Information on EC 1.14.13.63 - 3-hydroxyphenylacetate 6-hydroxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.13.63
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RECOMMENDED NAME
GeneOntology No.
3-hydroxyphenylacetate 6-hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Styrene degradation
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (6-hydroxylating)
3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.
CAS REGISTRY NUMBER
COMMENTARY hide
114705-01-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BiA1, gene phacB
SwissProt
Manually annotated by BRENDA team
strain BiA1, gene phacB
SwissProt
Manually annotated by BRENDA team
strain JS-7
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Manually annotated by BRENDA team
strain S1, highest enzyme activity when grown on 3-hydroxyphenylacetate
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Manually annotated by BRENDA team
strain S1, highest enzyme activity when grown on 3-hydroxyphenylacetate
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxyphenoxyacetate + NADH + O2
?
show the reaction diagram
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3,4-dihydroxyphenylacetate + NAD(P)H + O2 + H+
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3,4-Dihydroxyphenylacetate + NADH + O2
2,4,5-Trihydroxyphenylacetate + NAD+
show the reaction diagram
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3-Hydroxyphenylacetate + NAD(P)H + O2
?
show the reaction diagram
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enzyme in the 3-hydroxyphenylacetate catabolism
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3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
show the reaction diagram
3-Hydroxyphenylacetate + NADPH + O2
2,5-Dihydroxyphenylacetate + NADP+
show the reaction diagram
4-Hydroxyphenylacetate + NADH + O2
2,4-Dihydroxyphenylacetate + NAD+
show the reaction diagram
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additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
show the reaction diagram
Q078T0
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
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?
3-Hydroxyphenylacetate + NAD(P)H + O2
?
show the reaction diagram
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enzyme in the 3-hydroxyphenylacetate catabolism
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3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activity with NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the enzyme is a cytochrome P450 monooxygenase containing a heme iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Chloromercuri-4-nitrophenol
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5,5'-dithiobis(2-nitrobenzoate)
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Cl-
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competitive to the aromatic substrate
p-hydroxymercuribenzoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
3,4-Dihydroxyphenylacetate
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0.079
3-hydroxyphenylacetate
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0.15
NADH
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0.14
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.6
3,4-Dihydroxyphenylacetate
Flavobacterium sp.
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22.4
3-hydroxyphenylacetate
Flavobacterium sp.
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36
NADH
Flavobacterium sp.
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35.8
NADPH
Flavobacterium sp.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2544
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purified enzyme, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3 - 8.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8.9
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50% of maximal activity at pH 7.3 and 8.9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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SDS-PAGE
50000
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gel filtration
63000
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2 * 63000, SDS-PAGE
150000 - 200000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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37°C, stable
7425
9
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strong inactivation above
7425
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3-hydroxyphenylacetate protects against thermal inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression pattern, sequence comparison, expression in a recombinant Aspergillus nidulans strain
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information