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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Application
Application on EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase
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synthesis
enzyme completely transforms 4-substituted halophenols to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM results in a 2.5-20fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography results in the production of purified products with a final yield of between 33% and 38%
synthesis
investigation of a flask-scale production of caffeic acid from p-coumaric acid as the model reaction for HpaBC-catalyzed synthesis of hydroxycinnamic acids. Since the initial concentrations of the substrate p-coumaric acid higher than 40 mM markedly inhibits its 4-hydroxyphenylacetate 3-hydroxylases-catalyzed oxidation, the reaction is carried out by repeatedly adding 20 mM of this substrate to the reaction mixture. Furthermore, by using the whole-cell catalyst in the presence of glycerol, the experimental setup achieves the high-yield production of caffeic acid, i.e., 56.6 mM (10.2 g/l) within 24 h. These catalytic activities of 4-hydroxyphenylacetate 3-hydroxylases will provide an easy and environment-friendly synthetic approach to hydroxycinnamic acids
synthesis
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enzyme shows relatively broad substrate specificity, which allows the conversion of a number of non-natural phenolic compounds, into the corresponding catechols. The reaction can be performed based on formate as the electron donor and the organometallic complex [Rh(bpy)-Cp*(H2O)]2+ (Cp*: 1,2,3,4,5-pentamethylcyclopentadiene, bpy: 2,2'-bipyridyl) as the catalyst for FAD reduction
synthesis
in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively
synthesis
overexpression of the HpaB and HpaC genes in Saccharomyces cerevisiae achieves hydroxytyrosol titers of 1.15 mg/l and 4.6 mg/l in a minimal medium in which either 1 mM tyrosine or 1 mM tyrosol are respectively added
synthesis
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overexpression of the HpaB and HpaC genes in Saccharomyces cerevisiae achieves hydroxytyrosol titers of 1.15 mg/l and 4.6 mg/l in a minimal medium in which either 1 mM tyrosine or 1 mM tyrosol are respectively added
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synthesis
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in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively
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