tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
| tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.61 | ||||||||
| CAS no. | 39391-17-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (EC 2.1.1.61) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 5-methylaminomethyl-2-thiouridylic acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thio-uridylate)-methyltransferase. Other names in common use include transfer ribonucleate 5-methylaminomethyl-2-thiouridylate, 5-methyltransferase, and tRNA 5-methylaminomethyl-2-thiouridylate 5'-methyltransferase.
Structural studies
[edit]As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2DER, 2DET, 2DEU, and 2HMA.
References
[edit]- Taya Y, Nishimura S (1973). "Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate". Biochem. Biophys. Res. Commun. 51 (4): 1062–8. doi:10.1016/0006-291X(73)90035-1. PMID 4703553.
- Taya Y, Nishimura S (1977). Salvatore, F., Borek, E., Zappia, V., Williams-Ashman, H.G., Schlenk, F. (eds.). "The Biochemistry of Adenosylmethionine". New York: Columbia University Press: 251.
{{cite journal}}: Cite journal requires|journal=(help)
