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Information on EC 2.1.1.69 - 5-hydroxyfuranocoumarin 5-O-methyltransferase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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5-hydroxyfuranocoumarin 5-O-methyltransferase
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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
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S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + bergapten
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methyl group transfer
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linear furanocoumarin biosynthesis
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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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bergaptol-5-O-methyltransferase
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furanocoumarin 5-methyltransferase
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furanocoumarin 5-O-methyltransferase
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methyltransferase, bergaptol
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BMT
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Swissprot
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Bai Zhi
UniProt
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Michx.
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Michx.
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brenda
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brenda
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brenda
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S-adenosyl-L-methionine + 5,7-dihydroxycoumarin
S-adenosyl-L-homocysteine + citropten
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6% of the activity with bergaptol
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?
S-adenosyl-L-methionine + 5,8-dihydroxypsoralen
S-adenosyl-L-homocysteine + ?
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2.6% of the activity with bergaptol
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?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
S-adenosyl-L-methionine + bergaptol
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
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additional information
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S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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best substrate
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?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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?
S-adenosyl-L-methionine + bergaptol
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S-adenosyl-L-methionine + bergaptol
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late enzyme of the furanocoumarin pathway
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S-adenosyl-L-methionine + bergaptol
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final methylation in the biosynthesis of the furanocoumarin bergapten
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?
S-adenosyl-L-methionine + bergaptol
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part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
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?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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furanocoumarinbiosynthesis
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additional information
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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
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additional information
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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
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additional information
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no activity against xanthoxol
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S-adenosyl-L-methionine + bergaptol
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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furanocoumarinbiosynthesis
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S-adenosyl-L-methionine + bergaptol
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late enzyme of the furanocoumarin pathway
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S-adenosyl-L-methionine + bergaptol
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final methylation in the biosynthesis of the furanocoumarin bergapten
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S-adenosyl-L-methionine + bergaptol
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part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
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S-adenosyl-L-methionine
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additional information
the enzyme does not require a divalent cation for activity
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kinetin
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strong inhibition
Mg2+
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slightly inhibits the O-methylation of bergaptol
p-chloromercuribenzoic acid
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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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Co2+
1.5 mM, 21% inhibition
Co2+
severe inhibition at 1.5 mM
Cu2+
1.5 mM, 100% inhibition
Cu2+
severe inhibition at 0.1 mM, complete inhibition at 1.5 mM
Ni2+
1.5 mM, 47% inhibition
Ni2+
severe inhibition at 0.1 mM, complete inhibition at 1.5 mM
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0.001
5-hydroxyxanthotoxin
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0.0031 - 10.68
S-adenosyl-L-methionine
0.0028
bergaptol
42°C, pH 8.0
0.56
bergaptol
recombinant enzyme, at pH 7.5, at 35°C
0.0031
S-adenosyl-L-methionine
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reaction with bergaptol or 5-hydroxyxanthotoxin
0.0065
S-adenosyl-L-methionine
42°C, pH 8.0
10.68
S-adenosyl-L-methionine
recombinant enzyme, at pH 7.5, at 35°C
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0.000056
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5-hydroxyxanthotoxin
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7.5
in potassium phosphate buffer
8.5 - 9
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5-hydroxyanthotoxin as substrate
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6.5 - 9.3
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pH 6.5: about 30% of maximal activity, pH 9.3: about 45% of maximal activity
6.5 - 9
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5.9
calculated from amino acid sequence
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tapetum and pollen
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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
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epidermis, subepidermal cells and oil duct epithelial cells
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very young leaf buds
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oil duct epithelial cells, ovule and funiculus
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young shoots of field-grown plants
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vascular bundle, oil duct epithelial cells and collenchymatic parenchyma
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from leaf petiols, cells activated by an elicitor from Phytophtora megasperma, no activity in untreated cells
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uninfected cells from cotyledons
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in young leaf the enzyme is active exclusively in the epithelial cells of oil ducts
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vascular bundle, oil duct epithelial cells and pallisade parenchyma of young and old leaves
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sterile leaf cell culture
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activated by UV-light or fungal elicitor
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brenda
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36000
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2 * 36000, SDS-PAGE
38700
x * 38700, calculated
39000
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
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dimer
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2 * 36000, SDS-PAGE
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x * 38700, calculated
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x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
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5
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below: inactivation within 30 min
485668
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2-mercaptoethanol stabilizes during purification and storage
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-20 C, stable for 20 days in 50% v/v glycerol
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-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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0°C, stored below undesalted, 40% loss of activity after 5 weeks
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partially purified by ammonium sulfate precipitation
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His-tagged enzyme is expressed in Escherichia coli
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BMT_AMMMJ
354
38727
Swiss-Prot
BMT_GLELI
359
39384
Swiss-Prot
A0A166U5H3_9APIA
359
39269
TrEMBL
J9PHM5_9APIA
359
39248
TrEMBL
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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
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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
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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
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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
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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)
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)
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brenda
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