1.14.13.7: phenol 2-monooxygenase (NADPH)
This is an abbreviated version!
For detailed information about phenol 2-monooxygenase (NADPH), go to the full flat file.
Word Map on EC 1.14.13.7
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1.14.13.7
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catechols
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phenol-degrading
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hydroxylases
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2,3-dioxygenase
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trichosporon
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cutaneum
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meta-cleavage
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diiron
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cresol
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comamonas
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2-hydroxymuconic
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testosteroni
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haldane
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coke
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radioresistens
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carboxylate-bridged
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meta-pathway
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ortho-cleavage
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methylococcus
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cis,cis-muconate
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coking
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environmental protection
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industry
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synthesis
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degradation
- 1.14.13.7
- catechols
-
phenol-degrading
- hydroxylases
-
2,3-dioxygenase
- trichosporon
- cutaneum
-
meta-cleavage
-
diiron
- cresol
- comamonas
-
2-hydroxymuconic
- testosteroni
-
haldane
-
coke
- radioresistens
-
carboxylate-bridged
-
meta-pathway
-
ortho-cleavage
-
methylococcus
- cis,cis-muconate
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coking
- environmental protection
- industry
- synthesis
- degradation
Reaction
Synonyms
DmpLNO, flavin containing monooxygenase, LmPH, Mph, MphN, multi-component phenol hydroxylase, multicomponent PH, multicomponent phenol hydroxylase, multicomponent phenol hydroxylase alpha subunit, NCgl2588, oxygenase, phenol 2-mono-, PHE, phenol hydroxylase, phenol o-hydroxylase, PHH, phhY, PHIND, PHO, PHR, single-component PH, SPH
ECTree
1.14.13.7 phenol 2-monooxygenase (NADPH)Advanced search results
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results (Engineering
Engineering on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C349S
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the mutant shows 30% activity compared to the wild type enzyme
C476S
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the mutant shows 45% activity compared to the wild type enzyme
D75N
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the mutant shows 288% activity compared to the wild type enzyme
P261S
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the mutant shows 15% activity compared to the wild type enzyme
R262S
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the mutant shows 427% activity compared to the wild type enzyme
R269L
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the mutant shows 232% activity compared to the wild type enzyme
D54N
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slower reaction than wild type enzyme, higher dissociation constant for binding of phenol than wild type enzyme
P364S
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only 13% of the FAD is utilized to hydroxylate the substrate phenol, when resorcinol is used as substrate, the reaction is not significantly different from the reaction of the wild type enzyme
R281M
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slower reaction than wild type enzyme, binds the FAD cofactor more weakly than wild type enzyme
additional information
additional information
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production ToMO mutants with modified regioselectivity compared with the regioselectivity of the wild-type protein in order to alter the ability of the recombinant upper pathway to produce methylcatechol isomers from toluene and to produce 3,4-dimethylcatechol from o-xylene, the combination of ToMO mutant E103G and phenol oxidase increases the production of 4-methylcatechol from toluene and the formation of 3,4-dimethylcatechol from o-xylene, overview
additional information
-
production ToMO mutants with modified regioselectivity compared with the regioselectivity of the wild-type protein in order to alter the ability of the recombinant upper pathway to produce methylcatechol isomers from toluene and to produce 3,4-dimethylcatechol from o-xylene, the combination of ToMO mutant E103G and phenol oxidase increases the production of 4-methylcatechol from toluene and the formation of 3,4-dimethylcatechol from o-xylene, overview
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