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1.14.13.243: toluene 2-monooxygenase

This is an abbreviated version!
For detailed information about toluene 2-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.243

Reaction

2-methylphenol
+
NADH
 +
H+
 +
O2
=
3-methylcatechol
 +
NAD+
 +
H2O

Synonyms

toluene ortho-monooxygenase, tomA1/2/3/4/5

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.243 toluene 2-monooxygenase

Engineering

Engineering on EC 1.14.13.243 - toluene 2-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A106E
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in hydroxylase alpha-subunit TomA3, variant degrades its natural substrate toluene 63% faster than wild-type, with 50% 2-methylphenol, 25% 3-methylphenol, and 25% 4-methylphenol being formed. Whole cells expressing the A106E variant have two times better naphthalene-to-1-naphthol activity than the wild-type, and the regiospecificity of the A106E variant is unchanged, with 98% 1-naphthol formed
A113H
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
A113I
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole
A113V
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole
V106A
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3, colony turns green. Mutant degrades trichloroethylene, 1,1-dichloroethylene, and trans-dichloroethylene more rapidly than wild-type. Whole cells expressing the mutant synthesize 1-naphthol six times faster than wild-type enzyme
V106A/A113G
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
V106M
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation of the alpha-hydroxylase subunit TomA3, improves both rate and enantioselectivity. 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 the mutant
A106E
-
mutation in hydroxylase alpha-subunit TomA3, variant degrades its natural substrate toluene 63% faster than wild-type, with 50% 2-methylphenol, 25% 3-methylphenol, and 25% 4-methylphenol being formed. Whole cells expressing the A106E variant have two times better naphthalene-to-1-naphthol activity than the wild-type, and the regiospecificity of the A106E variant is unchanged, with 98% 1-naphthol formed
-
A113H
-
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
-
A113I
-
mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole
-
A113V
-
mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole
-
V106A
-
mutation in subunit TomA3, colony turns green. Mutant degrades trichloroethylene, 1,1-dichloroethylene, and trans-dichloroethylene more rapidly than wild-type. Whole cells expressing the mutant synthesize 1-naphthol six times faster than wild-type enzyme
-
V106A/A113G
-
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
-
V106M
-
mutation of the alpha-hydroxylase subunit TomA3, improves both rate and enantioselectivity. 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 the mutant
-