1.14.14.9: 4-hydroxyphenylacetate 3-monooxygenase
This is an abbreviated version!
For detailed information about 4-hydroxyphenylacetate 3-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.9
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1.14.14.9
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flavin
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3,4-dihydroxyphenylacetate
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baumannii
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flavin-dependent
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tyrosol
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hydroxytyrosol
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fmnh
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two-protein
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piceatannol
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synthesis
- 1.14.14.9
- flavin
- 3,4-dihydroxyphenylacetate
- baumannii
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flavin-dependent
- tyrosol
- hydroxytyrosol
- fmnh
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two-protein
- piceatannol
- synthesis
Reaction
Synonyms
4 HPA 3-hydroxyylase, 4-HPA hydroxylase, 4-hydroxyphenylacetate 3-hydroxylase, 4-hydroxyphenylacetic acid 3-hydroxylase, 4HPA 3-monooxygenase, 4HPA3H, C2-hpah, EC 1.14.13.3, HPA 3-hydroxylase, HpaB, hpaBC, HpaC, HPAH, More, p-hydroxyphenylacetate 3-hydroxylase, p-hydroxyphenylacetate hydroxylase, p-hydroxyphenylacetic 3-hydroxylase, TPY_2462, two-component p-hydroxyphenylacetate hydroxylase
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Cofactor
Cofactor on EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase
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FAD
FMN and FAD can substitute for each other, required
FAD
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a flavoprotein, provides reduced flavin FAD- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FADH2 reacts with oxygen to form C(4a)-hydroperoxy-FAD, the C2-FADH2-4-hydroxyphenylacetate complex reacts more slowly
FAD
binding structure, binding causes conformational changes, overview
FAD
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FAD is not tightly bound to HpaC, the flavin reductase component of the enzyme, and is bound in the groove in the extended and folded conformation, binding site structure, overview
FADH2
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used as substrate and cofactor, enzyme binds FADH in absence of 4-hydroxyphenlyacetate and protects it from rapid autoxidation by O2
FADH2
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bound to the enzyme in vivo, which has a high affinity for FADH2, cosubstrate needs to be protected by the enzyme against oxidation to FAD by O2
FMN
FMN and FAD can substitute for each other, required
FMN
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a flavoprotein, provides reduced flavin FMNH- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FMNH2 reacts with oxygen to form C(4a)-hydroperoxy-FMN, the C2-FMNH2-4-hydroxyphenylacetate complex reacts more slowly
FMN
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a flavoprotein, provides reduced flavin for the oxygenase component of the enzyme to hydroxylate 4-hydroxyphenylacetate, the apoenzyme of the FMN reductase component C1 binds to oxidized FMN tightly in presence of the substrate
FMN
involved in reaction step 1 catalyzed by the NADH-dependent FMN reductase enzyme component C1
FMNH2
involved in reaction step 2 catalyzed by the monooxygenase enzyme component C2
NAD(P)H
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product NAD+ is bound in the groove in the extended and folded conformation, binding site structure, overview
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similar enzyme which oxidizes both NADH and NADPH
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additional information
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hydroxyphenylacetate forms a dead end complex with the (C2-C4a)-hydroxy-FMN intermediate inhibiting the bound flavin from returning to the oxidized form, FADH2 is equally active, the enzyme oxygenase component C2 has the unusual ability to use both common flavin cofactors in catalysis, kinetics, overview
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