7-methylxanthosine synthase
| 7-methylxanthosine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.158 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 7-methylxanthosine synthase (EC 2.1.1.158) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + xanthosine S-adenosyl-L-homocysteine + 7-methylxanthosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and xanthosine, whereas its two products are S-adenosylhomocysteine and 7-methylxanthosine.
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:xanthosine N7-methyltransferase. Other names in common use include xanthosine methyltransferase, XMT, xanthosine:S-adenosyl-L-methionine methyltransferase, CtCS1, CmXRS1, CaXMT1, and S-adenosyl-L-methionine:xanthosine 7-N-methyltransferase.
References
[edit]- Negishi O, Ozawa T, Imagawa H (1985). "The role of xanthosine in the biosynthesis of caffeine in coffee plants". Agric. Biol. Chem. 49 (7): 2221–2222. doi:10.1271/bbb1961.49.2221.
- Mizuno K, Kato M, Irino F, Yoneyama N, Fujimura T, Ashihara H (July 2003). "The first committed step reaction of caffeine biosynthesis: 7-methylxanthosine synthase is closely homologous to caffeine synthases in coffee (Coffea arabica L.)". FEBS Letters. 547 (1–3): 56–60. doi:10.1016/S0014-5793(03)00670-7. PMID 12860386.
- Uefuji H, Ogita S, Yamaguchi Y, Koizumi N, Sano H (May 2003). "Molecular cloning and functional characterization of three distinct N-methyltransferases involved in the caffeine biosynthetic pathway in coffee plants". Plant Physiology. 132 (1): 372–80. doi:10.1104/pp.102.019679. PMC 166982. PMID 12746542.
- Yoneyama N, Morimoto H, Ye CX, Ashihara H, Mizuno K, Kato M (February 2006). "Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme". Molecular Genetics and Genomics. 275 (2): 125–35. doi:10.1007/s00438-005-0070-z. PMID 16333668.
