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Information on EC 1.14.14.92 - benzoate 4-monooxygenase
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1.14.14.92 benzoate 4-monooxygenaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.
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Word Map
- 1.14.14.92
- rhodotorula
- minuta
-
beta-ketoadipate
- l-phenylalanine
-
basidiomycete
-
dissimilation
-
cochliobolus
- tetrahydropteridine
-
yarrowia
- graminis
- lipolytica
- lunatus
-
ascomycete
- isobutene
- pharmacology
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
benzoate 4-hydroxylase, benzoate-4-hydroxylase, cyp53b1, benzoate para-hydroxylase, benzoate-p-hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzoate 1,2-dioxygenase
benzoate 4-hydroxylase
-
-
-
-
benzoate para-hydroxylase
benzoate-4-hydroxylase
-
-
-
-
benzoate-p-hydroxylase
-
-
-
-
benzoic 4-hydroxylase
-
-
-
-
benzoic acid 4-hydroxylase
-
-
-
-
CYP53B1
EC 1.14.13.12
-
-
formerly
-
hydroxylase, benzoate 4-
-
-
-
-
oxygenase, benzoate 4-mono-
-
-
-
-
additional information
the enzyme belongs to the cytochrome P450 CYP53 family, cf. EC 1.14.13.23
benzoate 1,2-dioxygenase
product of genes benA (large subunit), benB (small subunit), benC (electron transfer component)
benzoate 1,2-dioxygenase
product of genes benA (large subunit), benB (small subunit), benC (electron transfer component)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzoate + [reduced NADPH-hemoprotein reductase] + O2 = 4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + 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
benzoate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.
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CAS REGISTRY NUMBER
COMMENTARY
39391-25-8
-
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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-chlorobenzoate + [reduced NADPH-hemoprotein reductase] + O2
2-chloro-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
2-fluorobenzoate + [reduced NADPH-hemoprotein reductase] + O2
2-fluoro-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
2-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
2,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
2-methylbenzoate + [reduced NADPH-hemoprotein reductase] + O2
2-methyl-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
2-methylbenzoic acid + NADPH + O2
4-hydroxy-2-methylbenzoic acid + NADP+ + H2O
-
-
-
?
3-chlorobenzoate + [reduced NADPH-hemoprotein reductase] + O2
3-chloro-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-fluorobenzoate + [reduced NADPH-hemoprotein reductase] + O2
3-fluoro-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-hydroxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-hydroxybenzoic acid + [reduced NADPH-hemoprotein reductase] + O2
3,4-dihydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
reaction of 3-hydroxybenzoate 4-monooxygenase, EC 1.14.13.23
-
-
?
3-methoxybenzoate + [reduced NADPH-hemoprotein reductase] + O2
3-methoxy-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-methylbenzoate + [reduced NADPH-hemoprotein reductase] + O2
3-methyl-4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
3-methylbenzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxy-3-methylbenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoate + 6,7-dimethyltetrahydropterin + O2
4-hydroxybenzoate + oxidized 6,7-dimethyltetrahydropterin + H2O
-
-
-
-
r
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
cinnamate + [reduced NADPH-hemoprotein reductase] + O2
4-coumarate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very low turnover rate
-
?
benzoate + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
-
r
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
cis-benzoate dihydrodiol is subsequently dehydrogenated to catechol which is cleaved further
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
cis-benzoate dihydrodiol is subsequently dehydrogenated to catechol which is cleaved further
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
specific for benzoate, NADPH is absolutely required, 30% activity with ascorbate as electron donor
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme is involved in degradation of chlorinated benzoic acid derivatives e.g. 2-chlorobenzoate and 3-chlorobenzoate
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
specific for benzoate, NADPH is absolutely required, 30% activity with ascorbate as electron donor
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
benzoic acid has a regulatory effect on the enzyme
-
-
?
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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
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
benzoate + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme is involved in degradation of chlorinated benzoic acid derivatives e.g. 2-chlorobenzoate and 3-chlorobenzoate
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
cis-benzoate dihydrodiol is subsequently dehydrogenated to catechol which is cleaved further
-
?
benzoate + [reduced NADPH-hemoprotein reductase] + O2
2-hydro-1,2-dihydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
cis-benzoate dihydrodiol is subsequently dehydrogenated to catechol which is cleaved further
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
benzoic acid + [reduced NADPH-hemoprotein reductase] + O2
4-hydroxybenzoic acid + [oxidized NADPH-hemoprotein reductase] + H2O
benzoic acid has a regulatory effect on the enzyme
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrahydropteridine
-
required as prosthetic group, maximal activity with 6,7-dimethyl 5,6,7,8-tetrahydropteridine, 60% activity with biopterine and tetrahydrofolic acid
tetrahydropteridine
-
essential for activity, hydroxylation is not supported when NADH, NADPH, dithiothreitol, 2-mercaptoethanol and ascorbic acid are added alone to the reaction mixture, stimulation when added together with tetrahydropteridine
additional information
-
tetrahydropteridine has no effect on benzoate 4-hydroxylase activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
heme iron, the heme-binding domain FSFGPRSCVG at residues 421430 is located in the C-terminal region
NaCl
10% is optimal NaCl concentration for Chromohalobacter sp. strain HS-2
Fe2+
-
preincubation for 10 min in the presence of benzoate results in maximal activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one
competitive inhibitor
2-phenylpyrimidine-5-carboxylic acid
second best inhibitor among hit compounds, good behaviour in the spectral binding assay but weak antifungal activity
3-methyl-4-(1H-pyrrol-1-yl)benzoic acid
best inhibitor among hit compounds, best in the spectral binding assay and has second best antifungal activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
hydroxylation is not supported when NADH, NADPH, dithiothreitol, 2-mercaptoethanol and ascorbic acid are added alone to the reaction mixture, stimulation when added together with tetrahydropteridine
dithiothreitol
-
hydroxylation is not supported when NADH, NADPH, dithiothreitol, 2-mercaptoethanol and ascorbic acid are added alone to the reaction mixture, stimulation when added together with tetrahydropteridine
additional information
benzoic acid induces transcription of the gene encoding the enzyme and has a regulatory effect
-
ascorbic acid
-
hydroxylation is not supported when NADH, NADPH, dithiothreitol, 2-mercaptoethanol and ascorbic acid are added alone to the reaction mixture, stimulation when added together with tetrahydropteridine
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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
0.005
cinnamate
-
reconstituted enzyme system consisting of benzoate 4-hydroxylase i.e. P450rm, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine
0.04
benzoate
-
reconstituted enzyme system consisting of benzoate 4-hydroxylase, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine
0.667
benzoate
-
reconstituted enzyme system consisting of benzoate 4-hydroxylase i.e. P450rm, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine
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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
-
activity in cells grown on benzoate, 2-chlorobenzoate or 3-chlorobenzoate
additional information
-
recombinant enzyme expressed in Yarrowia lipolytica clones, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
-
approx. 35% of maximal activity at pH 4.5, approx. 15% of maximal activity at pH 8.0
5.5 - 8.2
-
approx. 30% of maximal activity at pH 5.5, approx. 35% of maximal activity at pH 8.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
white-rot fungus, a lignin-degrading basidiomycete, ATCC 34541
SwissProt
brenda
ben A subunits; isolated from salted fermented clams
UniProt
brenda
ben B subunits; isolated from salted fermented clams
UniProt
brenda
ben C subunits; isolated from salted fermented clams
UniProt
brenda
ben A subunits; isolated from salted fermented clams
UniProt
brenda
ben B subunits; isolated from salted fermented clams
UniProt
brenda
ben C subunits; isolated from salted fermented clams
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
the enzyme is involved in detoxification of benzoate, a key intermediate in aromatic compound metabolism in fungi. Because this enzyme is unique to fungi, it is a promising drug target in fungal pathogens of other eukaryotes
metabolism
the enzyme is involved in detoxification of benzoate, a key intermediate in aromatic compound metabolism in fungi
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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). BPHA_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
517
1
58044
Swiss-Prot
Secretory Pathway (Reliability: 1)
BPHA_ASPNG
517
1
58016
Swiss-Prot
Secretory Pathway (Reliability: 1)
M5CD23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
562
2
62357
TrEMBL
Secretory Pathway (Reliability: 2)
M5CA26_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
212
1
24024
TrEMBL
other Location (Reliability: 5)
M5CH82_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
241
0
26619
TrEMBL
other Location (Reliability: 1)
A2QBF9_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
563
1
62739
TrEMBL
Secretory Pathway (Reliability: 1)
B8QM33_COCLU
501
1
56798
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F8B0U2_CERFI
494
0
57546
TrEMBL
other Location (Reliability: 1)
A0A0B7FYF3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
466
1
51862
TrEMBL
Secretory Pathway (Reliability: 5)
A2QF47_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
474
1
54029
TrEMBL
Secretory Pathway (Reliability: 2)
A2QTT5_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
515
1
58571
TrEMBL
Secretory Pathway (Reliability: 4)
M5CEK5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
241
0
26626
TrEMBL
other Location (Reliability: 1)
A2QJV6_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
518
1
59381
TrEMBL
Secretory Pathway (Reliability: 1)
B8MMA4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
516
2
57853
TrEMBL
Secretory Pathway (Reliability: 1)