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Information on EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase
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1.14.13.2 4-hydroxybenzoate 3-monooxygenaseIUBMB Comments
A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).
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Word Map
- 1.14.13.2
- flavin
- fad
- fluorescens
-
flavoproteins
- isoalloxazine
- protocatechuate
-
3,4-dioxygenase
-
ballou
- 2,4-dihydroxybenzoate
-
massey
-
entsch
-
gatti
- 3-hydroxybenzoate
-
c4a-hydroperoxide
- degradation
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
p-hydroxybenzoate hydroxylase, para-hydroxybenzoate hydroxylase, 4-hydroxybenzoate hydroxylase, 4-hydroxybenzoate 3-hydroxylase, m-hydroxybenzoate hydroxylase, 4hba 3-hydroxylase, 4-hba 3-monooxygenase, phbhase, 4-hba-3-hydroxylase, 4-hbmo, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-HBA 3-hydroxylase
4-HBA 3-monooxygenase
4-HBA-3-hydroxylase
-
-
-
-
4-HBMO
4-hydroxybenzoate 3-hydroxylase
4-hydroxybenzoate 3-monooxygenase
-
-
-
-
4-hydroxybenzoate monooxygenase
-
-
-
-
4-hydroxybenzoic hydroxylase
-
-
-
-
m-hydroxybenzoate hydroxylase
MobA
oxygenase, 4-hydroxybenzoate 3-mono-
-
-
-
-
p-hydroxybenzoate hydroxylase
p-hydroxybenzoate-3-hydroxylase
-
-
-
-
p-hydroxybenzoic acid hydrolase
-
-
-
-
p-hydroxybenzoic acid hydroxylase
p-hydroxybenzoic hydroxylase
-
-
-
-
para-hydroxybenzoate hydroxylase
-
-
-
-
PHBAD
-
-
-
-
PHBH
PHBHase
-
-
-
-
PobA
POHBase
-
-
-
-
4-hydroxybenzoate 3-hydroxylase
-
-
-
-
p-hydroxybenzoate hydroxylase
-
-
-
-
p-hydroxybenzoic acid hydroxylase
-
-
-
-
PHBH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
bi uni uni uni ping-pong mechanism
-
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
rate of formation of the flavin hydroperoxide is not influenced by pH-change. Rate of hydroxylation reaction increases with pH. The H-bond network abstracts the phenolic proton from p-hydroxybenzoate in the transition state of oxygen transfer. Product deprotonation enhances the rate of a specific conformational change required for both product relase and the elimination of water
-
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
kinetic scheme of reductive half-reaction, flavin movement can occur in the presence or absence of NADPH, but NADPH stimulates movement to the reactive conformation required for hydride transfer
-
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).
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CAS REGISTRY NUMBER
COMMENTARY
9059-23-8
-
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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
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
3,4-dihydroxybenzoic acid + NADPH + H+ + O2
gallic acid + NADP+ + H2O
-
weak activity
-
-
?
3-bromo-4-hydroxybenzoate + NADPH + O2
?
-
3.2% of the activity with 4-hydroxybenzoate
-
-
?
3-Chloro-4-hydroxybenzoate + NADPH + O2
?
-
6.5% of the activity with 4-hydroxybenzoate
-
-
?
3-Fluoro-4-hydroxybenzoate + NADPH + O2
?
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
4-aminobenzoate + NADPH + O2
?
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + ferricyanide
protocatechuate + NADP+ + ferrocyanide
-
-
-
?
4-toluate + NADPH + O2
?
-
0.29% of the activity with 4-hydroxybenzoate
-
-
?
benzene sulfonate + NADPH + O2
?
-
0.34% of the activity with 4-hydroxybenzoate
-
-
?
m-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
p-hydroxybenzoate + NADPH + O2
? + NADP+ + H2O
is transformed to a lesser extent than m-hydroxybenzoate
-
-
?
2,3-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
3.1% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
1.5% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
slow reaction, formation of at least 3 intermediates, a spectral intermediate that is believed to be an oxygenated form of the enzyme-bound flavin prosthetic group
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
8% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
8% of the activity with 4-hydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2-chloro-4-hydroxybenzoate + NADH + O2
?
-
40% of the activity with 4-hydroxybenzoate
-
-
?
2-chloro-4-hydroxybenzoate + NADH + O2
?
-
40% of the activity with 4-hydroxybenzoate
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
?
-
50% of the activity with 4-hydroxybenzoate
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
?
-
50% of the activity with 4-hydroxybenzoate
-
-
?
3,4-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
the enzyme prefers NADPH to NADH
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme is expressed at basal level, presence of 4-hydroxybenzoate enhances activity
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
inducible enzyme
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
first step in the bacterial metabolism when 4-hydroxybenzoate is used as growth substrate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme catalyzes an intermediate step in the degradation of aromatic compounds in soil microorganisms
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
-
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH. 4HBA hydroxylase can be induced by 4HBA, 4-cresol, and 4-hydroxybenzaldehyde
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
-
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
at least three intermediates
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-mercaptobenzoate + NADPH + O2
4,4'-dithiobisbenzoate + ?
-
50% of the activity with 4-hydroxybenzoate
-
?
additional information
?
-
-
the enzyme also shows low activities with 2- and 3-hydroxybenzoate as well as D-glucose
-
-
-
additional information
?
-
-
p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
-
-
-
additional information
?
-
-
p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
-
-
-
additional information
?
-
is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol
-
-
-
additional information
?
-
-
is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol
-
-
-
additional information
?
-
is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol
-
-
-
additional information
?
-
-
no hydroxylase activity is observed with 3-hydroxybenzoate, resorcinol, 3-nitrophenol, benzoate, 2,4-dihydroxybenzoate, 4-chlorobenzoate, 4-aminobenzoate, 4-aminophenol, 4-nitrophenol, and 4-dinitrobenzene
-
-
-
additional information
?
-
-
a Tyr seems to be involved in substrate activation
-
-
-
additional information
?
-
-
mutant enzyme Y385F hydroxylates 3,4-dihydroxybenzoate to form gallic acid
-
-
-
additional information
?
-
-
Arg42 is involved in binding of the 2'-phosphoadenosine moiety of NADPH
-
-
-
additional information
?
-
-
under anaerobic conditions, the enzyme can catalyze a reduction of FAD by NADPH provided that 4-hydroxybenzoate is present
-
-
-
additional information
?
-
-
the enzyme also shows low activities with 2- and 3-hydroxybenzoate as well as D-glucose
-
-
-
additional information
?
-
-
no activity with 2-hydroxybenzoate and 3-hydroxybenzoate
-
-
-
additional information
?
-
-
no activity with 2-hydroxybenzoate and 3-hydroxybenzoate
-
-
-
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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-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme is expressed at basal level, presence of 4-hydroxybenzoate enhances activity
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
inducible enzyme
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
first step in the bacterial metabolism when 4-hydroxybenzoate is used as growth substrate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme catalyzes an intermediate step in the degradation of aromatic compounds in soil microorganisms
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
-
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
-
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH. 4HBA hydroxylase can be induced by 4HBA, 4-cresol, and 4-hydroxybenzaldehyde
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
additional information
?
-
-
p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
-
-
-
additional information
?
-
-
p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-deaza-FAD
-
when 1-deaza-FAD is used as cofactor, the enzyme carries out each step in catalysis except the transfer of oxygen to 4-hydroxybenzoate
6-Hydroxy-FAD
-
when 6-hydroxy-FAD is used as cofactor, the enzyme has a lower turnover rate than the native enzyme
arabinoflavin adenine dinucleotide
-
like native enzyme the arabinoflavin adenine dinucleotide containing 4-hydroxybenzoate hydroxylase preferentially binds the phenolate form of the substrate. The oxidative part of the catalytic cycle of a FAD-containing 4-hydroxybenzoate hydroxylase differs from the native enzyme. Partial uncoupling of hydroxylation results in the formation of about 0.3 mol of 3,4-dihydroxybenzoate and 0.7 mol of H2O2 per mol of NADPH oxidized
additional information
-
helix H2 is involved in determining the coenzyme specificity
-
FAD
-
Km for strain 420: 220 nM; Km for strain 557: 190 nM; Km for strain IG: 185 nM
FAD
-
flavin motion in 4-hydroxybenzoate hydroxylase is important for efficient reduction
FAD
-
thermodynamic and kinetic constants of the enzyme reconstituted with 8-substituted flavins; two flavin conformations in the enzyme: the in-position and the out-position. Substrate hydroxylation occurs while the flavin in the enzyme is in the in-conformation. Flavin must move to the out-conformation for proper formation of the charge-transfer complex between NADPH and FAD that is necessary for rapid flavin reduction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
metal ions (at 1 mM) Co2+, Ni2+, Mg2+, and Hg2+ shows little influence on hydroxylase activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin-3-O-gallate
-
non-competitive, binds to the enzyme in the proximity of the FAD binding site via formation of three hydrogen bonds
p-hydroxy-3-iodomethylbenzoate
-
1 mM, irreversible crosslinking to the substrate binding site
Phenylglyoxal
-
pseudo-first order kinetics, incorporation into the substrate-binding site
Br-
-
competitive with respect to NADPH; mixed type inhibition with respect to 4-hydroxybenzoate
Cl-
-
competitive with respect to NADPH; mixed type inhibition with respect to 4-hydroxybenzoate
diethyl dicarbonate
-
inhibition of wild-type enzyme, no inhibition of mutant enzyme H162R
I-
-
competitive with respect to NADPH; mixed type inhibition with respect to 4-hydroxybenzoate
PCMB
-
0.015 mM, more than 70% inhibition, partially restored by addition of 0.14 M 2-mercaptoethanol
additional information
-
one of the five sulfhydryl groups reacts rapidly and specifically with NEM, without inactivation of the enzyme
-
additional information
-
multisubunit inhibition by ether derivatives
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dihydroxybenzoate
-
increases the rate of NADP oxidation by 4-hydroxybenzoate, no hydroxylation during subsequent reoxidation by O2
3,4-dihydroxybenzoate
-
increases the rate of NADP oxidation by 4-hydroxybenzoate, no hydroxylation during subsequent reoxidation by O2
Benzoate
-
increases the rate of NADP oxidation by 4-hydroxybenzoate, no hydroxylation during subsequent reoxidation by O2
additional information
-
transcript levels of pobA, encoding p-hydroxybenzoate hydroxylase, are slightly increased in the absence of catabolite repression control protein Crc
-
additional information
-
the substrate analogue 5-hydroxypicolinate stimulates high rates of NADPH consumption by PHBH without the formation of an oxygenated product of 5-hydroxypicolinate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15702
3,4-dihydroxybenzoic acid
-
mutant Y385F/T294A, at pH 8.0 and 30°C
0.03
4-hydroxybenzoate
-
mutant enzyme H162R, H162Y, H162K, R269K, R269Y, R269N, R269S and R269T
additional information
additional information
-
Km value for NADPH above 0.5 mM: mutant enzymes R269D, R269T, R269N, R269Y, H162D, H162T, H162S, H162N
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.69
3,4-dihydroxybenzoic acid
-
mutant Y385F/T294A, at pH 8.0 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.26
-
mutant enzyme Y385F, with 4-hydroxybenzoate as substrate, at pH 8.0 and 30°C
0.45
-
mutant enzyme Y385F, with 3,4-dihydroxybenzoic acid as substrate, at pH 8.0 and 30°C
1.04
-
mutant enzyme Y385F/T294A, with 4-hydroxybenzoate as substrate, at pH 8.0 and 30°C
1.86
-
mutant enzyme Y385F/T294A, with 3,4-dihydroxybenzoic acid as substrate, at pH 8.0 and 30°C
16.85
-
wild type enzyme, with 4-hydroxybenzoate as substrate, at pH 8.0 and 30°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
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
enzyme is expressed in mutant strain MAO4, but not in wild-type strain
-
-
brenda
-
390026, 390028, 390043, 390050, 390052, 390053, 390054, 390055, 390056, 657936, 657951, 658045, 658048, 742143
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the pobA gene encoding the 4-hydroxybenzoate 3-monooxygenase is expressed during growth on hydroxybenzoic acids and glucose
Show AA Sequence and Transmembrane Helices (1923 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
45000
80000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
the monomeric form of PHBH, which is not achieved under conventional conditions, is isolated by entrapment in reverse micelles and by addition of DMSO. The PHBH monomer is catalytically more efficient than the PHBH dimer
tetramer
dimer
-
the monomeric form of PHBH, which is not achieved under conventional conditions, is isolated by entrapment in reverse micelles and by addition of DMSO. The PHBH monomer is catalytically more efficient than the PHBH dimer
tetramer
-
4 * 46000, strain 557, SDS-PAGE; 4 * 47500, strain 420, SDS-PAGE; 4 * 51000, strain IG, SDS-PAGE
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method in the presence of NaH2PO4 and K2HPO4 as precipitants. X-ray diffraction data are collected to a maximum resolution of 2.5 A on a synchrotron beamline. The crystal belongs to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 94.72, c = 359.68 A, gamma = 120°. The asymmetric unit contains two molecules
-
hanging drop vapor diffusion, hanging drops containing 4 mg/ml protein, 100 mM potassium phosphate, pH 7.0, 0.05 mM glutathione, 30 mM sodium sulfite, 0.02 mM FAD, 450 mM ammonium sulfate are equilibrated at 30°C for 7-10 days against a well solution of similar composition, but containing 900 mM ammonium sulfate, crystals of R220Q PHBH diffract to approx. 2.0 A
-
crystal of the enzyme complexed with 4-hydroxybenzoate are obtained using the hanging-drop method
-
crystal structure of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate
-
crystallization of mutant enzymes H162R and R269T by hanging drop vapour diffusion method
-
crystals of a arabinoflavin adenine dinucleotide -containing 4-hydroxybenzoate hydroxylase in complex with 4-hydroxybenzoate are obtained using the hanging drop method
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A400G
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R
A400G/K429R
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
H135P
alters the enzyme's substrate specificity; low ability to hydroxylate 3-aminophenol
K326I
lacks the ability to transform phenol to catechol as the wild-type
N227H/D416A
almost has the same transformation efficiency as mutant N227H/Q292R/D416A
N227H/Q292R/D416A
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
V257A
mutation enables the mutant to transform phenol to catechol, also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol, thus broadens the substrate range. Is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol as the wild-type
A400G
-
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R
-
H135P
-
alters the enzyme's substrate specificity; low ability to hydroxylate 3-aminophenol
-
K326I
-
lacks the ability to transform phenol to catechol as the wild-type
-
V257A
-
mutation enables the mutant to transform phenol to catechol, also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol, thus broadens the substrate range. Is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol as the wild-type
-
D38A
-
kcat/KM for 4-hydroxybenzoate is 16.8fold higher than wild-type value
D38Y
-
kcat/KM for 4-hydroxybenzoate is 11.8fold higher than wild-type value
D38Y/T42R
-
kcat/KM for 4-hydroxybenzoate is 32fold higher than wild-type value
T42R
-
kcat/KM for 4-hydroxybenzoate is 7.2fold higher than wild-type value
E49Q
H72N
K297M
N300D
P293S
-
mutation decreases the stability of the folded mutant protein compared to the wild-type PHBH
R220Q
-
1% of wild-type activity, lower affinity to 4-hydroxybenzoate than wild-type
S212A
-
the turnover of the substrate 2,4-dihydroxybenzoate is 1.5-fold faster than the rate observed with the wild-type
Y201F
Y385F
Y385F/T294A
-
the mutant displays much higher activity toward 3,4-dihydroxybenzoic acid than the wild type enzyme
H162K
-
less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH
H162R
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
H162Y
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
R269K
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
R269S
-
less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH
Y222A
Y222V
E49Q
-
investigation of oxygen half-reaction; mutation enhances the positive charge in the active site of PHBH, rate of hydroxylation is above that of wild-type, the rate of release of product is slower than the rate of return of the flavin to the oxidized state
E49Q
-
mutant has lost the ability in the oxidized state to rapidly exchange the product, i.e., 3,4-dihydroxybenzoate, for the substrate, p-hydroxybenzoate
H72N
-
investigation of oxygen half-reaction; rate of turnover is only about 8% of wild-type enzyme at all pH values
K297M
-
decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme. Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme
K297M
-
investigation of oxygen half-reaction; mutation decreases the positive charge in the active site of PHBH but does not interfere with with the H-bond network, 25fold decrease in the rate of hydroxylation compared to wild-type enzyme
N300D
-
mutation has profound effect on enzyme structure. The side chain of Asp300 moves away from the flavin, disrupting the interaction of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interaction with the flavin ring
N300D
-
330fold reduced reduction rate of the flavin of the enzyme by NADPH compared to wild-type enzyme, redox potential of the flavin is 20-40mV lower than that of the wild-type enzyme. The mutation interferes with the orientation of pyridine nucleotide and flavin during reduction, stabilizes flavin C(4a) intermediates, prevents substrate ionization, and alters the rates and strengths of ligand binding
N300D
-
decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme, Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme
Y201F
-
crystals differ from the wild-type enzyme at two surface positions, 228 and 249
Y201F
-
less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 10fold, when the mutant enzyme-4-hydroxybenzoate complex reacts with oxygen, a long-lived flavin-C(4a)-hydroperoxide is observed, which slowly eliminates H2O2 with very little hydroxylation
Y385F
-
crystals differ from the wild-type enzyme at two surface positions, 228 and 249
Y385F
-
less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 100fold, the mutant enzyme reacts with oxygen to form 25% oxidized enzyme and 75% flavin hydroperoxide, which successfully hydroxylates the substrate. The mutant also hydroxylates the product 3,4-dihydroxybenzoate to form gallic acid
Y385F
-
mutant enzyme with a disrupted hydrogen-bonding network, substitution of 8-Cl-FAD in the mutant gives about 1.5fold increase in hydroxylation rate compared to the wild-type enzyme
Y385F
-
in the oxygen half-reaction, the rate of hydroxylation is 25fold slower than that for the wild-type enzyme at pH 6.5, in contrast to wild-type enzyme there is some formation of H2O2 in the reaction; investigation of oxygen half-reaction
Y385F
-
the mutant displays higher activity toward 3,4-dihydroxybenzoic acid than the wild type enzyme
Y222A
-
mutation makes the lifetime distribution of FAD in the enzyme simpler by removing the ultrafast 10-15 ps lifetime component
Y222V
-
mutation makes the lifetime distribution of FAD in the enzyme simpler by removing the ultrafast 10-15 ps lifetime component
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21
-
room temperature, without glycerol and EDTA, complete inactivation after 20 h
25
40
50
60
4
-
24 h, 40% loss of activity without stabilizer, 10% loss of activity in presence of 4-hydroxybenzoate, FAD and EDTA
4
-
50 mM phosphate buffer, 50 mM Tris-HCl, pH 8.0, 10% glycerol, 10 mM EDTA, loss of activity after 72 h
50
-
10 min, 60% loss of activity, in presence of 0.1 mM 4-hydroxybenzoate the enzyme retains 80% of its activity
50
-
50% loss of activity after 15 min, strain 420; 50% loss of activity after 45 min, strain 557; 50% loss of activity after 9 min, strain IG
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme rapidly loses activity in dilute solutions, below 2 mg/ml, without stabilizer
extremely unstable, undergoing rapid inactivation unless protected by substrates and other stabilizing agents
-
enzyme rapidly loses activity in dilute solutions, below 2 mg/ml, without stabilizer
-
enzyme rapidly loses activity in dilute solutions, below 2 mg/ml, without stabilizer
-
enzyme rapidly loses activity in dilute solutions, below 2 mg/ml, without stabilizer
-
enzyme rapidly loses activity in dilute solutions, below 2 mg/ml, without stabilizer
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 5 mM potassium phosphate, pH 7.5, 5% glycerol, stable for several months
-
0°C-4°C, as a precipitate under a solution of 50 mM potassium phosphate and 0.5 mM EDTA, pH 6.5-7.0, with 70% saturated ammonium sulfate, idefinitely stable
-
4°C, 24 h, 40% loss of activity without stabilizer, 10% loss of activity in presence of 4-hydroxybenzoate, FAD and EDTA
-
4°C, 50 mM phosphate buffer, 50 mM Tris-HCl, pH 8.0, 10% glycerol, 10 mM EDTA, loss of activity after 72 h
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
microheterogeneity of the highly purified enzyme. Different form of enzyme molecules are due to the partial oxidation of Cys116 in the sequence of the enzyme
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
mobA gene from pSEB2 cloned into pZR80. Random mutations introduced into the mobA gene and cloned into pCR2.1-TOPO and transformed into Escherichia coli Top10
mutant enzymes R42S and R42K expressed in transformed Escherichia coli TG2 cells
-
plasmid mutagenesis for high-level expression of 4-hydroxybenzoate hydroxylase
-
When expressed in Escherichia coli, p-hydroxybenzoate hydroxylase transforms p-hydroxybenzoate into protocatechuate
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
4-hydroxybenzoate 3-hydroxylase-encoding pobA transcripts are nearly absent in presence of benzoate and benzoate drastically decreases the transcription of this gene. Repression is mediated by pobR, the transcriptional activator of pobA gene
enzyme expression is induced by 4-hydroxybenzoate via the transcriptional activator PobR. Addition of radish and cabbage hydrolysates to culture significantly induces the expression of the enzyme via PobR
4-hydroxybenzoate 3-hydroxylase-encoding pobA transcripts are nearly absent in presence of benzoate and benzoate drastically decreases the transcription of this gene. Repression is mediated by pobR, the transcriptional activator of pobA gene
-
4-hydroxybenzoate 3-hydroxylase-encoding pobA transcripts are nearly absent in presence of benzoate and benzoate drastically decreases the transcription of this gene. Repression is mediated by pobR, the transcriptional activator of pobA gene
-
-
enzyme expression is induced by 4-hydroxybenzoate via the transcriptional activator PobR. Addition of radish and cabbage hydrolysates to culture significantly induces the expression of the enzyme via PobR
-
enzyme expression is induced by 4-hydroxybenzoate via the transcriptional activator PobR. Addition of radish and cabbage hydrolysates to culture significantly induces the expression of the enzyme via PobR
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
a bienzyme-based Clark electrode is developed for the interference-free determination of L-glutamate. This sensor is based on the specific dehydrogenation by L-glutamate dehydrogenase (EC 1.4.1.3) in combination with p-hydroxybenzoate hydroxylase (EC 1.14.13.2). The enzymes are entrapped by a poly(carbamoyl) sulfonate hydrogel on a Teflon membrane
degradation
degradation
-
in soil conditions, Phomopsis liquidambari effectively decomposes 99% of the available 4-hydroxybenzoic acid within 48 h. 4-Hydroxybenzoic acid hydroxylase activity is present in a high level early at 20 h, followed by 3,4-dihydroxybenzoic acid decarboxylase which reaches its highest relative activity at 24 h, and finally catechol 1,2-dioxygenase exhibits peak activity at 32 h
degradation
-
in soil conditions, Phomopsis liquidambari effectively decomposes 99% of the available 4-hydroxybenzoic acid within 48 h. 4-Hydroxybenzoic acid hydroxylase activity is present in a high level early at 20 h, followed by 3,4-dihydroxybenzoic acid decarboxylase which reaches its highest relative activity at 24 h, and finally catechol 1,2-dioxygenase exhibits peak activity at 32 h
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whited, G.M.; Gibson, D.T.
Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1
J. Bacteriol.
173
3017-3020
1991
Pseudomonas mendocina, Pseudomonas mendocina KR1
brenda
Howell, L.G.; Spector, T.; Massey, V.
Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
J. Biol. Chem.
247
4340-4350
1972
Pseudomonas fluorescens
brenda
Spector, T.; Massey, V.
Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
J. Biol. Chem.
247
4679-4687
1972
Pseudomonas fluorescens
brenda
Spector, T.; Massey, V.
p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate
J. Biol. Chem.
247
5632-5636
1972
Pseudomonas fluorescens
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Delftia acidovorans, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas putida A 3.12, Pseudomonas putida M-6
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Pseudomonas fluorescens
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Pseudomonas aeruginosa
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Pseudomonas fluorescens
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Pseudomonas aeruginosa
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Pseudomonas fluorescens
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Pseudomonas fluorescens
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Pseudomonas fluorescens
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Chemical modification of sulfhydryl groups in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Involvement in catalysis and assignment in the sequence
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Pseudomonas fluorescens
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Pseudomonas fluorescens
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Purification and properties of p-hydroxybenzoate hydroxylases from Rhodococcus strains
Biochemistry (Moscow)
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Rhodococcus opacus, Rhodococcus rhodnii, Rhodococcus rhodnii 135, Rhodococcus rhodochrous, Rhodococcus rhodochrous 172, Rhodococcus sp., Rhodococcus sp. 400
brenda
Moran, G.R.; Entsch, B.; Palfey, B.A.; Ballou, D.P.
Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala
Biochemistry
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Pseudomonas aeruginosa (P20586)
brenda
Fernandez, J.; Dimarco, A.A.; Ornston, L.N.; Harayama, S.
Purification and characterization of Acinetobacter calcoaceticus 4-hydroxybenzoate 3-hydroxylase after its overexpression in Escherichia coli
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Acinetobacter calcoaceticus
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Klebsiella pneumoniae
brenda
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Moraxella sp., Moraxella sp. GU2
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Salituro, F.G.; Demeter, D.A.; Weintraub, H.J.R.; Lippert, B.J.; Resvick, R.J.; McDonald, I.A.
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Pseudomonas fluorescens
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Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin
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Pseudomonas fluorescens
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Pseudomonas aeruginosa, Pseudomonas fluorescens (P00438)
brenda
Eppink, M.H.M.; Schreuder, H.A.; Van Berkel, W.J.H.
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Pseudomonas fluorescens
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Seibold, B.; Matthes, M.; Eppink, M.H.M.; Lingens, F.; Van Berkel, W.J.H.; Mueller, R.
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Pseudomonas sp., Pseudomonas sp. CBS3
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Eppink, M.H.M.; Schreuder, H.A.; Van Berkel, W.J.H.
Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants
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Pseudomonas fluorescens
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Purification and characterization of p-hydroxybenzoate 3-hydroxylase from Comamonas testosteroni
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Acinetobacter sp., Comamonas testosteroni, Comamonas testosteroni Kh 122-3S, Pseudomonas sp.
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Comamonas testosteroni
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Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring
Biochemistry
33
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1994
Pseudomonas fluorescens
brenda
Lah, M.S.; Palfey, B.A.; Schreuder, H.A.; Ludwig, M.L.
Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: The Tyr201Phe, Tyr385Phe, and Asn300Asp variants
Biochemistry
33
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Pseudomonas aeruginosa
brenda
Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
Comparison of chemical inactivation of salicylate 5-hydroxylase, m-hydroxybenzoate 6-hydroxylase, and p-hydroxybenzoate 3-hydroxylase from Rhodococcus erythropolis
Seimei Kogaku Kogyo Gijutsu Kenkyusho Kenkyu Hokoku
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Rhodococcus erythropolis
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brenda
Entsch, B.; Palfey, B.A.; Ballou, D.P.; Massey, V.
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Pseudomonas aeruginosa
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Palfey, B.A.; Entsch, B.; Ballou, D.P.; Massey, V.
Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp
Biochemistry
33
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1994
Pseudomonas aeruginosa
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Moran, G.R.; Entsch, B.
Plasmid mutagenesis by PCR for high-level expression of para-hydroxybenzoate hydroxylase
Protein Expr. Purif.
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Pseudomonas aeruginosa
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Ortiz-Maldonado, M.; Gatti, D.; Ballou, D.P.; Massey, V.
Structure-function correlation of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins
Biochemistry
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Pseudomonas aeruginosa
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Ortiz-Maldonado, M.; Aeschliman, S.M.; Ballou, D.P.; Masey, V.
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl flavin
Biochemistry
40
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2001
Pseudomonas aeruginosa
brenda
Palfey, B.A.; Basu, R.; Frederick, K.K.; Entsch, B.; Ballou, D.P.
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant
Biochemistry
41
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2002
Pseudomonas aeruginosa
brenda
Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase
Biochemistry
42
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2003
Pseudomonas aeruginosa
brenda
Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis
Biochemistry
43
15246-15257
2004
Pseudomonas aeruginosa
brenda
Ortiz-Maldonado, M.; Cole, L.J.; Dumas, S.M.; Entsch, B.; Ballou, D.P.
Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover
Biochemistry
43
1569-1579
2004
Pseudomonas aeruginosa
brenda
Wang, J.; Ortiz-Maldonado, M.; Entsch, B.; Massey, V.; Ballou, D.; Gatti, D.L.
Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase
Proc. Natl. Acad. Sci. USA
99
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2002
Pseudomonas aeruginosa (P20586)
brenda
Frederick, K.K.; Palfey, B.A.
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase
Biochemistry
44
13304-13314
2005
Pseudomonas aeruginosa (P20586)
brenda
Bertani, I.; Kojic, M.; Venturi, V.
Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358
Microbiology
147
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Pseudomonas putida, Pseudomonas putida (Q9R9T1), Pseudomonas putida WCS358, Pseudomonas putida WCS358 (Q9R9T1)
brenda
Kwon, S.Y.; Kang, B.S.; Kim, G.H.; Kim, K.J.
Expression, purification, crystallization and initial crystallographic characterization of the p-hydroxybenzoate hydroxylase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
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2007
Corynebacterium glutamicum
brenda
Huang, Y.; Zhao, K.X.; Shen, X.H.; Jiang, C.Y.; Liu, S.J.
Genetic and biochemical characterization of a 4-hydroxybenzoate hydroxylase from Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
78
75-83
2008
Corynebacterium glutamicum
brenda
Chang, H.K.; Zylstra, G.J.
Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase
Biochem. Biophys. Res. Commun.
371
149-153
2008
Comamonas testosteroni (Q6SSJ6), Comamonas testosteroni GZ39, Comamonas testosteroni GZ39 (Q6SSJ6)
brenda
Kudryashova, E.V.; Visser, A.J.; van Berkel, W.J.
Monomer formation and function of p-hydroxybenzoate hydroxylase in reverse micelles and in dimethylsulfoxide/water mixtures
Chembiochem
9
413-419
2008
Pseudomonas fluorescens
brenda
Deveryshetty, J.; Suvekbala, V.; Varadamshetty, G.; Phale, P.S.
Metabolism of 2-, 3- and 4-hydroxybenzoates by soil isolates Alcaligenes sp. strain PPH and Pseudomonas sp. strain PPD
FEMS Microbiol. Lett.
268
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2007
Alcaligenes sp., Pseudomonas sp.
brenda
Kim, D.; Kim, S.W.; Choi, K.Y.; Lee, J.S.; Kim, E.
Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2
FEMS Microbiol. Lett.
280
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2008
Chromohalobacter sp., Chromohalobacter sp. HS-2
brenda
Van Den Berg, P.A.; Grever, K.; Van Hoek, A.; Van Berkel, W.J.; Visser, A.J.
Time-resolved fluorescence analysis of the mobile flavin cofactor in p-hydroxybenzoate hydroxylase
J. Chem. Sci.
119
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2007
Pseudomonas fluorescens
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brenda
Cui, Y.; Barford, J.P.; Renneberg, R.
Development of an L-glutamate biosensor using the coimmobilization of L-glutamate dehydrogenase and p-hydroxybenzoate hydroxylase on a Clark-type electrode
Sens. Actuators B Chem.
B127
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2007
Pseudomonas sp.
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Zimmermann, T.; Sorg, T.; Siehler, S.Y.; Gerischer, U.
Role of Acinetobacter baylyi Crc in catabolite repression of enzymes for aromatic compound catabolism
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Acinetobacter baylyi, Acinetobacter baylyi ADPU54
brenda
Chen, Y.; Peng, Y.; Dai, C.; Ju, Q.
Biodegradation of 4-hydroxybenzoic acid by Phomopsis liquidambari
Appl. Soil Ecol.
51
102-110
2011
Diaporthe liquidambaris, Diaporthe liquidambaris B3
brenda
Donoso, R.A.; Perez-Pantoja, D.; Gonzalez, B.
Strict and direct transcriptional repression of the pobA gene by benzoate avoids 4-hydroxybenzoate degradation in the pollutant degrader bacterium Cupriavidus necator JMP134
Environ. Microbiol.
13
1590-1600
2011
Cupriavidus necator, Cupriavidus necator JMP 134-1
brenda
Romero-Silva, M.J.; Mendez, V.; Agullo, L.; Seeger, M.
Genomic and functional analyses of the gentisate and protocatechuate ring-cleavage pathways and related 3-hydroxybenzoate and 4-hydroxybenzoate peripheral pathways in Burkholderia xenovorans LB400
PLoS ONE
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e56038
2013
Paraburkholderia xenovorans
brenda
Chen, Z.; Shen, X.; Wang, J.; Wang, J.; Yuan, Q.; Yan, Y.
Rational engineering of p-hydroxybenzoate hydroxylase to enable efficient gallic acid synthesis via a novel artificial biosynthetic pathway
Biotechnol. Bioeng.
114
2571-2580
2017
Pseudomonas aeruginosa
brenda
Dalvi, S.; Youssef, N.H.; Fathepure, B.Z.
Microbial community structure analysis of a benzoate-degrading halophilic archaeal enrichment
Extremophiles
20
311-321
2016
Haloferax volcanii, Haloferax volcanii DS2
brenda
Ceveryshetty, J.; Suvekbala, V.; Varadamshetty, G.; Phale, P.S.
Metabolism of 2-, 3- and 4-hydroxybenzoates by soil isolates Alcaligenes sp. strain PPH and Pseudomonas sp. strain PPD
FEMS Microbiol. Lett.
268
59-66
2007
Alcaligenes sp. PPH, Pseudomonas sp. PPD
brenda
Van Den Berg, P.A.; Grever, K.; Van Hoek, A.; Van Berkel, W.J.; Visser, A.J.
Time-resolved fluorescence analysis of the mobile flavin cofactor in p-hydroxybenzoate hydroxylase
J. Chem. Sci.
119
123-133
2007
Pseudomonas fluorescens
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brenda
Wang, J.-Y.; Zhou, L.; Chen, B.; Sun, S.; Zhang, W.; Li, M.; Tang, H.; Jiang, B.-L.; Tang, J.L.; He, Y.-W.
A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
Sci. Rep.
5
18456
2015
Xanthomonas campestris, Xanthomonas campestris ATCC 33913
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brenda
Cui, Y.; Barford, J.P.; Renneberg, R.
Development of an L-glutamate biosensor using the coimmobilization of L-glutamate dehydrogenase and p-hydroxybenzoate hydroxylase on a Clark-type electrode
Sens. Actuators B Chem.
B127
358-361
2007
Pseudomonas sp.
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brenda
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