Transferring one-carbon groups;
(1) S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin = S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin (general reaction);
(2) S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + bergapten [RN:
Converts bergaptol into bergapten, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities . The enzyme methylates the 5-hydroxy group of some hydroxy- and methylcoumarins, such as 5-hydroxyxanthotoxin , but has little activity on non-coumarin phenols . Caffeate, 5-hydroxyferulate and daphnetin are not substrates . Cu2+, Zn2+ and Co2+ cause enzyme inhibition . (see also EC
, 8-hydroxyfuranocoumarin 8-O-methyltransferase)
EC 184.108.40.206 created 1984 (EC 220.127.116.11 created 1989, incorporated 2006), modified 2006
ec00999 Biosynthesis of various plant secondary metabolites
ec01110 Biosynthesis of secondary metabolites
K21550 5-hydroxyfuranocoumarin 5-O-methyltransferase
Thompson HJ, Sharma SK, Brown SA.
O-methyltransferases of furanocoumarin biosynthesis.
Sharma SK, Garrett JM, Brown SA.
Separation of the S-adenosylmethionine: 5- and 8-hydroxyfuranocoumarin O-methyltransferases of Ruta graveolens L. by general ligand affinity chromatography.
Hauffe, K.D., Hahlbrock, K. and Scheel, D.
Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley cells - S-adenosyl-L-methionine-bergaptol and S-adenosyl-L-methionine-xanthotoxol O-methyltransferases.
Z Naturforsch C: Biosci 41:228-239 (1986)
Hehmann M, Lukacin R, Ekiert H, Matern U
Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol O-methyltransferase.
ExplorEnz - The Enzyme Database: 18.104.22.168
ExPASy - ENZYME nomenclature database: 22.214.171.124
CAS: 67339-12-2 101637-31-4
LinkDB All DBs