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
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Cofactor
Cofactor on EC 1.14.14.20 - phenol 2-monooxygenase (FADH2)
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FAD
PheA2 uses FAD both as a substrate and as a prosthetic group, strictly dependent on, neither FMN nor riboflavin can replace FAD in this reaction. PheA2 is a a homodimer, with each subunit containing a highly fluorescent FAD prosthetic group
FAD
activity of the oxygenase component His6PheA1 of phenol hydroxylase is strictly dependent on FAD
FADH2
FAD is bound to PheA2, binding structure analysis, overview
FADH2
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PheA2 is a single domain homodimeric protein with each FAD-containing subunit being organized around a six-stranded beta-sheet and a capping alpha-helix. The tightly bound FAD prosthetic group binds near the dimer interface, and the re face of the FAD isoalloxazine ring is fully exposed to solvent, binding structure, overview
NADH
PheA2 uses NADH in order to reduce FAD, according to a random sequential kinetic mechanism
NADH
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addition of NADH to crystalline PheA2 reduces the flavin cofactor, the NAD product is bound in a wide solvent-accessible groove adopting an unusual folded conformation with ring stacking, binding structure, overview
NADH
NADH is a much better coenzyme for PheA2 than NADPH
NADPH
can be used instead of NADH as electron donor, using either FAD or FMN as electron acceptor, but with an affinity 5fold or 10fold lower than NADH, respectively
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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. PheA2 contains a dual binding cleft for NADH and FAD substrate, which alternate during catalysis. No activity with FMN, riboflavin, and NADPH
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additional information
the flavoprotein monooxygenase uses electrons of NAD(P)H to activate and cleave a molecule of oxygen through the formation of an intermediate flavin hydroperoxide and enable the incorporation of an oxygen atom into the substrate
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additional information
the flavoprotein monooxygenase uses electrons of NAD(P)H to activate and cleave a molecule of oxygen through the formation of an intermediate flavin hydroperoxide and enable the incorporation of an oxygen atom into the substrate
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additional information
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the free FAD acts as a true substrate. In addition to FAD, PheA2 is also active with FMN and riboflavin. The turnover rate of PheA2 with free flavins is strongly dependent on temperature. At 25°C, the activity with FMN and riboflavin is much higher than with FAD, but when the temperature is raised to 53°C, the turnover rates with the different flavins becomes nearly identical. Dichlorophenolindophenol is a poor cofactor
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additional information
the free FAD acts as a true substrate. In addition to FAD, PheA2 is also active with FMN and riboflavin. The turnover rate of PheA2 with free flavins is strongly dependent on temperature. At 25°C, the activity with FMN and riboflavin is much higher than with FAD, but when the temperature is raised to 53°C, the turnover rates with the different flavins becomes nearly identical. Dichlorophenolindophenol is a poor cofactor
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additional information
the free FAD acts as a true substrate. In addition to FAD, PheA2 is also active with FMN and riboflavin. The turnover rate of PheA2 with free flavins is strongly dependent on temperature. At 25°C, the activity with FMN and riboflavin is much higher than with FAD, but when the temperature is raised to 53°C, the turnover rates with the different flavins becomes nearly identical. Dichlorophenolindophenol is a poor cofactor
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