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Information on EC 2.1.1.283 - emodin O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.283
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.283 emodin O-methyltransferase
IUBMB Comments
The enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
emodin o-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-EOMT
CGZ69_28180
emodin-1-OH-O-methyltransferase
EOMT
GedA
O-methyltransferase
OMT
SpOMT7740
additional information
additional information
see also 2.1.1.88, cf. EC 2.1.1.42
additional information
see also 2.1.1.88, cf. EC 2.1.1.42
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + emodin = S-adenosyl-L-homocysteine + questin
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
geodin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:emodin 8-O-methyltransferase
The enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + aloe emodin
S-adenosyl-L-homocysteine + 8-methoxy-1-hydroxy-3-(hydroxymethyl)anthracene-9,10-dione
S-adenosyl-L-methionine + beta-sitosterol
S-adenosyl-L-homocysteine + 3-methoxy-beta-sitosterol
Substrates: low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + O-methoxy-genistein
Substrates: when genistein is used as substrate, mass spectras of three O-methoxy genistein (mono-, di-, and tri-O-methoxy genistein) are detected, low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + mono-methoxy-luteolin
Substrates: lower activity
Products: -
Products: -
?
S-adenosyl-L-methionine + phloretin
S-adenosyl-L-homocysteine + mono-methoxy-phloretin
Substrates: lower activity
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + 1,3,8-trihydroxy-6-methoxy-9,10-anthraquinone
?
-
Substrates: i.e. citreorosein, 22% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + 1,3,8-trihydroxy-6-methoxy-9,10-anthraquinone
?
-
Substrates: i.e. citreorosein, 22% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-hydroxyflavone
S-adenosyl-L-homocysteine + 3-methoxyflavone
Substrates: lower activity
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-hydroxyflavone
S-adenosyl-L-homocysteine + 3-methoxyflavone
Substrates: lower activity
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + 7-hydroxy-8-methoxyflavone
Substrates: best substrate
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + 7-hydroxy-8-methoxyflavone
Substrates: best substrate
Products: -
Products: -
?
S-adenosyl-L-methionine + 7-chloroemodin
?
-
Substrates: 18% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + 7-chloroemodin
?
-
Substrates: 18% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + aloe emodin
S-adenosyl-L-homocysteine + 8-methoxy-1-hydroxy-3-(hydroxymethyl)anthracene-9,10-dione
Substrates: low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + aloe emodin
S-adenosyl-L-homocysteine + 8-methoxy-1-hydroxy-3-(hydroxymethyl)anthracene-9,10-dione
Substrates: low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + catenarin
?
-
Substrates: 80% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + catenarin
?
-
Substrates: 80% of the activity compared to emodin
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: the enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Aspergillus terreus HXN301
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: the enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: low activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: the enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Aspergillus terreus HXN301
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
-
Substrates: the enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin
Products: -
Products: -
?
S-adenosyl-L-methionine + emodin
S-adenosyl-L-homocysteine + questin
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Mg2+ or Mn2+ is not an absolute requirement, nor increases the enzyme activity
additional information
no or poor effect by Ca2+, Ni2+, Fe2+, Fe3+, and EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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pI VALUE
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
Highest Expressing Human Cell Lines
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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
-
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
-
metabolism
methyltransferases are involved in post-modification during biosynthesis of secondary metabolites performing terminal modification
metabolism
-
methyltransferases are involved in post-modification during biosynthesis of secondary metabolites performing terminal modification
-
additional information
O-methyltransferases (OMTs) are commonly regiospecific
additional information
-
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). GEDA_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
486
0
53916
Swiss-Prot
-
A0A1B1W6Z7_STRC0
342
0
36858
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y173A/R343A
Y173A/R343A
the mutant produces questin plus 1-O-methylemodin from emodin
Y173A/R343A
-
the mutant produces questin plus 1-O-methylemodin from emodin
-
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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
agriculture
synthesis
agriculture
the enzyme may be used for the production of physcion or other site-specific O-methylated anthraquinone derivatives with potential applications as biopesticides
agriculture
-
the enzyme may be used for the production of physcion or other site-specific O-methylated anthraquinone derivatives with potential applications as biopesticides
-
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
-
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
Chen, Z.G.; Fujii, I.; Ebizuka, Y.; Sankawa, U.
Emodin O-methyltransferase from Aspergillus terreus
Arch. Microbiol.
158
29-34
1992
Aspergillus terreus, Aspergillus terreus IMI 16043
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)
brenda
Xue, Y.; Liang, Y.; Zhang, W.; Geng, C.; Feng, D.; Huang, X.; Dong, S.; Zhang, Y.; Sun, J.; Qi, F.; Lu, X.
Characterization and structural analysis of emodin-O-methyltransferase from Aspergillus terreus
J. Agric. Food Chem.
70
5728-5737
2022
Aspergillus terreus (Q0CCY5), Aspergillus terreus NIH2624 (Q0CCY5)
brenda
Qi, F.; Zhang, W.; Xue, Y.; Geng, C.; Jin, Z.; Li, J.; Guo, Q.; Huang, X.; Lu, X.
Microbial production of the plant-derived fungicide physcion
Metab. Eng.
74
130-138
2022
Aspergillus terreus, Aspergillus terreus HXN301
brenda
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