HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
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.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.1.1.69
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
5-hydroxyfuranocoumarin 5-O-methyltransferase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
101637-31-4
-
67339-12-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
6% of the activity with bergaptol
-
?
S-adenosyl-L-methionine + 5,8-dihydroxypsoralen
S-adenosyl-L-homocysteine + ?
-
2.6% of the activity with bergaptol
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
-
-
-
-
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
-
-
-
-
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
best substrate
-
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
-
-
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
late enzyme of the furanocoumarin pathway
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
final methylation in the biosynthesis of the furanocoumarin bergapten
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
-
-
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
-
-
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
-
-
-
?
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
-
furanocoumarinbiosynthesis
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
furanocoumarinbiosynthesis
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
late enzyme of the furanocoumarin pathway
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
final methylation in the biosynthesis of the furanocoumarin bergapten
-
-
?
S-adenosyl-L-methionine + bergaptol
?
-
part of plant/pathogen interaction, enzyme of the furanocoumarin pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme does not require a divalent cation for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
vascular bundle, oil duct epithelial cells and collenchymatic parenchyma
-
from leaf petiols, cells activated by an elicitor from Phytophtora megasperma, no activity in untreated cells
-
in young leaf the enzyme is active exclusively in the epithelial cells of oil ducts
-
vascular bundle, oil duct epithelial cells and pallisade parenchyma of young and old leaves
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.69)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
