7-methylxanthosine synthase

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
7-methylxanthosine synthase
Identifiers
EC number2.1.1.158
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 (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.


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