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Enzyme Nomenclature
Information on EC 1.14.13.64 - 4-hydroxybenzoate 1-hydroxylase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.64
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoate 1-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Requires FAD. The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor.
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CAS REGISTRY NUMBER
COMMENTARY
134214-78-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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overexpression of the enzyme increases the tolerance of Candida parapsilosis cells to the antifungal drug terbinafine
physiological function
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overexpression of the enzyme increases the tolerance of Candida parapsilosis cells to the antifungal drug terbinafine
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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
2,4-dihydroxybenzoate + NADPH + O2
1,2,4-trihydroxybenzene + NADP+ + CO2
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-
-
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2-fluoro-4-hydroxybenzoate + NADPH + O2
2-fluoro-1,4-dihydroxybenzene + NADP+ + CO2
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-
-
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3,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
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-
-
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3,4-Dihydroxybenzoate + NADPH + O2
1,2,4-Trihydroxybenzene + NADP+ + CO2
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-
-
-
tetrafluoro-4-hydroxybenzoate + NAD(P)H + O2
2,3,5,6-tetrafluorohydroquinone + NAD(P)+ + CO2
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-
-
-
?
2,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
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-
-
-
?
2,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
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-
-
-
?
2,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
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-
-
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2,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
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-
-
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2-fluoro-4-hydroxybenzoate + NADH + O2
2-fluoro-1,4-dihydroxybenzene + NAD+ + CO2
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-
-
-
2-fluoro-4-hydroxybenzoate + NADH + O2
2-fluoro-1,4-dihydroxybenzene + NAD+ + CO2
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-
-
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3,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
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-
-
-
?
3,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
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-
-
-
?
4-hydroxy-3-nitrobenzoate + NAD(P)H + O2
2-nitrobenzene-1,4-diol + NAD(P)+ + CO2
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-
-
-
?
4-hydroxy-3-nitrobenzoate + NAD(P)H + O2
2-nitrobenzene-1,4-diol + NAD(P)+ + CO2
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-
-
-
?
4-hydroxybenzoate + NAD(P)H + H+ + O2
hydroquinone + NAD(P)+ + H2O + CO2
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-
-
-
?
4-hydroxybenzoate + NAD(P)H + H+ + O2
hydroquinone + NAD(P)+ + H2O + CO2
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-
-
-
?
4-Hydroxybenzoate + NAD(P)H + O2
?
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initial reaction of the catabolism of 4-hydroxybenzoate
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4-Hydroxybenzoate + NAD(P)H + O2
?
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the enzyme is induced when the yeast is grown on either 4-hydroxybenzoate, 2,3-dihydroxybenzoate, or 3,4-dihydroxybenzoate as the sole carbon source
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4-Hydroxybenzoate + NAD(P)H + O2
?
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initial reaction of the catabolism of 4-hydroxybenzoate
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4-hydroxybenzoate + NADH + 2 H+ + O2
hydroquinone + NAD+ + H2O + CO2
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-
-
-
?
4-hydroxybenzoate + NADH + 2 H+ + O2
hydroquinone + NAD+ + H2O + CO2
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-
-
-
?
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
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-
-
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4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
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NADH is the preferred electron donor
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4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
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-
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4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
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NADH is the preferred electron donor
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4-hydroxybenzoate + NADH + O2
hydroquinone + NAD+ + CO2
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the enzyme prefers NADH over NADPH as electron donor
-
-
?
4-hydroxybenzoate + NADH + O2
hydroquinone + NAD+ + CO2
-
the enzyme prefers NADH over NADPH as electron donor
-
-
?
4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
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-
-
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4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
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NADH is the preferred electron donor
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4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
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-
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4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
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NADH is the preferred electron donor
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-
4-hydroxybenzoate + NADPH + O2
hydroquinone + NADP+ + CO2
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the enzyme prefers NADH over NADPH as electron donor
-
-
?
4-hydroxybenzoate + NADPH + O2
hydroquinone + NADP+ + CO2
-
the enzyme prefers NADH over NADPH as electron donor
-
-
?
additional information
?
-
-
the enzyme is induced when yeast is grown on either 4-hydroxybenzoate, 2,4-dihydroxybenzoate or 3,4-dihydroxybenzoate as the sole carbon source
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-
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additional information
?
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the phenolate form of the substrates is important for catalysis and the substrate hydroxylation involvesthe electrophilic attack of the putative flavin hydroperoxide at the C1-atom of the aromatic ring
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-
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additional information
?
-
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the enzyme is induced when yeast is grown on either 4-hydroxybenzoate, 2,4-dihydroxybenzoate or 3,4-dihydroxybenzoate as the sole carbon source
-
-
-
additional information
?
-
-
the phenolate form of the substrates is important for catalysis and the substrate hydroxylation involvesthe electrophilic attack of the putative flavin hydroperoxide at the C1-atom of the aromatic ring
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
-
-
-
-
?
2,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
-
-
-
-
?
3,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
-
-
-
-
?
3,4-dihydroxybenzoate + NAD(P)H + H+ + O2
benzene-1,2,4-triol + NAD(P)+ + H2O + CO2
-
-
-
-
?
4-hydroxybenzoate + NAD(P)H + H+ + O2
hydroquinone + NAD(P)+ + H2O + CO2
-
-
-
-
?
4-hydroxybenzoate + NAD(P)H + H+ + O2
hydroquinone + NAD(P)+ + H2O + CO2
-
-
-
-
?
4-Hydroxybenzoate + NAD(P)H + O2
?
-
initial reaction of the catabolism of 4-hydroxybenzoate
-
-
-
4-Hydroxybenzoate + NAD(P)H + O2
?
-
the enzyme is induced when the yeast is grown on either 4-hydroxybenzoate, 2,3-dihydroxybenzoate, or 3,4-dihydroxybenzoate as the sole carbon source
-
-
-
4-Hydroxybenzoate + NAD(P)H + O2
?
-
initial reaction of the catabolism of 4-hydroxybenzoate
-
-
-
additional information
?
-
-
the enzyme is induced when yeast is grown on either 4-hydroxybenzoate, 2,4-dihydroxybenzoate or 3,4-dihydroxybenzoate as the sole carbon source
-
-
-
additional information
?
-
-
the enzyme is induced when yeast is grown on either 4-hydroxybenzoate, 2,4-dihydroxybenzoate or 3,4-dihydroxybenzoate as the sole carbon source
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 4-hydroxybenzoate 1-hydroxylase gene from Candida parapsilosis CBS604 and a glucosyltransferase (arbutin synthase) gene from Rauvolfia serpentina are introduced into Escherichia coli lead to the production of 54.71 mg/l of arbutin from glucose
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
synthesis
pharmacology
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construction of a novel artificial pathway for arbutin biosynthesis in Escherichia colid. De novo biosynthesis of arbutin from simple carbon sources is established and a generalizable strategy for the biosynthesis of shikimate pathway derived chemicals is provided. Arbutin is a hydroquinone glucoside compound existing in various plants. It is widely used in pharmaceuticaland cosmetic industries owing to its well-known skin-lightening property as well as anti-oxidant, anti-microbial, and anti-inflammatory activities. A 4-hydroxybenzoate 1-hydroxylase gene from Candida parapsilosis CBS604 and a glucosyltransferase (arbutin synthase) gene from Rauvolfia serpentina are introduced into Escherichia coli lead to the production of 54.71 mg/l of arbutin from glucose. Further redirection of carbon flux into arbutin biosynthesis pathway by enhancing shikimate pathway genes enables production of 3.29 g/l arbutin, which is a 60-fold increase compared with the initial strain. Final optimization of glucose concentration added in the culture medium is able to further improve the titer of arbutin to 4.19 g/l in shake flasks experiments, which is around 77-fold higher than that of initial strain
pharmacology
-
construction of a novel artificial pathway for arbutin biosynthesis in Escherichia colid. De novo biosynthesis of arbutin from simple carbon sources is established and a generalizable strategy for the biosynthesis of shikimate pathway derived chemicals is provided. Arbutin is a hydroquinone glucoside compound existing in various plants. It is widely used in pharmaceuticaland cosmetic industries owing to its well-known skin-lightening property as well as anti-oxidant, anti-microbial, and anti-inflammatory activities. A 4-hydroxybenzoate 1-hydroxylase gene from Candida parapsilosis CBS604 and a glucosyltransferase (arbutin synthase) gene from Rauvolfia serpentina are introduced into Escherichia coli lead to the production of 54.71 mg/l of arbutin from glucose. Further redirection of carbon flux into arbutin biosynthesis pathway by enhancing shikimate pathway genes enables production of 3.29 g/l arbutin, which is a 60-fold increase compared with the initial strain. Final optimization of glucose concentration added in the culture medium is able to further improve the titer of arbutin to 4.19 g/l in shake flasks experiments, which is around 77-fold higher than that of initial strain
-
synthesis
-
construction of a novel artificial pathway for arbutin biosynthesis in Escherichia colid. De novo biosynthesis of arbutin from simple carbon sources is established and a generalizable strategy for the biosynthesis of shikimate pathway derived chemicals is provided. Arbutin is a hydroquinone glucoside compound existing in various plants. It is widely used in pharmaceutical and cosmetic industries owing to its well-known skin-lightening property as well as anti-oxidant, anti-microbial, and anti-inflammatory activities. A 4-hydroxybenzoate 1-hydroxylase gene from Candida parapsilosis CBS604 and a glucosyltransferase (arbutin synthase) gene from Rauvolfia serpentina are introduced into Escherichia coli lead to the production of 54.71 mg/l of arbutin from glucose. Further redirection of carbon flux into arbutin biosynthesis pathway by enhancing shikimate pathway genes enables production of 3.29 g/l arbutin, which is a 60-fold increase compared with the initial strain. Final optimization of glucose concentration added in the culture medium is able to further improve the titer of arbutin to 4.19 g/l in shake flasks experiments, which is around 77-fold higher than that of initial strain
synthesis
-
construction of a novel artificial pathway for arbutin biosynthesis in Escherichia colid. De novo biosynthesis of arbutin from simple carbon sources is established and a generalizable strategy for the biosynthesis of shikimate pathway derived chemicals is provided. Arbutin is a hydroquinone glucoside compound existing in various plants. It is widely used in pharmaceutical and cosmetic industries owing to its well-known skin-lightening property as well as anti-oxidant, anti-microbial, and anti-inflammatory activities. A 4-hydroxybenzoate 1-hydroxylase gene from Candida parapsilosis CBS604 and a glucosyltransferase (arbutin synthase) gene from Rauvolfia serpentina are introduced into Escherichia coli lead to the production of 54.71 mg/l of arbutin from glucose. Further redirection of carbon flux into arbutin biosynthesis pathway by enhancing shikimate pathway genes enables production of 3.29 g/l arbutin, which is a 60-fold increase compared with the initial strain. Final optimization of glucose concentration added in the culture medium is able to further improve the titer of arbutin to 4.19 g/l in shake flasks experiments, which is around 77-fold higher than that of initial strain
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.64)
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