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Information on EC 1.14.13.64 - 4-hydroxybenzoate 1-hydroxylase
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1.14.13.64 4-hydroxybenzoate 1-hydroxylaseIUBMB Comments
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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Word Map
- 1.14.13.64
- parapsilosis
- phenol
- hydroquinone
- flavoprotein
- 1,4-dihydroxybenzene
-
6-hydroxylase
- gentisate
- arbutin
- synthesis
-
fad-dependent
- 3-hydroxybenzoate
- shikimate
-
glucosyltransferase
- pharmacology
The expected taxonomic range for this enzyme is: Candida parapsilosis
Synonyms
4-hydroxybenzoate 1-hydroxylase, 4-hydroxybenzoate 1-hydroxylase (decarboxylating), 4-hydroxybenzoate 1-monooxygenase, MNX1, Mnx1p, Oxygenase, 4-hydroxybenzoate 1-mono, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxybenzoate 1-hydroxylase
4-hydroxybenzoate 1-hydroxylase (decarboxylating)
-
-
-
-
4-hydroxybenzoate 1-monooxygenase
-
-
-
-
MNX1
Mnx1p
Oxygenase, 4-hydroxybenzoate 1-mono
-
-
-
-
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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
-
-
-
?
2-fluoro-4-hydroxybenzoate + NADPH + O2
2-fluoro-1,4-dihydroxybenzene + NADP+ + CO2
-
-
-
?
3,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
-
-
-
?
3,4-Dihydroxybenzoate + NADPH + O2
1,2,4-Trihydroxybenzene + NADP+ + CO2
-
-
-
?
tetrafluoro-4-hydroxybenzoate + NAD(P)H + O2
2,3,5,6-tetrafluorohydroquinone + NAD(P)+ + CO2
-
-
-
-
?
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
-
-
-
-
?
2,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
-
-
-
?
2,4-Dihydroxybenzoate + NADH + O2
1,2,4-Trihydroxybenzene + NAD+ + CO2
-
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
2-fluoro-1,4-dihydroxybenzene + NAD+ + CO2
-
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
2-fluoro-1,4-dihydroxybenzene + NAD+ + 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-hydroxy-3-nitrobenzoate + NAD(P)H + O2
2-nitrobenzene-1,4-diol + NAD(P)+ + CO2
-
-
-
-
?
4-hydroxy-3-nitrobenzoate + NAD(P)H + O2
2-nitrobenzene-1,4-diol + NAD(P)+ + 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
-
-
?
4-hydroxybenzoate + NADH + 2 H+ + O2
hydroquinone + NAD+ + H2O + CO2
-
-
-
?
4-hydroxybenzoate + NADH + 2 H+ + O2
hydroquinone + NAD+ + H2O + CO2
-
-
-
?
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
-
-
-
?
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
-
NADH is the preferred electron donor
-
?
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
-
NADH is the preferred electron donor
-
?
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
-
-
-
?
4-hydroxybenzoate + NADH + O2
hydroquinone + NAD+ + CO2
-
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
-
-
-
?
4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
-
NADH is the preferred electron donor
-
?
4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
-
-
-
?
4-Hydroxybenzoate + NADPH + O2
1,4-Dihydroxybenzene + NADP+ + CO2
-
NADH is the preferred electron donor
-
?
4-hydroxybenzoate + NADPH + O2
hydroquinone + NADP+ + CO2
-
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
-
-
?
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
-
-
?
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 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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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
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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INHIBITOR
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
overexpression of the enzyme increases the tolerance of Candida parapsilosis cells to the antifungal drug terbinafine
physiological function
-
overexpression of the enzyme increases the tolerance of Candida parapsilosis cells to the antifungal drug terbinafine
-
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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). G8B709_CANPC
Candida parapsilosis (strain CDC 317 / ATCC MYA-4646)
479
0
52508
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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SUBUNIT
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
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
an artificial pathway is established in Escherichia coli for high-level production of arbutin from simple carbon sources in Escherichia coli for high-level production of arbutin from simple carbon sources. Introduction of the genes for 4-hydroxybenzoate 1-hydroxylase from Candida parapsilosis CBS604 and hydroquinone glucosyltransferase from Rauvolfia serpentina into Escherichia coli leads 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. 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
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
-
an artificial pathway is established in Escherichia coli for high-level production of arbutin from simple carbon sources in Escherichia coli for high-level production of arbutin from simple carbon sources. Introduction of the genes for 4-hydroxybenzoate 1-hydroxylase from Candida parapsilosis CBS604 and hydroquinone glucosyltransferase from Rauvolfia serpentina into Escherichia coli leads 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. 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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van Berkel, W.J.H.; Eppink, M.H.M.; Middelhoven, W.J.; Vervoort, J.; Rietjens, I.M.C.M.
Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase
FEMS Microbiol. Lett.
121
207-216
1994
Candida parapsilosis, Candida parapsilosis CBS604
brenda
Eppink, M.H.M.; Boeren, S.A.; Vervoort, J.; van Berkel, W.J.H.
Purification and properties of 4-hydroxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide-dependent monooxygenase from Candida parapsilosis CBS604
J. Bacteriol.
179
6680-6687
1997
Candida parapsilosis, Candida parapsilosis CBS604
brenda
Moonen, M.J.H.; Fraaije, M.W.; Rietjens, I.M.C.M.; Laane, C.; Van Berkel, W.J.H.
Flavoenzyme-catalyzed oxygenations and oxidations of phenolic compounds
Adv. Synth. Catal.
344
1023-1035
2002
Candida parapsilosis, Candida parapsilosis CBS604
-
brenda
Holesova, Z.; Jakubkova, M.; Zavadiakova, I.; Zeman, I.; Tomaska, L.; Nosek, J.
Gentisate and 3-oxoadipate pathways in the yeast Candida parapsilosis: identification and functional analysis of the genes coding for 3-hydroxybenzoate 6-hydroxylase and 4-hydroxybenzoate 1-hydroxylase
Microbiology
157
2152-2163
2011
Candida parapsilosis
brenda
Shen, X.; Wang, J.; Wang, J.; Chen, Z.; Yuan, Q.; Yan, Y.
High-level de novo biosynthesis of arbutin in engineered Escherichia coli
Metab. Eng.
42
52-58
2017
Candida parapsilosis, Candida parapsilosis (G8B709), Candida parapsilosis CBS604, Candida parapsilosis CBS604 (G8B709)
brenda
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