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Information on EC 2.1.1.69 - 5-hydroxyfuranocoumarin 5-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.69
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.69 5-hydroxyfuranocoumarin 5-O-methyltransferase
IUBMB Comments
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 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase)
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
bergaptol o-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bergaptol O-methyltransferase
BMT
EC 2.1.1.92
-
-
formerly
-
furanocoumarin 5-methyltransferase
-
-
-
-
furanocoumarin 5-O-methyltransferase
-
-
-
-
methyltransferase, bergaptol
-
-
-
-
BMT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin = S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
converts bergaptol into bergapten. Methylates the 5-hydroxyl of some hydroxy- and methyl- coumarins, but has little activity on non-coumarin phenols
-
-
-
S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + bergapten
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
linear furanocoumarin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5-hydroxyfurocoumarin 5-O-methyltransferase
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)
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CAS REGISTRY NUMBER
COMMENTARY
101637-31-4
-
67339-12-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 5,7-dihydroxycoumarin
S-adenosyl-L-homocysteine + citropten
-
Substrates: 6% of the activity with bergaptol
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,8-dihydroxypsoralen
S-adenosyl-L-homocysteine + ?
-
Substrates: 2.6% of the activity with bergaptol
Products: -
Products: -
?
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin
S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
Substrates: best substrate
Products: -
Products: -
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: late enzyme of the furanocoumarin pathway
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: final methylation in the biosynthesis of the furanocoumarin bergapten
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
Substrates: the enzyme has rigid substrate affinity to bergaptol
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: furanocoumarinbiosynthesis
Products: -
Products: -
?
additional information
?
-
Substrates: less than 1% activity, compared to bergaptol, with substrates caffeate, 5-hydroxyferulate, caffeic acid methyl ester, caffeoyl coenzyme A, 3-(3,4-dihydroxyphenyl)propionate, esculetin, daphnetin
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 1% activity, compared to bergaptol, with substrates caffeate, 5-hydroxyferulate, caffeic acid methyl ester, caffeoyl coenzyme A, 3-(3,4-dihydroxyphenyl)propionate, esculetin, daphnetin
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has no activity with xanthotol, (E)-2'-hydroxychalcone, (E)-3'-hydroxychalcone, caffeic acid, 4-hydroxycoumarin, 7-hydroxycoumarin,4,7-dihydroxycoumarin, 5,7-dihydroxyflavone, ferulic acid, and resveratrol
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity against phenol, resorcinol, phloroglucinol, 3-hydroxy-4-methoxybenzaldehyde, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2-hydroxyphenylacetic acid, 3-hydroxycinnamic acid, and quercetin-7,4'-dimethyl ether lower than 10% of the activity observed with bergaptol as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity against xanthoxol
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin
S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: late enzyme of the furanocoumarin pathway
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: final methylation in the biosynthesis of the furanocoumarin bergapten
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
?
-
Substrates: part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
Substrates: the enzyme has rigid substrate affinity to bergaptol
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
Substrates: furanocoumarinbiosynthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme does not require a divalent cation for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Fe2+ and Zn2+ only slightly affect enzyme activity at 0.1 mM. The addition of Mn2+, Fe3+, and Ca2+ barely affects enzyme catalytic activity. The enzyme is not inhibited by EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0031
S-adenosyl-L-methionine
-
reaction with bergaptol or 5-hydroxyxanthotoxin
10.68
S-adenosyl-L-methionine
recombinant enzyme, at pH 7.5, at 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
6.5 - 9.3
-
pH 6.5: about 30% of maximal activity, pH 9.3: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
calculated from amino acid sequence and estimated by SDS-PAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity decreases from high activity in young cotyledons, where it is assumed to participate in flavonoid biosynthesis, to low activity at late stages of cotyledon development
brenda
-
epidermis, subepidermal cells and oil duct epithelial cells
brenda
-
from leaf petiols, cells activated by an elicitor from Phytophtora megasperma, no activity in untreated cells
brenda
-
in young leaf the enzyme is active exclusively in the epithelial cells of oil ducts
brenda
-
vascular bundle, oil duct epithelial cells and pallisade parenchyma of young and old leaves
brenda
-
vascular bundle, oil duct epithelial cells and collenchymatic parenchyma
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BMT_GLELI
359
0
39384
Swiss-Prot
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I157F/V320I
the mutant shows about 4fold increased activity compared to the wild type enzyme
I157H
the mutant shows strongly reduced activity compared to the wild type enzyme
I157Y
the mutant shows about 2.4fold increased activity compared to the wild type enzyme
I157Y/S265F/V315N
the mutant shows severely reduced activity compared to the wild type enzyme
I157Y/S265N
the mutant shows about 1.5fold increased activity compared to the wild type enzyme
L122F
the mutant shows reduced activity compared to the wild type enzyme
L122H
the mutant shows severely reduced activity compared to the wild type enzyme
L122H/W261H
the mutant shows reduced severely activity compared to the wild type enzyme
L122H/W261H/H126F
the mutant shows severely reduced activity compared to the wild type enzyme
L122H/W261H/H126W
the mutant shows severely reduced activity compared to the wild type enzyme
S265I
the mutant shows about 2.5fold increased activity compared to the wild type enzyme
S265N
the mutant shows about 1.9fold increased activity compared to the wild type enzyme
V315F
the mutant shows severely reduced activity compared to the wild type enzyme
V320I
high-catalytic activity mutant with about 8.5fold increased activity compared to the wild type enzyme
V320Y
the mutant shows reduced activity compared to the wild type enzyme
W261H
the mutant shows about 1.9fold increased activity compared to the wild type enzyme
W261L
the mutant shows slightly reduced activity compared to the wild type enzyme
Y319F
the mutant shows about 5fold increased activity compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored and refrozen, activity against bergaptol is essentially unchanged after 18 days and is still 65% of the initial value after 34 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Ni-NTA column chromatography
glutathione S-transferase-conjugated affinity resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharma, S.K.; Garrett, J.M.; Brown, S.A.
Separation of the S-adenosylmethionine: 5-and 8-hydroxyfuranocoumarin O-methyltransferases of Ruta graveolens L. by general ligand affinity chromatography
Z. Naturforsch. C
34
387-391
1979
Ruta graveolens
-
brenda
Thompson, H.J.; Sharma, S.K.; Brown, S.A.
O-Methyltransferases of furanocoumarin biosynthesis
Arch. Biochem. Biophys.
188
272-281
1978
Heracleum maximum, Heracleum maximum Michx., Ruta graveolens
brenda
Sharma, S.K.; Brown, S.A.
Affinity chromatography of Ruta graveolens L. O-methyltransferases. Studies demonstrating the potential of the technique in the mechanistic investigation of O-methyltransferases
Can. J. Biochem.
57
986-995
1979
Ruta graveolens
brenda
Hauffe, K.D.; Hahlbrock, K.; Scheel, D.
Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley cells: S-adenosyl-L-methionine:bergaptol and S-adenosyl-L-methionine:xanthotoxol O-methyltransferase
Z. Naturforsch. C
41
228-239
1986
Petroselinum crispum
-
brenda
Dangl, J.L.; Hauffe, K.D.; Lipphardt, S.; Hahlbrock, K.; Scheel, D.
Parsley protoplasts retain differential responsiveness to u.v. light and fungal elicitor
EMBO J.
6
2551-2556
1987
Petroselinum crispum
brenda
Knogge, W.; Kombrink, E.; Schmelzer, E.; Hahlbrock, K.
Occurence of phytoalexins and other putative defense-related substances in uninfected parsley plants
Planta
171
279-287
1987
Petroselinum crispum
brenda
Wu, S.C.; Hahlbrock, K.
In situ localization of phenylpropanoid-related gene expression in different tissues of light- and dark-grown parsley seedlings
Z. Naturforsch. C
47
591-600
1992
Petroselinum crispum
-
brenda
Jahnen, W.; Hahlbrock, K.
Differential regulation and tissue specific distribution of enzymes of phenylpropanoid pathways in developing parsley seedlings
Planta
173
453-458
1988
Petroselinum crispum
brenda
Reinold, S.; Hahlbrock, K.
In situ localization of phenylpropanoid biosynthetic mRNAs and proteins in parsley (Petroselinum crispum)
Bot. Acta
110
431-443
1997
Petroselinum crispum
-
brenda
Hehmann, M.; Lukacin, R.; Ekiert, H.; Matern, U.
Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol O-methyltransferase
Eur. J. Biochem.
271
932-940
2004
Ammi majus (Q6T1F6), Ammi majus
brenda
Lo, S.; Chung, P.; Wang, C.
Molecular cloning and functional analysis of bergaptol-O-methyltransferase from Angelica dahurica (Bai Zhi) and using it to efficiently produce bergapten in E. coli
Bot. Stud.
53
197-206
2012
Angelica dahurica (J9PHM5)
-
brenda
Zhao, Y.; Wang, N.; Zeng, Z.; Xu, S.; Huang, C.; Wang, W.; Liu, T.; Luo, J.; Kong, L.
Cloning, functional characterization, and catalytic mechanism of a bergaptol O-methyltransferase from Peucedanum praeruptorum Dunn
Front. Plant Sci.
7
722
2016
Kitagawia praeruptora (A0A166U5H3)
brenda
Zhao, Y.; Wang, N.; Wu, H.; Zhou, Y.; Huang, C.; Luo, J.; Zeng, Z.; Kong, L.
Structure-based tailoring of the first coumarins-specific bergaptol O-methyltransferase to synthesize bergapten for depigmentation disorder treatment
J. Adv. Res.
21
57-64
2020
Kitagawia praeruptora (A0A166U5H3)
brenda
Chen, C.; Wang, Y.; Xu, L.; Wang, S.; Chen, X.; Shen, Y.
Characterization of abscisic acid and ethylene in regulating the white blush in fresh-cut carrots
Int. J. Mol. Sci.
23
12788
2022
Daucus carota
brenda
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