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
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.69
-
RECOMMENDED NAME
GeneOntology No.
5-hydroxyfuranocoumarin 5-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin = S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
linear furanocoumarin biosynthesis
-
-
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)
CAS REGISTRY NUMBER
COMMENTARY hide
101637-31-4
-
67339-12-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
Bai Zhi
UniProt
Manually annotated by BRENDA team
Michx.
-
-
Manually annotated by BRENDA team
Michx.
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 5,7-dihydroxycoumarin
S-adenosyl-L-homocysteine + citropten
show the reaction diagram
-
6% of the activity with bergaptol
-
?
S-adenosyl-L-methionine + 5,8-dihydroxypsoralen
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
2.6% of the activity with bergaptol
-
-
?
S-adenosyl-L-methionine + 5-hydroxyxanthotoxin
S-adenosyl-L-homocysteine + isopimpinellin
show the reaction diagram
S-adenosyl-L-methionine + bergaptol
?
show the reaction diagram
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
show the reaction diagram
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + bergaptol
?
show the reaction diagram
S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
show the reaction diagram
-
furanocoumarinbiosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme does not require a divalent cation for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
kinetin
-
strong inhibition
Mg2+
-
slightly inhibits the O-methylation of bergaptol
p-chloromercuribenzoic acid
-
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
5-hydroxyxanthotoxin
-
-
0.0028 - 0.56
bergaptol
0.0031 - 10.68
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000029
-
bergaptol
0.000056
-
5-hydroxyxanthotoxin
0.000375
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8
-
-
7.5
in potassium phosphate buffer
8.5 - 9
-
5-hydroxyanthotoxin as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
6.5 - 9.3
-
pH 6.5: about 30% of maximal activity, pH 9.3: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
tapetum and pollen
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
epidermis, subepidermal cells and oil duct epithelial cells
Manually annotated by BRENDA team
-
very young leaf buds
Manually annotated by BRENDA team
-
oil duct epithelial cells, ovule and funiculus
Manually annotated by BRENDA team
-
young shoots of field-grown plants
Manually annotated by BRENDA team
-
vascular bundle, oil duct epithelial cells and collenchymatic parenchyma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
activated by UV-light or fungal elicitor
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
-
gel filtration
110000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 36000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
below: inactivation within 30 min
485668
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification and storage
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20 C, stable for 20 days in 50% v/v glycerol
-
-20C, stored and refrozen, activity against bergaptol is essentially unchanged after 18 days and is still 65% of the initial value after 34 days
-
0C, stored below undesalted, 40% loss of activity after 5 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified by ammonium sulfate precipitation
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from dark-grown plants
His-tagged enzyme is expressed in Escherichia coli