tRNA (guanine-N1-)-methyltransferase
From Wikipedia, the free encyclopedia
In enzymology, a tRNA (guanine-N1-)-methyltransferase (EC 2.1.1.31) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + tRNA
S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N1-methylguanine.
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 (guanine-N1-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 1-methyltransferase, tRNA guanine 1-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanine-1-N-)-methyltransferase.
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[edit] Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1OY5, 1P9P, 1UAJ, 1UAK, 1UAL, and 1UAM.
[edit] References
- IUBMB entry for 2.1.1.31
- BRENDA references for 2.1.1.31 (Recommended.)
- PubMed references for 2.1.1.31
- PubMed Central references for 2.1.1.31
- Google Scholar references for 2.1.1.31
- Hurwitz J, Gold M, Anders M (1964). "The Enzymatic Methylation of Ribonucleic Acid and Deoxyribonucleic Acid. 3. Purification of Soluble Ribonucleic Acid-Methylating Enzymes". J. Biol. Chem. 239: 3462–3473. PMID 14245404.
- Bjork GR, Svensson I (1969). "Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae". Eur. J. Biochem. 9: 207–215. PMID 69267419.
- Smolar N, Hellman U, Svensson I (1975). "Two transfer RNA (1-methylguanine) methylases from yeast". Nucleic. Acids. Res. 2: 993–1004. PMID 1096087.
- Glick JM, Averyhart VM, Leboy PS (1978). "Purification and characterization of two tRNA-(guanine)-methyltransferases from rat liver". Biochim. Biophys. Acta. 518: 158–171. PMID 629973.
[edit] External links
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- The CAS registry number for this enzyme class is 37256-99-8.

