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EC Tree
IUBMB Comments A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
benzoate 4-hydroxylase, benzoate-4-hydroxylase, cyp53b1, benzoate para-hydroxylase, benzoate-p-hydroxylase,
more
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benzoate 1,2-dioxygenase
product of genes benA (large subunit), benB (small subunit), benC (electron transfer component)
benzoate 4-hydroxylase
-
-
-
benzoate para-hydroxylase
benzoate-4-hydroxylase
-
-
-
benzoate-p-hydroxylase
-
-
-
benzoic 4-hydroxylase
-
-
-
benzoic acid 4-hydroxylase
-
-
-
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 para-hydroxylase
-
-
benzoate para-hydroxylase
-
-
CYP53B1
-
-
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benzoate + [reduced NADPH-hemoprotein reductase] + O2 = 4-hydroxybenzoate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
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benzoate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.
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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
-
-
?
4-chlorobenzoate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
4-methylbenzoate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
benzoate + 6,7-dimethyltetrahydropterin + O2
4-hydroxybenzoate + oxidized 6,7-dimethyltetrahydropterin + H2O
-
-
-
r
benzoate + NADH + H+ + O2
4-hydroxybenzoate + NAD+ + H2O
-
-
-
r
benzoate + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + 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
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
-
?
nicotinate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
picolinate + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
benzoate + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
r
benzoate + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
r
benzoate + NADPH + H+ + O2
4-hydroxybenzoate + NADP+ + H2O
-
-
-
r
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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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
-
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
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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FAD
-
2fold stimulation of NADPH oxidation rate
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
-
pteridine independent activity
-
additional information
-
tetrahydropteridine has no effect on benzoate 4-hydroxylase activity
-
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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+
-
required for activity
Fe2+
-
preincubation for 10 min in the presence of benzoate results in maximal activity
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(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one
competitive inhibitor
2,2'-dipyridyl
-
0.05 mM; 50% inhibition
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
4-nitrobenzoate
-
38% inhibition
8-hydroxyquinoline
-
5 mM, complete inhibition
aminopterin
-
0.5 mM, 10% inhibition
benzoate methyl ester
-
slight inhibition
Benzyl acetate
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0.5 mM, 21% inhibition
benzyl alcohol
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0.5 mM, 10% inhibition
benzylformate
-
0.5 mM, 10% inhibition
iodoacetamide
-
5 mM, 43% inhibition
iodoacetate
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5 mM, 23% inhibition
KCN
-
30 mM, 21% inhibition
Mg2+
-
0.001-0.01 mM, complete inhibition
Mn2+
-
0.001-0.01 mM, complete inhibition
Mo2+
-
0.001-0.01 mM, complete inhibition
o-phenanthroline
-
0.05 mM, 70% inhibition
oxalate
-
2 mM, 20% inhibition
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.052 mM, 39% inhibition
phenylalanine
-
0.5 mM, 21% inhibition
Quinacrine
-
0.5 mM, 47% inhibition
quinine-HCl
-
0.5 mM, 42% inhibition
SKF-525A
-
cytochorme P450 inhibitor, 1 mM, 51% inhibition
trans-cinnamate
-
0.5 mM, 55% inhibition
Zn2+
-
0.001-0.01 mM, complete inhibition
CO
-
strong inhibition
Cu2+
-
0.001-0.01 mM, complete inhibition
Cu2+
-
0.005 mM, 50% inhibition
diethyldithiocarbamate
-
5 mM, 95% inhibition
diethyldithiocarbamate
-
0.5 mM, 21% inhibition
Hg2+
-
0.001-0.01 mM, complete inhibition
Hg2+
-
0.005 mM, 70% inhibition
m-Hydroxybenzoate
-
-
m-Hydroxybenzoate
-
12% inhibition
salicylate
-
-
salicylate
-
20% inhibition
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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
-
30% of activity with NADPH as electron donor
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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0.31
2-Chlorobenzoate
-
-
0.097
2-Fluorobenzoate
-
-
0.28
2-Hydroxybenzoate
-
-
0.127
3-chlorobenzoate
-
-
0.086
3-Fluorobenzoate
-
-
0.189
3-Methoxybenzoate
-
-
0.673
3-methylbenzoate
-
-
0.045
6,7-dimethyltetrahydropterin
-
-
0.029
benzoate
-
-
0.019
NADPH
-
-
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2.33
2-Chlorobenzoate
-
-
4.33
2-Fluorobenzoate
-
-
4.17
2-Hydroxybenzoate
-
-
3.67
2-Methylbenzoate
-
-
6.17
3-chlorobenzoate
-
-
4.83
3-Fluorobenzoate
-
-
4.5
3-hydroxybenzoate
-
-
6.17
3-methylbenzoate
-
-
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
1
benzoate
-
turnover rate in microsomes
4
benzoate
-
turnover rate in microsomes
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0.00181
2-phenylpyrimidine-5-carboxylic acid
pH 7.4, 22°C
0.0017
3-methyl-4-(1H-pyrrol-1-yl)benzoic acid
pH 7.4, 22°C
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0.041
-
activity in cells grown on benzoate
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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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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30
-
-
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25 - 38
-
rapid decrease of activity above 38°C and below 25°C
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-
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brenda
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-
brenda
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UniProt
brenda
gene CYP53B1
-
-
brenda
white-rot fungus, a lignin-degrading basidiomycete, ATCC 34541
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
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
gene CYP53B1
-
-
brenda
red yeast
-
-
brenda
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-
-
brenda
-
brenda
-
-
brenda
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-
membrane associated
brenda
-
more than 90% of activity
-
brenda
-
-
brenda
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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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CP53_ASPNG
517
1
58016
Swiss-Prot
Secretory Pathway (Reliability: 1 )
A0A0B2RW13_GLYSO
682
0
76563
TrEMBL
other Location (Reliability: 1 )
Q4WZZ5_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
519
1
58486
TrEMBL
Secretory Pathway (Reliability: 1 )
V5Z129_9PEZI
504
1
56730
TrEMBL
Secretory Pathway (Reliability: 1 )
Q6MYG4_ASPFM
586
1
65348
TrEMBL
other Location (Reliability: 2 )
A2QTT5_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
515
1
58571
TrEMBL
Secretory Pathway (Reliability: 4 )
M5CDI6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
901
0
99519
TrEMBL
other Location (Reliability: 5 )
A0A0F4YLL5_TALEM
578
3
65028
TrEMBL
Secretory Pathway (Reliability: 1 )
A2QRJ4_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
476
0
52736
TrEMBL
Secretory Pathway (Reliability: 1 )
M5BV61_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
345
1
38042
TrEMBL
Secretory Pathway (Reliability: 5 )
Q39LN9_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
413
0
45549
TrEMBL
-
A2QBA0_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
505
1
55776
TrEMBL
Secretory Pathway (Reliability: 2 )
B8MMA4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
516
2
57853
TrEMBL
Secretory Pathway (Reliability: 1 )
B8QM33_COCLU
501
1
56798
TrEMBL
Secretory Pathway (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 )
M5CEK5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
241
0
26626
TrEMBL
other Location (Reliability: 1 )
M5CA26_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
212
1
24024
TrEMBL
other Location (Reliability: 5 )
A0A0F4Z427_TALEM
527
1
59484
TrEMBL
Secretory Pathway (Reliability: 2 )
A2Q9Q2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
518
1
58707
TrEMBL
Secretory Pathway (Reliability: 1 )
M5C331_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
416
1
45826
TrEMBL
other Location (Reliability: 3 )
A0A2S5BD01_9BASI
559
1
62614
TrEMBL
Secretory Pathway (Reliability: 3 )
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 )
A0A0F8B0U2_CERFI
494
0
57546
TrEMBL
other Location (Reliability: 1 )
A2QZD1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
588
3
65477
TrEMBL
Secretory Pathway (Reliability: 5 )
M5CCU6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
521
1
57651
TrEMBL
other Location (Reliability: 5 )
A0A0B7FYF3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
466
1
51862
TrEMBL
Secretory Pathway (Reliability: 5 )
A2R8R2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
507
1
57686
TrEMBL
Secretory Pathway (Reliability: 1 )
A2QF47_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
474
1
54029
TrEMBL
Secretory Pathway (Reliability: 2 )
M5CD23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
562
2
62357
TrEMBL
Secretory Pathway (Reliability: 2 )
C5PCX3_COCP7
Coccidioides posadasii (strain C735)
516
1
58329
TrEMBL
Secretory Pathway (Reliability: 1 )
M5CGD3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
180
1
20201
TrEMBL
Secretory Pathway (Reliability: 2 )
A8I4E8_9GAMM
456
0
51460
TrEMBL
-
A8I4F1_9GAMM
163
0
19290
TrEMBL
-
A8I4F4_9GAMM
342
0
37594
TrEMBL
-
B8QM33_COCLU
501
1
56798
TrEMBL
Secretory Pathway (Reliability: 1 )
Q4H2B4_PHACH
536
0
60050
TrEMBL
-
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60000
x * 60000, about, amino acid sequence calculation
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?
x * 60000, about, amino acid sequence calculation
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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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freezing and thawing has no effect
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quite stable in presence of benzoate
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0-4°C, enzyme concentration 0.050 mg/ml, pH 6.0-7.5, 15 days, no loss of activity
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0-4°C, pH 7.2-8.0, Tris-HCl buffer, 24 h, 50% loss of activity
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4°C, 24 h, 40% loss of activity
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DEAE-Sepharose, benzoate-agarose
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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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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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positively regulated at the transcriptional level by benzoic acid. Methyl benzoate and 4-aminobenzoate also act as inducers
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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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Durham, D.R.
Initial reactions involved in the dissimilation of mandelate by Rhodotorula graminis
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Optimization of the benzoate-inducible benzoate p-hydroxylase cytochrome P450 enzyme system in Aspergillus niger
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Aspergillus niger, Aspergillus niger N204
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Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger
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394
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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
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72
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334
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Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2
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280
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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
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52
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2012
Curvularia lunata (B8QM33)
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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)
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116
955-966
2014
Curvularia lunata (B8QM33), Curvularia lunata
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