1.14.13.236: toluene 4-monooxygenase
This is an abbreviated version!
For detailed information about toluene 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.236
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1.14.13.236
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hydroxylase
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diiron
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mendocina
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p-cresol
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regiospecificity
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ferredoxins
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cepacia
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rieske
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synthesis
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pickettii
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ortho-monooxygenase
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m-nitrophenol
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nitrobenzene
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2-naphthol
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3-monooxygenase
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rieske-type
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four-protein
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diferric
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o-xylene
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norcarane
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xanthobacter
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analysis
- 1.14.13.236
- hydroxylase
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diiron
- mendocina
- p-cresol
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regiospecificity
- ferredoxins
- cepacia
-
rieske
- synthesis
- pickettii
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ortho-monooxygenase
- m-nitrophenol
- nitrobenzene
- 2-naphthol
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3-monooxygenase
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rieske-type
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four-protein
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diferric
- o-xylene
- norcarane
- xanthobacter
- analysis
Reaction
Synonyms
T4moD, T4moF, T4MOH, TMO, TmoA, TmoC, TmoF, toluene-4-monooxygenase system protein A, TOM, TomA3
ECTree
1.14.13.236 toluene 4-monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.13.236 - toluene 4-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
V106M
mutant oxidizes methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increases from 51% for the wild type to 88% for this mutant. Function of residue V106 is the proper positioning or docking of the substrate with respect to the diiron atoms
V106M
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mutant oxidizes methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increases from 51% for the wild type to 88% for this mutant. Function of residue V106 is the proper positioning or docking of the substrate with respect to the diiron atoms
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D285A
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 2.7fold increase in activity with 2-phenylethanol
D285C
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 4fold increase in activity with 2-phenylethanol
D285I
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 6.6fold increase in activity with 2-phenylethanol
D285L
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 5.4fold increase in activity with 2-phenylethanol
D285P
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 3.3fold increase in activity with 2-phenylethanol
D285Q
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 10.5fold increase in activity with 2-phenylethanol
D285S
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 70% of wild-type activity
D285Y mutation in subunit TmoA,
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
3fold increase in activity with 2-phenylethanol
F205I
decrease in regiospecificity for p-cresol formation, about 5-fold increase in the percentage of m-cresol formation. Mutant gives nearly equivalent amounts of benzylic and phenolic products from p-xylene oxidation
G103A/A107S
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, produces 3-methylcatechol (98%) from o-cresol twofold faster and produces 3-methoxycatechol (82%) from 1mM o-methoxyphenol seven times faster than the wild-type
G103S
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, produces 40fold more methoxyhydroquinone from o-methoxyphenol than the wild-type
G103S/A107T
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, produces methylhydroquinone (92%) from o-cresol fourfold faster than wild-type
I100A
I100A/D285I
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 52fold increase in activity with 2-phenylethanol
I100A/D285Q
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 85fold increase in activity with 2-phenylethanol
I100D
I100G
I100G/D285I
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 14.1fold increase in activity with methyl p-tolyl sulfide
I100L
I100L/D285S
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 1.4fold increase in activity with styrene
I100S
I100V
Q141C
decrease in regiospecificity for p-cresol formation, mutant functions predominantly as an aromatic ring hydroxylase during the oxidation of p-xylene
S395C
mutation in subunit TmoA, shows a 15fold increase in 2-phenylethanol hydroxylation rate
T201A
T201F
mutation causes a substantial shift in the product distribution, and gives o- and p-cresol in a 1:1 ratio
T201G
T201S
D285A
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mutation in subunit TmoA, 2.7fold increase in activity with 2-phenylethanol
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D285P
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mutation in subunit TmoA, 3.3fold increase in activity with 2-phenylethanol
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F205I
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decrease in regiospecificity for p-cresol formation, about 5-fold increase in the percentage of m-cresol formation. Mutant gives nearly equivalent amounts of benzylic and phenolic products from p-xylene oxidation
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G103A/A107S
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mutation in subunit TmoA, produces 3-methylcatechol (98%) from o-cresol twofold faster and produces 3-methoxycatechol (82%) from 1mM o-methoxyphenol seven times faster than the wild-type
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G103S
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mutation in subunit TmoA, produces 40fold more methoxyhydroquinone from o-methoxyphenol than the wild-type
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G103S/A107T
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mutation in subunit TmoA, produces methylhydroquinone (92%) from o-cresol fourfold faster than wild-type
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I100A
I100G
I100L
I100S
I100V
Q141C
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decrease in regiospecificity for p-cresol formation, mutant functions predominantly as an aromatic ring hydroxylase during the oxidation of p-xylene
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S395C
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mutation in subunit TmoA, shows a 15fold increase in 2-phenylethanol hydroxylation rate
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T201A
T201F
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mutation causes a substantial shift in the product distribution, and gives o- and p-cresol in a 1:1 ratio
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T201G
T201S
additional information
I100A
mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
I100A
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 35fold increase in activity with 2-phenylethanol
I100D
mutant hydroxylates m-tyrosol to form hydroxytyrosol
I100D
mutation improves both reaction rate and enantioselectivity
I100G
mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
I100G
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 11fold increase in activity with methyl p-tolyl sulfide
I100G
mutation increases the wild-type oxidation rate of methyl phenyl sulfide by 1.7fold, and the enantiomeric excess rises from 86% to 98% pro-S. I100G oxidizes methyl para-tolyl sulfide 11 times faster than the wild type does and changes the selectivity from 41% pro-R to 77% pro-S
I100L
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, 0.9fold decrease in activity with styrene
I100L
Q6Q8Q7; Q6Q8Q6; Q6Q8Q5; Q6Q8Q4; Q6Q8Q3; Q6Q8Q2
mutation in subunit TmoA, produces 3-methoxycatechol from o-methoxyphenol four times faster than wild-type
I100S
mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
I100S
mutation improves both reaction rate and enantioselectivity
I100V
mutant hydroxylates m-tyrosol to form hydroxytyrosol
I100V
mutation improves both reaction rate and enantioselectivity
T201A
mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
T201A
mutation has no impact on steady-state catalysis or coupling. Mutant T201A gives stoichometric release of H2O2 during reaction in the absence of substrate and has a faster first-order rate constant for product formation than wild-type
T201G
mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
T201G
mutation has no impact on steady-state catalysis or coupling
T201S
mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
T201S
mutation has no impact on steady-state catalysis or coupling
I100A
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mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
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I100A
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mutation in subunit TmoA, 35fold increase in activity with 2-phenylethanol
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I100G
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mutation increases the wild-type oxidation rate of methyl phenyl sulfide by 1.7fold, and the enantiomeric excess rises from 86% to 98% pro-S. I100G oxidizes methyl para-tolyl sulfide 11 times faster than the wild type does and changes the selectivity from 41% pro-R to 77% pro-S
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I100G
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mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
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I100G
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mutation in subunit TmoA, 11fold increase in activity with methyl p-tolyl sulfide
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I100L
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mutation in subunit TmoA, produces 3-methoxycatechol from o-methoxyphenol four times faster than wild-type
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I100L
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mutation in subunit TmoA, 0.9fold decrease in activity with styrene
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I100S
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mutant hydroxylates o-tyrosol, m-tyrosol and p-tyrosol to form hydroxytyrosol
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T201A
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mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
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T201A
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mutation has no impact on steady-state catalysis or coupling. Mutant T201A gives stoichometric release of H2O2 during reaction in the absence of substrate and has a faster first-order rate constant for product formation than wild-type
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T201G
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mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
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T201S
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mutant retains catalytic activity and exhibits 80-90% coupling efficiency compared to 94% for wild-type, with p-cresol representing 90-95% of the total product distribution
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additional information
construction of variants with either four (DELTAN4-) seven (DELTAN7-), or 10 (DELTAN10-) residues removed from the N-terminal. Removal leads to statistically insignificant changes in kcat, KM, kcat/KM, and KI relative to the native protein. There is no significant change in the regiospecificity of toluene oxidation with any of the T4moD variants
additional information
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identification of three more toluene monooxygenase-encoding operons. Data suggest the important role of plasmids in the spread of toluene degradative capacity
