Biology:tRNA guanosine-2'-O-methyltransferase
| tRNA (guanosine-2'-O-)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.34 | ||||||||
| CAS number | 37257-01-5 | ||||||||
| 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 | ||||||||
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In enzymology, a tRNA guanosine-2'-O-methyltransferase (EC 2.1.1.34) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + tRNA [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 2'-O-methylguanosine.
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 guanosine-2'-O-methyltransferase. Other names in common use include transfer ribonucleate guanosine 2'-methyltransferase, tRNA guanosine 2'-methyltransferase, tRNA (guanosine 2')-methyltransferase, tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, tRNA (guanosine-2'-O-)-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1V2X and 1ZJR.
References
- Gefter ML (1969). "The in vitro synthesis of 2'-omethylguanosine and 2-methylthio 6N (gamma,gamma, dimethylallyl) adenosine in transfer RNA of Escherichia coli". Biochem. Biophys. Res. Commun. 36 (3): 435–41. doi:10.1016/0006-291X(69)90583-X. PMID 4898378.
- "Thermally induced biosynthesis of 2'-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27". Proc. Natl. Acad. Sci. U.S.A. 77 (4): 1922–6. 1980. doi:10.1073/pnas.77.4.1922. PMID 6990416. Bibcode: 1980PNAS...77.1922K.
- "Substrate recognition of tRNA (Guanosine-2'-)-methyltransferase from Thermus thermophilus HB27". J. Biol. Chem. 273 (40): 25721–7. 1998. doi:10.1074/jbc.273.40.25721. PMID 9748240.
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