HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.14.13.64 - 4-hydroxybenzoate 1-hydroxylase
for references in articles please use BRENDA:EC1.14.13.64Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 1.14.13.64
- dt
- fmn
-
diphosphopyridine
-
decolor
-
methemoglobinemia
- nitroreductase
- amaranth
- dicoumarol
-
fmn-dependent
- nadph-diaphorase
- diaphorases
-
1.6.99.2
- synthesis
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
mnx1p, 4-hydroxybenzoate 1-hydroxylase (decarboxylating), 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxybenzoate 1-hydroxylase (decarboxylating)
-
-
-
-
4-hydroxybenzoate 1-monooxygenase
-
-
-
-
MNX1
Mnx1p
Oxygenase, 4-hydroxybenzoate 1-mono
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
134214-78-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
4-Hydroxybenzoate + NADH + O2
1,4-Dihydroxybenzene + NAD+ + CO2
-
NADH is the preferred electron donor
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 CBS604
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.13.64)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
