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Information on EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase and Organism(s) Escherichia coli and UniProt Accession Q57160
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1.14.14.9 4-hydroxyphenylacetate 3-monooxygenaseIUBMB Comments
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor . FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].
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Word Map
- 1.14.14.9
- flavin
- 3,4-dihydroxyphenylacetate
- baumannii
-
flavin-dependent
- tyrosol
- hydroxytyrosol
- fmnh
-
two-protein
- piceatannol
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hpabc, 4-hydroxyphenylacetate 3-hydroxylase, p-hydroxyphenylacetate 3-hydroxylase, p-hydroxyphenylacetate hydroxylase, 4-hydroxyphenylacetate 3-monooxygenase, 4-hpa hydroxylase, 4-hydroxyphenylacetic acid 3-hydroxylase, 4hpa3h, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4 HPA 3-hydroxyylase
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-
-
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4-hydroxyphenylacetate 3-hydroxylase
4-hydroxyphenylacetic acid 3-hydroxylase
-
-
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HpaB
p-hydroxyphenylacetate 3-hydroxylase
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-
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p-hydroxyphenylacetate hydroxylase
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-
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p-hydroxyphenylacetic 3-hydroxylase
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4-hydroxyphenylacetate 3-hydroxylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
member of novel two-component flavin-diffusible monooxygenase family, both components required for hydroxylation. The genes are located on the same operon. Physical interaction between HpaB and HpaC is not required, enhancement of activity by direct interaction is not excluded. Contains reductase component
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4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
new type of FADH-utilizing monooxygenase
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4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
two enzymes suggested to be required for hydroxylase activity, member of new family of two-component aromatic hydroxylases. The hydroxylase, a flavoprotein, is encoded by hpaB and the coupling protein by hpaC gene
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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hydroxylation
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
4-hydroxyphenylacetate,FAD:oxygen oxidoreductase (3-hydroxylating)
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor [4]. FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].
CAS REGISTRY NUMBER
COMMENTARY
37256-71-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-bromophenol + NADH + H+ + O2
4-bromocatechol + NAD+ + H2O
rate of halophenol consumption 2.9 microM/min/g cell dry weight
-
-
?
4-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
rate of halophenol consumption 3.3 microM/min/g cell dry weight
-
-
?
4-fluorophenol + NADH + H+ + O2
4-fluorocatechol + NAD+ + H2O
rate of halophenol consumption 5.3 microM/min/g cell dry weight
-
-
?
4-iodophenol + NADH + H+ + O2
4-iodocatechol + NAD+ + H2O
rate of halophenol consumption 1.7 microM/min/g cell dry weight
-
-
?
2,5-dihydroxyphenylacetate + ?
?
-
155% of 4-hydroxyphenylacetate activity
-
-
?
3-hydroxyphenylacetate + FMNH2 + O2
3,4-hydroxyphenylacetate + FMN + H2O
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-
-
-
?
3-hydroxyphenylacetate + NADH + H+ + O2
3,4-hydroxyphenylacetate + NAD+ + H2O
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-
-
-
?
3-hydroxyphenylacetate + NADH + O2
3,4-hydroxyphenylacetate + NAD+ + H2O
-
82% activity of 4-hydroxyphenylacetate
-
?
4-hydroxyphenylacetate + FADH2 + O2
3,4-dihydroxyphenylacetate + FAD + H2O
-
-
-
-
?
L-tyrosine + FADH2 + O2
L-(3,4-dihydroxy)phenylalanine + FAD + H2O
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-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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O2 can be replaced by FADH
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis
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ir
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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initial reaction in the degradation of 4-hydroxyphenylacetate
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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inducible chromosomally encoded meta-cleavage pathway of aromatic degradation
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?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway
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?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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4-hydroxyphenylacetic acid degradative pathway
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?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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first enzyme in 4-hydroxyphenylacetate metabolism
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?
additional information
?
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rather broad substrate specificity, acting on mono- and dihydric phenols. Several substrates are below 50% of activity
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-
?
additional information
?
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3- and 4-hydroxyphenylacetate are both catalyzed by 3- or 4-hydroxyphenylacetate hydroxylase by the same route with 3,4-dihydroxyphenylacetate as the first common intermediate, cells grown on one compound are fully induced for the catabolism of the other
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-
?
additional information
?
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the enzyme does not form stable complexes or channel substrates with the NAD(P)H-flavin oxidoredctase HpaC, but NAD(P)H-flavin oxidoreductase HpaC is required for delivering of sufficient amounts of FADH2
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?
additional information
?
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no substrates: benzoic acid, dihydroxybenzoic acid, 4-methoxyphenylacetic acid, catechol, 4-hydroxy-D-2-phenylglycine, 4-hydroxy-L-2-phenylglycine, 3-hydroxy-4-methoxyphenylacetic acid, 4-tert-butylphenol, 3-methoxyphenylacetic acid, 4-hydroxy-3-methoxyphenylacetic acid
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylacetate + FADH2 + O2
3,4-dihydroxyphenylacetate + FAD + H2O
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-
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?
additional information
?
-
-
the enzyme does not form stable complexes or channel substrates with the NAD(P)H-flavin oxidoredctase HpaC, but NAD(P)H-flavin oxidoreductase HpaC is required for delivering of sufficient amounts of FADH2
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
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initial reaction in the degradation of 4-hydroxyphenylacetate
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
inducible chromosomally encoded meta-cleavage pathway of aromatic degradation
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
4-hydroxyphenylacetic acid degradative pathway
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
first enzyme in 4-hydroxyphenylacetate metabolism
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme is induced by 4-hydroxyphenylacetate, requiring NAD(P)H-flavin oxidoreductase HpaC for delivering of sufficient amounts of FADH2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, FADH2/FAD binding capacity, enzyme kinetics in a coupled assay with HpaC, a NAD(P)H-flavin oxidoreductase
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
120000 Da enzyme encoded by hpaB shows low hydroxylase activity which is increased in the presence of FAD and the coupling protein HpaC
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the active site is covered by a loop of great plasticity and strong tolerance towards extensive mutagenesis, but also is flexible loop and enables the entrance and stable binding of substrates into the active site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H155A
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drastically decreased hydroxylase activity with substrate 3-hydroxyphenylacetate
R113A
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drastically decreased hydroxylase activity with substrate 3-hydroxyphenylacetate
R379G
contrary to wild-type, mutant is not able to grow on 3-hydroxyphenylacetic acid. Residue 379 is located in the vicinity of the 4-hydroxyphenylacetic acid binding site, and plays an important role in mediating the entrance and stable binding of substrates to the active site
R379S
contrary to wild-type, mutant is not able to grow on 3-hydroxyphenylacetic acid
synthesis
construction of biosynthetic pathways for the production of tyrosol acetate and hydroxytyrosol acetate in Escherichia coli. Escherichia coli YeaE is the best aldehyde reductase for tyrosol accumulation. Tyrosol acetate production is achieved by overexpression of alcohol acetyltransferase ATF1 from Saccharomyces cerevisiae, and hydroxytyrosol acetate production by overexpression of 4-hydroxyphenylacetate 3-hydroxylase genes HpaBC
Y117A
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drastically decreased hydroxylase activity with substrate 3-hydroxyphenylacetate
additional information
additional information
-
creation of 4-hydroxyphenylacetate-negative mutants by minimal salt medium with ethylmethanesulfonate
additional information
changing the amino acid residues of section I of the flexible loop (mutant XS2, amino acids 207-211, GlyPheGlySerAla) into larger ones does not change the original secondary structure and the flexibility of the loop. The mutants show decreased activity towards substrates 4-coumaric acid, umbelliferone, resveratrol and naringenin. Changing the amino acid residues of section III of the flexible loop (mutant XS3, amino acids 215-217, GlyGluAsn) increases the Km values of towards p-coumaric acid and umbelliferone by 1.7fold and 1.2fold, respectively. The kcat value towards umbelliferone decreases by almost 2fold. Mutant XS4 incorporating the mutations in both XS2 and XS3 still keeps the secondary structure of the loop unchanged unchanged. In mutant XS5 the secondary structure of the loop is changed by replacing residues in section II of the loop (GlnValMet) with GlySerGly. Mutant XS5 shows reduced catalytic activity towards p-coumaric acid, umbelliferone and resveratrol. Mutant XS6 employs a loop containing mainly Gly, Ser, and Asp residues and shows the almost same specificity constant values towards p-coumaric acid and umbelliferone as wild-type
additional information
-
changing the amino acid residues of section I of the flexible loop (mutant XS2, amino acids 207-211, GlyPheGlySerAla) into larger ones does not change the original secondary structure and the flexibility of the loop. The mutants show decreased activity towards substrates 4-coumaric acid, umbelliferone, resveratrol and naringenin. Changing the amino acid residues of section III of the flexible loop (mutant XS3, amino acids 215-217, GlyGluAsn) increases the Km values of towards p-coumaric acid and umbelliferone by 1.7fold and 1.2fold, respectively. The kcat value towards umbelliferone decreases by almost 2fold. Mutant XS4 incorporating the mutations in both XS2 and XS3 still keeps the secondary structure of the loop unchanged unchanged. In mutant XS5 the secondary structure of the loop is changed by replacing residues in section II of the loop (GlnValMet) with GlySerGly. Mutant XS5 shows reduced catalytic activity towards p-coumaric acid, umbelliferone and resveratrol. Mutant XS6 employs a loop containing mainly Gly, Ser, and Asp residues and shows the almost same specificity constant values towards p-coumaric acid and umbelliferone as wild-type
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, HpaC, small protein, very stable, no significant loss of activity during 2 months
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4°C, 20 mM phosphate buffer, pH 8.0, concentrated with polyethylene glycol 20000
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion-exchange, gel filtration. Affinity chromatography for the expressed cholin-binding domain containing HpaB protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
synthesis
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooper, R.A.; Skinner, M.A.
Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli
J. Bacteriol.
143
302-306
1980
Escherichia coli, Escherichia coli C
Prieto, M.A.; Garcia, J.L.
Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme
J. Biol. Chem.
269
22823-22829
1994
Escherichia coli, no activity in Escherichia coli K-12
Prieto, M.A.; Perez-Aranda, A.; Garcia, J.L.
Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range
J. Bacteriol.
175
2162-2167
1993
Escherichia coli, no activity in Escherichia coli K-12
Xun, L.; Sandvik, E.R.
Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase
Appl. Environ. Microbiol.
66
481-486
2000
Escherichia coli
Galan, B.; Diaz, E.; Prieto, M.A.; Garcia, J.L.
Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily
J. Bacteriol.
182
627-636
2000
Escherichia coli, Klebsiella pneumoniae
Chaiyen, P.; Suadee, C.; Wilairat, P.
A novel two-protein component flavoprotein hydroxylase. p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii
Eur. J. Biochem.
268
5550-5561
2001
Acinetobacter baumannii, Escherichia coli, Pseudomonas putida
Louie, T.M.; Xie, X.S.; Xun, L.
Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase
Biochemistry
42
7509-7517
2003
Escherichia coli
Coulombel, L.; Nolan, L.C.; Nikodinovic, J.; Doyle, E.M.; OConnor, K.E.
Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase
Appl. Microbiol. Biotechnol.
89
1867-1875
2011
Escherichia coli (Q57160), Escherichia coli
Huang, Q.; Lin, Y.; Yan, Y.
Caffeic acid production enhancement by engineering a phenylalanine over-producing Escherichia coli strain
Biotechnol. Bioeng.
110
3188-3196
2013
Escherichia coli, Escherichia coli ATCC 31884
Kim, H.; Kim, S.; Kim, D.; Yoon, S.H.
A single amino acid substitution in aromatic hydroxylase (HpaB) of Escherichia coli alters substrate specificity of the structural isomers of hydroxyphenylacetate
BMC Microbiol.
20
109
2020
Escherichia coli (A0A140NG21), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NG21)
Deng, Y.; Faivre, B.; Back, O.; Lombard, M.; Pecqueur, L.; Fontecave, M.
Structural and functional characterization of 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli
ChemBioChem
21
163-170
2020
Escherichia coli
Guo, D.; Fu, X.; Sun, Y.; Li, X.; Pan, H.
De novo biosynthesis of tyrosol acetate and hydroxytyrosol acetate from glucose in engineered Escherichia coli
Enzyme Microb. Technol.
150
109886
2021
Escherichia coli (A0A140NG21), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NG21)
Muniz-Calvo, S.; Bisquert, R.; Puig, S.; Guillamon, J.M.
Overproduction of hydroxytyrosol in Saccharomyces cerevisiae by heterologous overexpression of the Escherichia coli 4-hydroxyphenylacetate 3-monooxygenase
Food Chem.
308
125646
2020
Escherichia coli (A0A140NG21), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NG21)
Wang, L.; Ma, X.; Ruan, H.; Chen, Y.; Gao, L.; Lei, T.; Li, Y.; Gui, L.; Guo, L.; Xia, T.; Wang, Y.
Optimization of the biosynthesis of B-ring ortho-hydroxylated flavonoids using the 4-hydroxyphenylacetate 3-hydroxylase complex (HpaBC) of Escherichia coli
Molecules
26
2919
2021
Escherichia coli (A0A140NG21), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NG21)
Shen, X.; Zhou, D.; Lin, Y.; Wang, J.; Gao, S.; Kandavelu, P.; Zhang, H.; Zhang, R.; Wang, B.C.; Rose, J.; Yuan, Q.; Yan, Y.
Structural insights into catalytic versatility of the flavin-dependent hydroxylase (HpaB) from Escherichia coli
Sci. Rep.
9
7087
2019
Escherichia coli (A0A140NG21), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NG21)
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