1.14.14.20: phenol 2-monooxygenase (FADH2)
This is an abbreviated version!
For detailed information about phenol 2-monooxygenase (FADH2), go to the full flat file.
Word Map on EC 1.14.14.20
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1.14.14.20
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two-component
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rhodococcus
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thermoglucosidasius
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catechols
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erythropolis
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isoalloxazine
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prosthetic
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nadh-dependent
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reductases
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fmnh2
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hydroxylases
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ping-pong
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homotetramer
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hydride
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environmental protection
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4-hydroxyphenylacetate
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fad-containing
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synthesis
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styrene
- 1.14.14.20
-
two-component
- rhodococcus
- thermoglucosidasius
- catechols
- erythropolis
- isoalloxazine
-
prosthetic
-
nadh-dependent
- reductases
- fmnh2
- hydroxylases
-
ping-pong
-
homotetramer
-
hydride
- environmental protection
- 4-hydroxyphenylacetate
-
fad-containing
- synthesis
- styrene
Reaction
Synonyms
FAD reductase, flavin reductase PheA2, PheA, PheA1, PheA2, phenol hydroxylase
ECTree
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Substrates Products
Substrates Products on EC 1.14.14.20 - phenol 2-monooxygenase (FADH2)
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REACTION DIAGRAM
4-methylphenol + FADH2 + O2
4-methylcatechol + FAD + H2O
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-
-
?
catechol + riboflavin + H2O
phenol + reduced riboflavin + O2
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-
-
r
2,4-dichlorocatechol + FAD + H2O
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-
-
?
2,4-dichlorophenol + FADH2 + O2
2,4-dichlorocatechol + FAD + H2O
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-
-
?
2-chlorocatechol + FAD + H2O
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-
-
?
2-chlorophenol + FADH2 + O2
2-chlorocatechol + FAD + H2O
poor substrate for isozyme PheA1(1)
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-
?
2-chlorophenol + FADH2 + O2
2-chlorocatechol + FAD + H2O
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-
-
?
2-chlorophenol + FADH2 + O2
2-chlorocatechol + FAD + H2O
poor substrate for isozyme PheA1(1)
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-
?
? + NAD(P)+ + H2O
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-
-
?
3-nitrophenol + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
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-
-
?
4-chlorocatechol + FAD + H2O
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-
-
?
4-chlorophenol + FADH2 + O2
4-chlorocatechol + FAD + H2O
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-
-
?
? + NAD(P)+ + H2O
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-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
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-
-
?
catechol + FAD + H2O
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-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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a two-component enzyme system: the smaller flavin reductase PheA2 component catalyzes the NADH-dependent reduction of free FAD according to a ping pong bisubstrate-biproduct mechanism. The reduced FAD is then used by the larger oxygenase component PheA1 to hydroxylate phenols to the corresponding catechols
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
PheA1 is required for activity, no activity by PheA2 alone. PheA2 acts according to a ping pong bi bi reaction mechanism in which NADH reduces the FAD cofactor, which in turn transfers electrons to the FAD substrate
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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reactive exogenous FAD substrate binds in the NADH cleft after release of NAD product. PheA2 is able to bind one FAD cofactor and one FAD substrate
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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a two-component enzyme system: the smaller flavin reductase PheA2 component catalyzes the NADH-dependent reduction of free FAD according to a ping pong bisubstrate-biproduct mechanism. The reduced FAD is then used by the larger oxygenase component PheA1 to hydroxylate phenols to the corresponding catechols
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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reactive exogenous FAD substrate binds in the NADH cleft after release of NAD product. PheA2 is able to bind one FAD cofactor and one FAD substrate
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
-
-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
PheA1 is required for activity, no activity by PheA2 alone. PheA2 acts according to a ping pong bi bi reaction mechanism in which NADH reduces the FAD cofactor, which in turn transfers electrons to the FAD substrate
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
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-
-
?
phenol + FADH2 + O2
catechol + FAD + H2O
hydroxylation of phenol in vitro requires the presence of both PheA1 and PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction, Km for FAD is 0.0134 mM, Km for NADH is 0.0533 mM. The hydroxylation of phenol in vitro depends on the molar ratio of His6PheA2 and His6PheA1 present in the reaction mixture, an increase of the amount of His6PheA1 in the assay results in a higher phenol hydroxylase activity. In the assay, a reductase/oxygenase molar ratio of 1:10 is used
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-
?
phenol + FADH2 + O2
catechol + FAD + H2O
hydroxylation of phenol in vitro requires the presence of both PheA1 and PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction. The hydroxylation of phenol in vitro depends on the molar ratio of His6PheA2 and His6PheA1 present in the reaction mixture, an increase of the amount of His6PheA1 in the assay results in a higher phenol hydroxylase activity. In the assay, a reductase/oxygenase molar ratio of 1:10 is used
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-
?
catechol + FMN + H2O
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-
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?
phenol + FMNH2 + O2
catechol + FMN + H2O
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-
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
hydroxylation of phenol in vitro requires the presence of both His6PheA1 and His6PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction
-
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
hydroxylation of phenol in vitro requires the presence of both His6PheA1 and His6PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction
-
-
?
catechol + NAD+ + H2O
the two-protein system phenol hydroxylase consists of an oxygenase (PheA1) and a flavin reductase (PheA2). PheA1 catalyzes the efficient ortho-hydroxylation of phenol to catechol when supplemented with PheA2 and FAD/NADH. PheA1 catalyzes the NADH-dependent reduction of free flavins according to a ping pong bi bi mechanism
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-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
the two-protein system phenol hydroxylase consists of an oxygenase (PheA1) and a flavin reductase (PheA2). PheA1 catalyzes the efficient ortho-hydroxylation of phenol to catechol when supplemented with PheA2 and FAD/NADH. PheA1 catalyzes the NADH-dependent reduction of free flavins according to a ping pong bi bi mechanism
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-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
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-
-
r
catechol + riboflavin + H2O
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-
-
?
phenol + reduced riboflavin + O2
catechol + riboflavin + H2O
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-
-
?
? + NAD(P)+ + H2O
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-
-
?
resorcinol + NAD(P)H + H+ + O2
? + NAD(P)+ + H2O
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-
-
?
?
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-
enzyme components PheA2 and PheA1 show no protein-protein interaction
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-
?
additional information
?
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enzyme components PheA2 and PheA1 show no protein-protein interaction
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-
?
additional information
?
-
enzyme components PheA2 and PheA1 show no protein-protein interaction
-
-
?
additional information
?
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-
PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
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-
?
additional information
?
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PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
-
-
?
additional information
?
-
PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
-
-
?
additional information
?
-
-
enzyme components PheA2 and PheA1 show no protein-protein interaction
-
-
?
additional information
?
-
enzyme components PheA2 and PheA1 show no protein-protein interaction
-
-
?
additional information
?
-
enzyme components PheA2 and PheA1 show no protein-protein interaction
-
-
?
additional information
?
-
-
PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
-
-
?
additional information
?
-
PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
-
-
?
additional information
?
-
PheA1 is required for activity of flavin reductase PheA2, no activity by PheA1 or PheA2 alone
-
-
?
additional information
?
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the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol
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?
additional information
?
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the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol
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-
?
additional information
?
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the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol
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-
?
additional information
?
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the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol
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-
?
additional information
?
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the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol
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-
?
additional information
?
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substrate speccificities of the three isozymes, overview
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?
additional information
?
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substrate speccificities of the three isozymes, overview
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?