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Enzyme Nomenclature
Information on EC 1.13.11.88 - isoeugenol monooxygenase
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1.13.11.88 isoeugenol monooxygenaseIUBMB Comments
Contains Fe(II). The enzyme, charcterised from the bacteria Pseudomonas putida and Pseudomonas nitroreducens, catalyses the epoxidation of the double bond in the side chain of isoeugenol, followed by a second oxygenation and cleavage of the side chain in the form of acetaldehyde.
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Word Map
- 1.13.11.88
- vanillin
- nitroreducens
- putida
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bl21de3
- synthesis
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phenylpropanoids
- acetaldehyde
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undesired
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fragrance
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pet21a
- trans-anethole
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
iem
iem
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isoeugenol + O2 = vanillin + acetaldehyde
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SYSTEMATIC NAME
IUBMB Comments
isoeugenol:oxygen 7,8-oxidoreductase (bond-cleaving)
Contains Fe(II). The enzyme, charcterised from the bacteria Pseudomonas putida and Pseudomonas nitroreducens, catalyses the epoxidation of the double bond in the side chain of isoeugenol, followed by a second oxygenation and cleavage of the side chain in the form of acetaldehyde.
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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
2-methoxy-4-vinylphenol + O2
vanillin + formaldehyde
about 1% of the activity with isoeugenol
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additional information
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oxidative cleavage of isoeugenol by Iem is catalyzed via a monooxygenation reaction, and incorporation of the oxygen atom from O2 into vanillin is preferred over incorporation from water. Iem exhibits no activity toward any other of the phenylpropanoid and styrene compounds tested
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?
additional information
?
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oxidative cleavage of isoeugenol by Iem is catalyzed via a monooxygenation reaction, and incorporation of the oxygen atom from O2 into vanillin is preferred over incorporation from water. Iem exhibits no activity toward any other of the phenylpropanoid and styrene compounds tested
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additional information
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enzyme catalyzes the initial step of isoeugenol degradation, the oxidative cleavage of the side chain double-bond of isoeugenol, to form vanillin. Enzyme catalyzes the incorporation of an oxygen atom from either molecular oxygen or water into vanillin
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?
additional information
?
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no substrates: eugenol, coniferyl alcohol, coniferyl aldehyde, ferulic acid, 3,4-dihydroxycinnamic acid, 3,4-dimethoxycinnamic acid, 4-methoxycinnamic acid, 4-hydroxycinnamic acid, 3-pyridinepropionic acid, alpha-methoxycinnamic acid, styrene, trans-beta-methylstyrene, trans-stilbene, trans-stilbene oxide, acrylic acid and trans-2-hexenoic acid
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?
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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
additional information
?
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enzyme catalyzes the initial step of isoeugenol degradation, the oxidative cleavage of the side chain double-bond of isoeugenol, to form vanillin. Enzyme catalyzes the incorporation of an oxygen atom from either molecular oxygen or water into vanillin
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?
additional information
?
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no substrates: eugenol, coniferyl alcohol, coniferyl aldehyde, ferulic acid, 3,4-dihydroxycinnamic acid, 3,4-dimethoxycinnamic acid, 4-methoxycinnamic acid, 4-hydroxycinnamic acid, 3-pyridinepropionic acid, alpha-methoxycinnamic acid, styrene, trans-beta-methylstyrene, trans-stilbene, trans-stilbene oxide, acrylic acid and trans-2-hexenoic acid
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory or activating at 1 mM: Mg(II), Mn(II), Mo(II), NADH, FAD, or ascorbic acid, EDTA, 1,10-phenanthroline, and Tiron
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additional information
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not inhibitory or activating at 1 mM: Mg(II), Mn(II), Mo(II), NADH, FAD, or ascorbic acid, EDTA, 1,10-phenanthroline, and Tiron
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additional information
not inhibitory: NAD+, NADH, NADP+, NADPH, FMN and FAD
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory or activating at 1 mM: Mg(II), Mn(II), Mo(II), NADH, FAD, or ascorbic acid, EDTA, 1,10-phenanthroline, and Tiron
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additional information
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not inhibitory or activating at 1 mM: Mg(II), Mn(II), Mo(II), NADH, FAD, or ascorbic acid, EDTA, 1,10-phenanthroline, and Tiron
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.145
isoeugenol
wild-type, 30°C, pH not specified in the publication
0.15
isoeugenol
mutant F281Q, 30°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.21
isoeugenol
wild-type, 30°C, pH not specified in the publication
7.58
isoeugenol
mutant F281Q, 30°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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strain is able to produce high amounts of vanillin when grown in the presence of isoeugenol, and is also capable of growing on isoeugenol as the sole carbon source. In the presence of isoeugenol, a growing culture produces 0.61 g/l vanillin (molar yield of 12.4%), whereas cell free extracts result in 0.9 g/l vanillin (molar yield of 14%)
physiological function
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strain is able to produce high amounts of vanillin when grown in the presence of isoeugenol, and is also capable of growing on isoeugenol as the sole carbon source. In the presence of isoeugenol, a growing culture produces 0.61 g/l vanillin (molar yield of 12.4%), whereas cell free extracts result in 0.9 g/l vanillin (molar yield of 14%)
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and docking of substrate isoeugenol to the active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H167A
mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity
H205A
mutation of conserved His residue, 6.8% residual catalytic activity
H218A
mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity
H282A
mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 20mM Tris/HCl, 10% glycerol, and 1mM dithiothreitol, pH 8.0, stable for several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of Iem is dependent on the amounts of isoeugenol and the positive regulatory protein IemR. Isoeugenol is the best inducer of Iem, followed by trans-anethole, which induces Iem to 58% of the transcription level observed for isoeugenol. Overproduction of regulatory protein IemR in Escherichia coli increases the transcription of Iem up to 96fold, even in the absence of isoeugenol
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
Escherichia coli cells expressing isoeugenol monooxygenase produce 28.3 g vanillin/l from 230 mM isoeugenol, with a molar conversion yield of 81% at 20°C after 6 h. No accumulation of undesired by-products, such as vanillic acid or acetaldehyde, is observed
synthesis
the vanillin producing activity is induced by presence of isoeugenol. Under the optimized reaction conditions, Pseudomonas putida cells produce 16.1 g/l vanillin from 150 mM isoeugenol, with a molar conversion yield of 71% at 20 °C after a 24-h incubation in the presence of 10% (v/v) dimethyl sulfoxide
synthesis
upon expression of mutant F281Q in Escherichia coli and employing sol-gel chitosan membrane for removing the produced vanillin from the biotransformation system, under the optimal conditions (pH 8.5, 30°C, 180 rpm, 0.5 g wet cells, 0.1 g chitosan membrane), vanillin concentrations reach 4.5 g/l after about 40 h
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamada, M.; Okada, Y.; Yoshida, T.; Nagasawa, T.
Biotransformation of isoeugenol to vanillin by Pseudomonas putida IE27 cells
Appl. Microbiol. Biotechnol.
73
1025-1030
2007
Pseudomonas putida (A5HV13)
brenda
Yamada, M.; Okada, Y.; Yoshida, T.; Nagasawa, T.
Purification, characterization and gene cloning of isoeugenol-degrading enzyme from Pseudomonas putida IE27
Arch. Microbiol.
187
511-517
2007
Pseudomonas putida (A5HV13)
brenda
Ryu, J.Y.; Seo, J.; Unno, T.; Ahn, J.H.; Yan, T.; Sadowsky, M.J.; Hur, H.G.
Isoeugenol monooxygenase and its putative regulatory gene are located in the eugenol metabolic gene cluster in Pseudomonas nitroreducens Jin1
Arch. Microbiol.
192
201-209
2010
Pseudomonas nitroreducens (C3VA26), Pseudomonas nitroreducens
brenda
Ryu, J.Y.; Seo, J.; Ahn, J.H.; Sadowsky, M.J.; Hur, H.G.
Transcriptional control of the isoeugenol monooxygenase of Pseudomonas nitroreducens Jin1 in Escherichia coli
Biosci. Biotechnol. Biochem.
76
1891-1896
2012
Pseudomonas nitroreducens (C3VA26), Pseudomonas nitroreducens
brenda
Ryu, J.Y.; Seo, J.; Park, S.; Ahn, J.H.; Chong, Y.; Sadowsky, M.J.; Hur, H.G.
Characterization of an isoeugenol monooxygenase (Iem) from Pseudomonas nitroreducens Jin1 that transforms isoeugenol to vanillin
Biosci. Biotechnol. Biochem.
77
289-294
2013
Pseudomonas nitroreducens (C3VA26), Pseudomonas nitroreducens
brenda
Yamada, M.; Okada, Y.; Yoshida, T.; Nagasawa, T.
Vanillin production using Escherichia coli cells over-expressing isoeugenol monooxygenase of Pseudomonas putida
Biotechnol. Lett.
30
665-670
2008
Pseudomonas putida (A5HV13), Pseudomonas putida
brenda
Shimoni, E.; Ravid, U.; Shoham, Y.
Isolation of a Bacillus sp. capable of transforming isoeugenol to vanillin
J. Biotechnol.
78
1-9
2000
Bacillus subtilis, Bacillus subtilis B2
brenda
Zhao, L.; Xie, Y.; Chen, L.; Xu, X.; Zhao, C.; Cheng, F.
Efficient biotransformation of isoeugenol to vanillin in recombinant strains of Escherichia coli by using engineered isoeugenol monooxygenase and sol-gel chitosan membrane
Process Biochem.
71
76-81
2018
Pseudomonas sp. (A0A384ZRB9)
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brenda
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