KEGG   ENZYME: 2.1.1.69Help
Entry
EC 2.1.1.69                 Enzyme                                 

Name
5-hydroxyfuranocoumarin 5-O-methyltransferase;
furanocoumarin 5-methyltransferase;
furanocoumarin 5-O-methyltransferase;
bergaptol 5-O-methyltransferase;
bergaptol O-methyltransferase;
bergaptol methyltransferase;
S-adenosyl-L-methionine:bergaptol O-methyltransferase;
BMT;
S-adenosyl-L-methionine:5-hydroxyfuranocoumarin 5-O-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:5-hydroxyfurocoumarin 5-O-methyltransferase
Reaction(IUBMB)
(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:R02882]
Reaction(KEGG)
R02882;
(other) R08538
Show
Substrate
S-adenosyl-L-methionine [CPD:C00019];
5-hydroxyfurocoumarin;
bergaptol [CPD:C00758]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
5-methoxyfurocoumarin;
bergapten [CPD:C01557]
Comment
Converts bergaptol into bergapten, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities [4]. The enzyme methylates the 5-hydroxy group of some hydroxy- and methylcoumarins, such as 5-hydroxyxanthotoxin [3], but has little activity on non-coumarin phenols [1]. Caffeate, 5-hydroxyferulate and daphnetin are not substrates [4]. Cu2+, Zn2+ and Co2+ cause enzyme inhibition [4]. (see also EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase)
History
EC 2.1.1.69 created 1984 (EC 2.1.1.92 created 1989, incorporated 2006), modified 2006
Reference
1  [PMID:28084]
  Authors
Thompson HJ, Sharma SK, Brown SA.
  Title
O-methyltransferases of furanocoumarin biosynthesis.
  Journal
Arch. Biochem. Biophys. 188 (1978) 272-81.
  Organism
Ruta graveolens, Heracleum lanatum
Reference
2  [PMID:156999]
  Authors
Sharma SK, Garrett JM, Brown SA.
  Title
Separation of the S-adenosylmethionine: 5- and 8-hydroxyfuranocoumarin O-methyltransferases of Ruta graveolens L. by general ligand affinity chromatography.
  Journal
Z. Naturforsch. [C]. 34C (1979) 387-91.
  Organism
Ruta graveolens
Reference
3
  Authors
Hauffe, K.D., Hahlbrock, K. and Scheel, D.
  Title
Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley cells - S-adenosyl-L-methionine-bergaptol and S-adenosyl-L-methionine-xanthotoxol O-methyltransferases.
  Journal
Z. Naturforsch. C: Biosci. 41 (1986) 228-239.
Reference
4  [PMID:15009205]
  Authors
Hehmann M, Lukacin R, Ekiert H, Matern U.
  Title
Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol O-methyltransferase.
  Journal
Eur. J. Biochem. 271 (2004) 932-40.
  Organism
Ammi majus
  Sequence
[up:Q6T1F6]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
67339-12-2 101637-31-4

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