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EC Tree
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
Synonyms
bergaptol o-methyltransferase,
more
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bergaptol O-methyltransferase
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bergaptol-5-O-methyltransferase
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EC 2.1.1.92
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formerly
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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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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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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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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 + a 5-hydroxyfurocoumarin
S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
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-
?
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
the enzyme has rigid substrate affinity to bergaptol
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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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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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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
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additional information
?
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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
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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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?
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S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin
S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin
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S-adenosyl-L-methionine + bergaptol
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S-adenosyl-L-methionine + bergaptol
S-adenosyl-L-homocysteine + bergapten
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
the enzyme has rigid substrate affinity to 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
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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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5.6
calculated from amino acid sequence and estimated by SDS-PAGE
5.9
calculated from amino acid sequence
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Swissprot
brenda
Bai Zhi
UniProt
brenda
Michx.
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brenda
Michx.
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brenda
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brenda
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UniProt
brenda
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brenda
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tapetum and pollen
brenda
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brenda
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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
brenda
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epidermis, subepidermal cells and oil duct epithelial cells
brenda
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very young leaf buds
brenda
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oil duct epithelial cells, ovule and funiculus
brenda
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young shoots of field-grown plants
brenda
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brenda
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from leaf petiols, cells activated by an elicitor from Phytophtora megasperma, no activity in untreated cells
brenda
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uninfected cells from cotyledons
brenda
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brenda
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brenda
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in young leaf the enzyme is active exclusively in the epithelial cells of oil ducts
brenda
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vascular bundle, oil duct epithelial cells and pallisade parenchyma of young and old leaves
brenda
lowest expression
brenda
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sterile leaf cell culture
brenda
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brenda
high expression
brenda
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vascular bundle, oil duct epithelial cells and collenchymatic parenchyma
brenda
low expression
brenda
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brenda
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activated by UV-light or fungal elicitor
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brenda
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BMT_AMMMJ
354
0
38727
Swiss-Prot
other Location (Reliability: 2 )
COMTS_PEUPR
364
0
39979
Swiss-Prot
other Location (Reliability: 2 )
BMT_GLELI
359
0
39384
Swiss-Prot
other Location (Reliability: 4 )
BMT_PEUPR
359
0
39269
Swiss-Prot
other Location (Reliability: 4 )
J9PHM5_9APIA
359
0
39248
TrEMBL
other Location (Reliability: 3 )
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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
?
x * 38700, calculated
?
x * 39000, calculated from amino acid sequence and estimated from SDS-PAGE
?
x * 39000, calculated from amino acid sequence
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in complex with S-adenosyl-L-homocysteine and bergaptol
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D226A
the mutant is almost inactive
F171A
the mutant is almost inactive
G203A
the mutant shows about 75% of wild type activity
H264A
the mutant is almost inactive
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
L312A
the mutant is almost inactive
M175A
the mutant is almost inactive
M316A
the mutant shows about 70% of wild type activity
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
Y319A
the mutant shows about 60% of wild type activity
Y319F
the mutant shows about 5fold increased activity compared to the wild type enzyme
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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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ammonium sulfate precipitation and Ni-NTA column chromatography
glutathione S-transferase-conjugated affinity resin column chromatography
partially purified by ammonium sulfate precipitation
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expressed in Escherichia coli BL21(DE3) cells
His-tagged enzyme is expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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the enzyme expression can be induced by methyl jasmonate
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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, Ruta graveolens, Heracleum maximum Michx.
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
-
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)
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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
Peucedanum praeruptorum (A0A166U5H3), Peucedanum praeruptorum
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
Peucedanum praeruptorum (A0A166U5H3), Peucedanum praeruptorum
brenda
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