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Information on EC 2.1.1.88 - 8-hydroxyquercetin 8-O-methyltransferase
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EC Tree
2.1.1.88 8-hydroxyquercetin 8-O-methyltransferaseIUBMB Comments
Also acts on 8-hydroxykaempferol, but not on the glycosides of 8-hydroxyflavonols. An enzyme from the flower buds of Lotus corniculatus.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
spomt7740, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CGZ69_28180
flavonol 8-O-methyltransferase
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methyltransferase, flavonol 8-
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O-methyltransferase
OMT
SpOMT7740
additional information
additional information
see also 2.1.1.283, cf. EC 2.1.1.42
additional information
see also 2.1.1.283, cf. EC 2.1.1.42
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone = S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone = S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
mechanism
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S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone = S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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,
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3,5,7,8,3',4'-hexahydroxyflavone 8-O-methyltransferase
Also acts on 8-hydroxykaempferol, but not on the glycosides of 8-hydroxyflavonols. An enzyme from the flower buds of Lotus corniculatus.
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CAS REGISTRY NUMBER
COMMENTARY
99775-17-4
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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 + 3,3',4',5,7,8-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxyflavone
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + 7-hydroxy-8-methoxyflavone
S-adenosyl-L-methionine + 8-hydroxykaempferol
S-adenosyl-L-homocysteine + 8-methoxykaempferol
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-
?
S-adenosyl-L-methionine + aloe emodin
S-adenosyl-L-homocysteine + 8-methoxy-1-hydroxy-3-(hydroxymethyl)anthracene-9,10-dione
low activity
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-
?
S-adenosyl-L-methionine + beta-sitosterol
S-adenosyl-L-homocysteine + 3-methoxy-beta-sitosterol
low activity
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-
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + O-methoxy-genistein
when genistein is used as substrate, mass spectras of three O-methoxy genistein (mono-, di-, and tri-O-methoxy genistein) are detected, low activity
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-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + mono-methoxy-luteolin
lower activity
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?
S-adenosyl-L-methionine + phloretin
S-adenosyl-L-homocysteine + mono-methoxy-phloretin
lower activity
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-
?
S-adenosyl-L-methionine + 3,3',4',5,7,8-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxyflavone
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-
-
?
S-adenosyl-L-methionine + 3,3',4',5,7,8-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxyflavone
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i.e. 8-hydroxyquercetin
i.e. 8-methoxyquercetin
?
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
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-
-
?
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
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-
-
?
S-adenosyl-L-methionine + 3-hydroxyflavone
S-adenosyl-L-homocysteine + 3-methoxyflavone
lower activity
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?
S-adenosyl-L-methionine + 3-hydroxyflavone
S-adenosyl-L-homocysteine + 3-methoxyflavone
lower activity
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?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + 7-hydroxy-8-methoxyflavone
best substrate
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?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + 7-hydroxy-8-methoxyflavone
best substrate
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?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
low activity
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?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
low activity
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?
additional information
?
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the enzyme shows a broad substrate specificity. SpOMT7740 catalyzes the O-methylation reaction to form various natural and non-natural O-methoxides, includes 7-hydroxy-8-O-methoxy flavone, 3-O-methoxy flavone, three mono-, di-, and tri-O-methoxy genistein, mono-O-methoxy phloretin, mono-O-methoxy luteolin, 3-O-methoxy beta-sitosterol, and O-methoxy anthraquinones (emodin and aloe emodin) and O-methoxy anthracycline (daunorubicin) exhibiting diverse substrate flexibility. Mass spectrometric analysis of reaction products. 7,8-Dihydroxyflavone is the best substrate for bioconversion to 7-hydroxy-8-O-methoxy flavone. The enzyme seems to prefer methylation of hydroxy groups at C8 position. No or poor activity with doxorubicin and daunorubicin
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additional information
?
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the enzyme shows a broad substrate specificity. SpOMT7740 catalyzes the O-methylation reaction to form various natural and non-natural O-methoxides, includes 7-hydroxy-8-O-methoxy flavone, 3-O-methoxy flavone, three mono-, di-, and tri-O-methoxy genistein, mono-O-methoxy phloretin, mono-O-methoxy luteolin, 3-O-methoxy beta-sitosterol, and O-methoxy anthraquinones (emodin and aloe emodin) and O-methoxy anthracycline (daunorubicin) exhibiting diverse substrate flexibility. Mass spectrometric analysis of reaction products. 7,8-Dihydroxyflavone is the best substrate for bioconversion to 7-hydroxy-8-O-methoxy flavone. The enzyme seems to prefer methylation of hydroxy groups at C8 position. No or poor activity with doxorubicin and daunorubicin
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additional information
?
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the enzyme shows a broad substrate specificity. SpOMT7740 catalyzes the O-methylation reaction to form various natural and non-natural O-methoxides, includes 7-hydroxy-8-O-methoxy flavone, 3-O-methoxy flavone, three mono-, di-, and tri-O-methoxy genistein, mono-O-methoxy phloretin, mono-O-methoxy luteolin, 3-O-methoxy beta-sitosterol, and O-methoxy anthraquinones (emodin and aloe emodin) and O-methoxy anthracycline (daunorubicin) exhibiting diverse substrate flexibility. Mass spectrometric analysis of reaction products. 7,8-Dihydroxyflavone is the best substrate for bioconversion to 7-hydroxy-8-O-methoxy flavone. The enzyme seems to prefer methylation of hydroxy groups at C8 position. No or poor activity with doxorubicin and daunorubicin
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NATURAL SUBSTRATE
NATURAL 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 + 3,3',4',5,7,8-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxyflavone
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?
S-adenosyl-L-methionine + 8-hydroxykaempferol
S-adenosyl-L-homocysteine + 8-methoxykaempferol
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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
Mg2+
additional information
no or poor effect by Ca2+, Ni2+, Fe2+, Fe3+, and EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-Methoxykaempferol
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product inhibition, competitive with respect to 8-hydroxykaempferol
S-adenosyl-L-homocysteine
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product inhibition, non-competitive with respect to S-adenosyl-L-methionine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
O-methyltransferases (OMTs) are categorized into three classes, where class 1 and class 2 are involved in the methylation of phenolic hydroxyl residues and class 3 is involved in the methylation of carboxyl groups to yield methyl esters
evolution
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O-methyltransferases (OMTs) are categorized into three classes, where class 1 and class 2 are involved in the methylation of phenolic hydroxyl residues and class 3 is involved in the methylation of carboxyl groups to yield methyl esters
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metabolism
methyltransferases are involved in post-modification during biosynthesis of secondary metabolites performing terminal modification
metabolism
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methyltransferases are involved in post-modification during biosynthesis of secondary metabolites performing terminal modification
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additional information
O-methyltransferases (OMTs) are commonly regiospecific
additional information
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O-methyltransferases (OMTs) are commonly regiospecific
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8OMT_MENPI
366
0
40849
Swiss-Prot
other Location (Reliability: 3)
A0A2G9I929_9LAMI
360
0
40069
TrEMBL
other Location (Reliability: 5)
A0A1B1W6Z7_STRC0
342
0
36858
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SpOMT7740, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL-1 Blue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
O-methyltransferases (OMTs) from microorganism sources have broad scope to methylate diverse classes of plant natural products to synthesize methyl derivatives. Enzyme SpOMT2884 from Streptomyces peucetius cloned into Escherichia coli shows the possibility of generating diverse O-methyl flavonoids 7,8-dihydroxyflavone (7,8-DHF), luteolin, quercetin, rutin, naringenin, daidzein, and formononetin
synthesis
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O-methyltransferases (OMTs) from microorganism sources have broad scope to methylate diverse classes of plant natural products to synthesize methyl derivatives. Enzyme SpOMT2884 from Streptomyces peucetius cloned into Escherichia coli shows the possibility of generating diverse O-methyl flavonoids 7,8-dihydroxyflavone (7,8-DHF), luteolin, quercetin, rutin, naringenin, daidzein, and formononetin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jay, M.; De Luca, V.; Ibrahim, R.K.
Purification, properties and kinetic mechanism of flavonol 8-O-methyltransferase from Lotus corniculatus L
Eur. J. Biochem.
153
321-325
1985
Lotus corniculatus
brenda
Willits, M.G.; Giovanni, M.; Prata, R.T.N.; Kramer, C.M.; De Luca, V.; Steffens, J.C.; Graser, G.
Bio-fermentation of modified flavonoids: an example of in vivo diversification of secondary metabolites
Phytochemistry
65
31-41
2004
Mentha x piperita (Q6VMW0)
brenda
Parajuli, P.; Pandey, R.P.; Nguyen, T.H.T.; Dhakal, D.; Sohng, J.K.
Substrate scope of O-methyltransferase from Streptomyces peucetius for biosynthesis of diverse natural products methoxides
Appl. Biochem. Biotechnol.
184
1404-1420
2018
Streptomyces peucetius subsp. caesius (A0A1B1W6Z7), Streptomyces peucetius subsp. caesius ATCC 27952 (A0A1B1W6Z7), Streptomyces peucetius subsp. caesius ATCC 27952
brenda
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Release 2023.1 (January 2023)
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