Literature summary for 2.1.1.158 extracted from

Qian, P.; Guo, H.B.; Yue, Y.; Wang, L.; Yang, X.; Guo, H.
Understanding the catalytic mechanism of xanthosine methyltransferase in caffeine biosynthesis from QM/MM molecular dynamics and free energy simulations (2016), J. Chem. Inf. Model., 56, 1755-1761 .

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Organism

Organism	UniProt	Comment	Textmining
Coffea canephora	A4GE69	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	both xanthosine and its monoanionic form with N3 deprotonated are used as the substrates for the methylation. While the methyl group can be transferred to the monoanionic form of xanthosine with a reasonable free energy barrier (about 17 kcal/mol), this is not the case for the neutral xanthosine (barrier is about 31 kcal/mol). The hydrogen bonding and hydrophobic interactions involving the monoanionic form closely represent the corresponding interactions in the crystal structure, which seems not to be the case for the reactant complex involving the neutral xanthosine	Coffea canephora	?	-	-
S-adenosyl-L-methionine + xanthosine	-	Coffea canephora	S-adenosyl-L-homocysteine + 7-methylxanthosine	-	?

Synonyms

Synonyms	Comment	Organism
XMT1	-	Coffea canephora

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Release 2023.1 (January 2023)