7-methylxanthosine synthase

7-methylxanthosine synthase
Identifiers
EC number 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

    • Negishi O; Ozawa T & Imagawa H (1985). "The role of xanthosine in the biosynthesis of caffeine in coffee plants". Agric. Biol. Chem. 49: 2221&ndash, 2222. doi:10.1271/bbb1961.49.2221.
    • Mizuno K; Kato M; Irino F; Yoneyama N; Fujimura T; Ashihara H (2003). "The first committed step reaction of caffeine biosynthesis: 7-methylxanthosine synthase is closely homologous to caffeine synthases in coffee (Coffea arabica L.)". FEBS Lett. 547 (1–3): 56&ndash, 60. doi:10.1016/S0014-5793(03)00670-7. PMID 12860386.
    • Uefuji H; Ogita S; Yamaguchi Y; Koizumi N; Sano H (2003). "Molecular cloning and functional characterization of three distinct N-methyltransferases involved in the caffeine biosynthetic pathway in coffee plants". Plant Physiol. 132 (1): 372&ndash, 80. doi:10.1104/pp.102.019679. PMC 166982. PMID 12746542.
    • Yoneyama N; Morimoto H; Ye CX; Ashihara H; Mizuno K; Kato M (2006). "Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme". Mol. Genet. Genomics. 275 (2): 125&ndash, 35. doi:10.1007/s00438-005-0070-z. PMID 16333668.


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