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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
-
dissimilation
-
basidiomycete
- tetrahydropteridine
-
yarrowia
-
cochliobolus
- lipolytica
- graminis
- lunatus
- isobutene
-
ascomycete
- pharmacology
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
An09g03500, benzoate 1,2-dioxygenase, benzoate 4-hydroxylase, benzoate para-hydroxylase, benzoate-4-hydroxylase, benzoate-p-hydroxylase, benzoic 4-hydroxylase, benzoic acid 4-hydroxylase, BphA, Cyp1, 
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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
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 421–430 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). CP53_ASPNG
517
1
58016
Swiss-Prot
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)
M5CA26_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
212
1
24024
TrEMBL
other Location (Reliability: 5)
M5C331_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
416
1
45826
TrEMBL
other Location (Reliability: 3)
A0A0B2RW13_GLYSO
682
0
76563
TrEMBL
other Location (Reliability: 1)
A2QTW5_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
517
1
58044
TrEMBL
Secretory Pathway (Reliability: 1)
A2QJV6_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
518
1
59381
TrEMBL
Secretory Pathway (Reliability: 1)
Q4WZZ5_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
519
1
58486
TrEMBL
Secretory Pathway (Reliability: 1)
A2QZD1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
588
3
65477
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0F8B0U2_CERFI
494
0
57546
TrEMBL
other Location (Reliability: 1)
C5PCX3_COCP7
Coccidioides posadasii (strain C735)
516
1
58329
TrEMBL
Secretory Pathway (Reliability: 1)
A2QRJ4_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
476
0
52736
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F4YLL5_TALEM
578
3
65028
TrEMBL
Secretory Pathway (Reliability: 1)
V5Z129_9PEZI
504
1
56730
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2S5BD01_9BASI
559
1
62614
TrEMBL
Secretory Pathway (Reliability: 3)
M5BV61_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
345
1
38042
TrEMBL
Secretory Pathway (Reliability: 5)
B8QM33_COCLU
501
1
56798
TrEMBL
Secretory Pathway (Reliability: 1)
A2QBA0_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
505
1
55776
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0B7FYF3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
466
1
51862
TrEMBL
Secretory Pathway (Reliability: 5)
M5CD23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
562
2
62357
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F4Z427_TALEM
527
1
59484
TrEMBL
Secretory Pathway (Reliability: 2)
M5CCU6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
521
1
57651
TrEMBL
other Location (Reliability: 5)
M5CH82_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
241
0
26619
TrEMBL
other Location (Reliability: 1)
M5CEK5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
241
0
26626
TrEMBL
other Location (Reliability: 1)
A2R8R2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
507
1
57686
TrEMBL
Secretory Pathway (Reliability: 1)
M5CDI6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
901
0
99519
TrEMBL
other Location (Reliability: 5)
Q6MYG4_ASPFM
586
1
65348
TrEMBL
other Location (Reliability: 2)
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)
A2QBF9_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
563
1
62739
TrEMBL
Secretory Pathway (Reliability: 1)
A2Q9Q2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
518
1
58707
TrEMBL
Secretory Pathway (Reliability: 1)
Q39LN9_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
413
0
45549
TrEMBL
-
M5CGD3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
180
1
20201
TrEMBL
Secretory Pathway (Reliability: 2)
B8QM33_COCLU
501
1
56798
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking and 3D simulation of inhibition. Reaction mechanism assumes that the enzyme is membrane-bound and suggests that the hydrophobic ligands enter the active site through a channel, that is surrounded by numerous nonpolar residues including four prolines and is adjacent to the membrane-anchoring N-terminus
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, enzyme concentration 0.050 mg/ml, pH 6.0-7.5, 15 days, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protamine sulfate, heat treatment, calcium phosphate gel, ammonium sulfate, DEAE-Sephadex, Sephadex G-150
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protamine sulfate, tricalcium phosphate gel, DEAE-cellulose, alumina C-gamma gel
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of benzoate 4-hydroxylase and cytochrome P450 reductase in Aspergillus niger increases enzyme activity
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gene CYP1f, DNA and amino acid sequence determination and analysis, five introns and six exons, functional expression in Pichia pastoris
gene CYP53B1, functional overexpression in Yarrowia lipolytica strain UOFS Y-2366, multiple copies of CYP53B1 cDNA cloned under control of POX2 promoter, construction of several clones, feeding of stearic acid to the recombinant yeast leads to high accumulation of 4-hydroxybenzoate
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His-tagged benzoate 4-monooxygenase is expressed in Escherichia coli C43(DE3) cells
PCR amplification, expression in Escherichia coli BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
positively regulated at the transcriptional level by benzoic acid. Methyl benzoate and 4-aminobenzoate also act as inducers
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
pharmacology
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. By identifying selected derivatives of cinnamic acid as possible antifungal drugs, and CYP53 family enzymes as their targets, a potential inhibitor-target system for antifungal drugs is developed
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Durham, D.R.
Initial reactions involved in the dissimilation of mandelate by Rhodotorula graminis
J. Bacteriol.
160
778-780
1984
Rhodotorula graminis
brenda
McNamee, C.; Durham, D.R.
Properties of a membrane-associated benzoate-4-hydroxylase from Rhodotorula graminis
Biochem. Biophys. Res. Commun.
129
485-492
1985
Rhodotorula graminis
brenda
Reddy, C.C.; Vaidyanathan, C.S.
Purification and properties of benzoate-4-hydroxylase from a soil pseudomonad
Arch. Biochem. Biophys.
177
488-498
1976
Pseudomonas sp.
brenda
Reddy, C.C.; Vaidyanathan, C.S.
Purification, properties and induction of a specific benzoate-4-hydroxylase from Aspergillus niger (UBC 814)
Biochim. Biophys. Acta
384
46-57
1975
Aspergillus niger, Aspergillus niger UBC 814
brenda
Shailubhai, K.; Sahasrabudhe, S.R.; Vora, K.A.; Modi, V.V.
Degradation of chlorinated derivatives of phenoxyacetic acid and benzoic acid by Aspergillus niger
FEMS Microbiol. Lett.
18
279-282
1983
Aspergillus niger
-
brenda
Fukuda, H.; Nakamura, K.; Sukita, E.; Ogawa, T.; Fujii, T.
Cytochrome P450rm from Rhodotorula minuta catalyzes 4-hydroxylation of benzoate
J. Biochem.
119
314-318
1996
Cystobasidium minutum
brenda
Van Den Brink, J.M.; Van Den Hondel, C.A.M.J.J.; Van Gorcom, R.F.M.
Optimization of the benzoate-inducible benzoate p-hydroxylase cytochrome P450 enzyme system in Aspergillus niger
Appl. Microbiol. Biotechnol.
46
360-364
1996
Aspergillus niger, Aspergillus niger N204
brenda
Faber, B.W.; van Gorcom, R.F.; Duine, J.A.
Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger
Arch. Biochem. Biophys.
394
245-254
2001
Aspergillus niger
brenda
Shiningavamwe, A.; Obiero, G.; Albertyn, J.; Nicaud, J.M.; Smit, M.
Heterologous expression of the benzoate para-hydroxylase encoding gene (CYP53B1) from Rhodotorula minuta by Yarrowia lipolytica
Appl. Microbiol. Biotechnol.
72
323-329
2006
Cystobasidium minutum, Cystobasidium minutum CBS 2177
brenda
Matsuzaki, F.; Wariishi, H.
Molecular characterization of cytochrome P450 catalyzing hydroxylation of benzoates from the white-rot fungus Phanerochaete chrysosporium
Biochem. Biophys. Res. Commun.
334
1184-1190
2005
Phanerochaete chrysosporium (Q4H2B4)
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
235-241
2008
Chromohalobacter sp. HS-2 (A8I4E8), Chromohalobacter sp. HS-2 (A8I4F1), Chromohalobacter sp. HS-2 (A8I4F4), Chromohalobacter sp. HS2 (A8I4E8), Chromohalobacter sp. HS2 (A8I4F1), Chromohalobacter sp. HS2 (A8I4F4)
brenda
Berne, S.; Podobnik, B.; Zupanec, N.; Novak, M.; Krasevec, N.; Turk, S.; Korosec, B.; Lah, L.; Suligoj, E.; Stojan, J.; Gobec, S.; Komel, R.
Virtual screening yields inhibitors of novel antifungal drug target, benzoate 4-monooxygenase
J. Chem. Inf. Model.
52
3053-3063
2012
Curvularia lunata (B8QM33)
brenda
Antunes, M.S.; Hodges, T.K.; Carpita, N.C.
A benzoate-activated promoter from Aspergillus niger and regulation of its activity
Appl. Microbiol. Biotechnol.
100
5479-5489
2016
Aspergillus niger (P17549)
brenda
Korosec, B.; Sova, M.; Turk, S.; Krasevec, N.; Novak, M.; Lah, L.; Stojan, J.; Podobnik, B.; Berne, S.; Zupanec, N.; Bunc, M.; Gobec, S.; Komel, R.
Antifungal activity of cinnamic acid derivatives involves inhibition of benzoate 4-hydroxylase (CYP53)
J. Appl. Microbiol.
116
955-966
2014
Curvularia lunata (B8QM33), Curvularia lunata
brenda
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