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2-methoxy-4-vinylphenol + O2
vanillin + formaldehyde
about 1% of the activity with isoeugenol
-
-
?
4-vinylguaiacol + O2
vanillin + formaldehyde
32% conversion
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
additional information
?
-
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
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-
-
?
isoeugenol + O2
vanillin + acetaldehyde
the conversion is significantly increased at high substrate concentration (50 and 100 mM)
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-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
the conversion is significantly increased at high substrate concentration (50 and 100 mM)
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
-
-
-
?
isoeugenol + O2
vanillin + acetaldehyde
92% conversion
-
-
?
additional information
?
-
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
?
-
-
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
?
-
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
-
-
?
additional information
?
-
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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1,10-phenanthroline
66.54% residual activity in the presence of 5 mM 1,10-phenanthroline
8-hydroxyquinoline
1 mM, 90% loss of activity
Ag+
1 mM, 73% loss of activity
Ca2+
-
64.6% residual activity at 10 mM
EDTA
64.77% residual activity in the presence of 5 mM EDTA
ethyl acetate
in the presence 10% (v/v) ethyl acetate, the enzyme shows 19.35% residual activity with isoeugenol and 35.06% residual activity with 4-vinylguaiacol as substrate
Fe2+
70.55% residual activity in the presence of 5 mM Fe2+
Hg2+
1 mM, 87% loss of activity
K+
-
about 90 % residual activity at 10 mM
Mg2+
-
about 90 % residual activity at 10 mM
Mn2+
-
69.4% residual activity at 10 mM
n-Butyl alcohol
in the presence of 10% (v/v) n-butyl alcohol, the enzyme shows 38.19% residual activity with isoeugenol and 21.44% residual activity with 4-vinylguaiacol as substrate
n-caprylic alcohol
in the presence of 10% (v/v) n-caprylic acid, the enzyme shows 74.73% residual activity with isoeugenol as substrate
-
n-octane
in the presence of 10% (v/v) n-octane, the enzyme shows 55.34% residual activity with isoeugenol and 70.45% residual activity with 4-vinylguaiacol as substrate
p-chloromercuribenzoic acid
1 mM, 44% loss of activity
petroleum ether
in the presence of 10% (v/v) petroleum ether, the enzyme shows 46.05% residual activity with isoeugenol as substrate
-
phenylhydrazine
1 mM, 95% loss of activity
R-cycloserine
1 mM, 48% loss of activity
Toluene
in the presence of 10% (v/v) toluene, the enzyme shows 39.56% residual activity with isoeugenol and 29.36% residual activity with 4-vinylguaiacol as substrate
Triton X-100
66.54% residual activity in the presence of 5 mM Triton X-100
Vanillin
-
there is an incremental decrease in enzyme activity with the increasing vanillin concentration
Co2+
1 mM, 40% of initial activity
Co2+
-
about 80% residual activity at 10 mM
Cu2+
1 mM, 56% loss of activity
Cu2+
severe inhibition (3.17% residual activity) at 5 mM Cu2+
Fe3+
-
21.6% residual activity at 10 mM
Fe3+
62.51% residual activity in the presence of 5 mM Fe3+
Ni2+
1 mM, 49% of initial activity
Ni2+
-
about 45% residual activity at 10 mM
Ni2+
74.61% residual activity in the presence of 5 mM Ni2+
Zn2+
1 mM, 35% of initial activity
Zn2+
-
about 50% residual activity at 10 mM
Zn2+
77.07% residual activity in the presence of 5 mM Zn2+
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
-
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
-
additional information
not inhibitory: NAD+, NADH, NADP+, NADPH, FMN and FAD
-
additional information
not significantly inhibited by SDS and 2,2-bipyridine
-
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G398A
-
the mutation results in a 1.3fold increase in specific activity
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
I352R
-
the mutant with 99.7% activity shows better thermostability than the wild type enzyme (70.4% residual activity after 15 min at 35°C)
K83R
-
the mutant with 103.9% activity shows better thermostability than the wild type enzyme (84.2% residual activity after 15 min at 35°C)
K83R/I352R
-
the mutant with 99.2% activity shows better thermostability than the wild type enzyme (87.8% residual activity after 15 min at 35°C)
K83R/K95R
-
the mutant with 104.8% activity shows better thermostability than the wild type enzyme (92.1% residual activity after 15 min at 35°C)
K83R/K95R/G398A
-
the mutant with 130.1% activity shows better thermostability than the wild type enzyme (94.1% residual activity after 15 min at 35°C)
K83R/K95R/I352R
-
the mutant with 114.3% activity shows better thermostability than the wild type enzyme (90.1% residual activity after 15 min at 35°C)
K83R/K95R/L273F
-
compared with the wild type enzyme, the thermal inactivation half-lives (t1/2) of the mutant at 25°C, 30°C, and 35°C increase 2.9fold, 11.9fold, and 24.7fold, respectively. Simultaneously, it also exhibits a 4.8fold increase in kcat, leading to a 1.2fold increase in catalytic efficiency. The tolerance of the mutant to metal ions is also improved
K95R
-
the mutant with 106.6% activity shows better thermostability than the wild type enzyme (68% residual activity after 15 min at 35°C)
L273F
-
the mutant exhibits 1.17fold increase in specific activity compared to the wild type enzyme
G398A
-
the mutation results in a 1.3fold increase in specific activity
-
I352R
-
the mutant with 99.7% activity shows better thermostability than the wild type enzyme (70.4% residual activity after 15 min at 35°C)
-
K83R
-
the mutant with 103.9% activity shows better thermostability than the wild type enzyme (84.2% residual activity after 15 min at 35°C)
-
K95R
-
the mutant with 106.6% activity shows better thermostability than the wild type enzyme (68% residual activity after 15 min at 35°C)
-
L273F
-
the mutant exhibits 1.17fold increase in specific activity compared to the wild type enzyme
-
F281Q
mutant displays the highest conversion of isoeugenol
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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)
-
brenda
Zhao, L.; Jiang, Y.; Fang, H.; Zhang, H.; Cheng, S.; Rajoka, M.S.R.; Wu, Y.
Biotransformation of isoeugenol into vanillin using immobilized recombinant cells containing isoeugenol monooxygenase active aggregates
Appl. Biochem. Biotechnol.
189
448-458
2019
Pseudomonas putida
brenda
Wang, Q.; Wu, X.; Lu, X.; He, Y.; Ma, B.; Xu, Y.
Efficient biosynthesis of vanillin from isoeugenol by recombinant isoeugenol monooxygenase from Pseudomonas nitroreducens Jin1
Appl. Biochem. Biotechnol.
193
1116-1128
2021
Pseudomonas nitroreducens (C3VA26), Pseudomonas nitroreducens, Pseudomonas nitroreducens Jin1 (C3VA26)
brenda
Tang, J.; Shi, L.; Li, L.; Long, L.; Ding, S.
Expression and characterization of a 9-cis-epoxycarotenoid dioxygenase from Serratia sp. ATCC 39006 capable of biotransforming isoeugenol and 4-vinylguaiacol to vanillin
Biotechnol. Rep.
18
e00253
2018
Serratia sp. ATCC 39006 (A0A2I5TAF0)
brenda
Lu, X.; Wu, X.; Ma, B.; Xu, Y.
Enhanced thermostability of Pseudomonas nitroreducens isoeugenol monooxygenase by the combinatorial strategy of surface residue replacement and consensus mutagenesis
Catalysts
11
1199
2021
Pseudomonas nitroreducens, Pseudomonas nitroreducens Jin1
-
brenda