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Enzyme Nomenclature
Information on EC 2.1.1.69 - 5-hydroxyfuranocoumarin 5-O-methyltransferase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.69
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RECOMMENDED NAME
GeneOntology No.
5-hydroxyfuranocoumarin 5-O-methyltransferase
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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
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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
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67339-12-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
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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 + caffeic acid
S-adenosyl-L-homocysteine + ?
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-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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-
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S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
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-
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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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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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-
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-
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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-
-
-
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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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-
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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?
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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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INHIBITORS
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
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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
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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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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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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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.69)
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