMC 2491481. PMID 18567810.
- ^ Schaefer M, Pollex T, Hanna K, Tuorto F, Meusburger M, Helm M, Lyko F (August 2010). "RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage". Genes & Development. 24 (15): 1590–5. doi:10.1101/gad.586710. PMC 2912555. PMID 20679393.
External links
[edit]- TRNA+(cytosine38-C5)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)