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IUBMB Comments A flavoprotein (FAD). Acts on anthranilate and 4-aminosalicylate but not on salicylate (cf. EC 1.14.13.1 salicylate 1-monooxygenase).
Synonyms
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4-aminobenzoate hydroxylase
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oxygenase, 4-aminobenzoate mono-
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4-aminobenzoate + NAD(P)H + H+ + O2 = 4-hydroxyaniline + NAD(P)+ + H2O + CO2
4-aminobenzoate + NAD(P)H + H+ + O2 = 4-hydroxyaniline + NAD(P)+ + H2O + CO2
A-stereospecificity
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4-aminobenzoate + NAD(P)H + H+ + O2 = 4-hydroxyaniline + NAD(P)+ + H2O + CO2
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4-aminobenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
A flavoprotein (FAD). Acts on anthranilate and 4-aminosalicylate but not on salicylate (cf. EC 1.14.13.1 salicylate 1-monooxygenase).
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2-amino-5-chlorobenzoate + NAD(P)H + O2
4-chloro-2-hydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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3,4-diaminobenzoate + NAD(P)H + O2
2-amino-4-hydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: 17.3% of the reaction with 4-aminobenzoate
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3-chloro-4-aminobenzoate + NAD(P)H + H+ + O2
2-chloro-4-hydroxyaniline + NAD(P)+ + H2O + CO2
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Substrates: -
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4-amino-2-chlorobenzoate + NAD(P)H + O2
3-chloro-4-hydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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4-aminobenzoate + NAD(P)H + O2
4-hydroxyaniline + NAD(P)+ + H2O + CO2
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Substrates: -
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4-aminobenzoate + NADH + H+ + O2
4-hydroxyaniline + NAD+ + H2O + CO2
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Substrates: -
r
4-aminosalicylate + NAD(P)H + O2
3,4-dihydroxyaniline + NAD(P)+ + H2O2 + CO2
4-hydroxybenzoate + NAD(P)H + O2
quinol + NAD(P)+ + H2O2 + CO2
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Substrates: 8.4% of the reaction with 4-aminobenzoate
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anthranilate + NAD(P)H + O2
2-hydroxyaniline + NAD(P)+ + H2O2 + CO2
additional information
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4-aminosalicylate + NAD(P)H + O2
3,4-dihydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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4-aminosalicylate + NAD(P)H + O2
3,4-dihydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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anthranilate + NAD(P)H + O2
2-hydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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anthranilate + NAD(P)H + O2
2-hydroxyaniline + NAD(P)+ + H2O2 + CO2
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Substrates: -
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additional information
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Substrates: not: aniline
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additional information
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Substrates: not: 4-aminobenzyl-alcohol
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additional information
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Substrates: several aromatic compounds stimulate NADH oxidation, but no hydroxylated product is formed, all of the O2 consumed is converted to H2O2
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additional information
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Substrates: not: benzoic acid
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additional information
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Substrates: not: salicylate
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FAD
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FAD
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0.91 mol of FAD per mol of enzyme
NADPH
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68% of the activity with NADH
NADPH
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62% of the activity with NADH
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AgNO3
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93% inactivation at 0.1 mM
Br-
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37% inactivation at 0.1 M
Cl-
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30% inactivation at 0.1 M
Cu2+
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severe inhibition at 1 mM
CuSO4
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91% inactivation at 0.1 mM
F-
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20% inactivation at 0.1 M
Fe2+
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slight inhibition at 1 mM
Hg2+
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complete inhibition at 0.1 mM
HgCl2
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92% inactivation at 0.1 mM
I-
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62% inactivation at 0.1 M
NO3-
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45% inactivation at 0.1 M
SCN-
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60% inactivation at 0.1 M
additional information
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amphoteric and anionic detergents cause inactivation
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p-chloromercuribenzoate
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94% inactivation at 0.1 mM
p-chloromercuribenzoate
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complete inhibition at 0.1 mM
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0.0204 - 0.4739
4-Aminobenzoate
0.0204
4-Aminobenzoate
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0.1117
4-Aminobenzoate
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at pH 7
0.4739
4-Aminobenzoate
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at pH 8
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brenda
mushroom
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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Q92402_AGABI
460
1
51021
TrEMBL
Secretory Pathway (Reliability: 3 )
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50950
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calculated from amino acid sequence
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monomer
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1 * 49000, SDS-PAGE
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30
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60 min, little loss of activity in presence of 0.1 mM FAD and 0.02% bovine serum albumin
35
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10 min, 50 mM potassium phosphate buffer, pH 7.0, 0.1 mM FAD, 0.02% bovine serum albumin, stable
40
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10 min, 50 mM potassium phosphate buffer, pH 7.0, 0.1 mM FAD, 0.02% bovine serum albumin, about 70% loss of activity
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10 min, 50 mM potassium phosphate buffer, pH 7.0, 0.1 mM FAD, 0.02% bovine serum albumin, 97% loss of activity
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10 min, 50 mM potassium phosphate buffer, pH 7.0, 0.1 mM FAD, 0.02% bovine serum albumin, 98% loss of activity
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-20°C, 10 mM potassium phosphate buffer, pH 7.0, 20% glycerol, 6 months, stable
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-20°C, 50 mM potassium phosphate buffer, pH 7.0, 20% glycerol, 1 mM 2-mercaptoethanol, 0.01 mM FAD, stable for 1 month
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DNA fragments encoding various partial amino acid sequences of the enzyme
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fusion protein with glutathione-S-transferase
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Tsuji, H.; Ogawa, T.; Bando, N.; Sasaoka, K.
Purification and properties of 4-aminobenzoate hydroxylase, a new monooxygenase from Agaricus bisporus
J. Biol. Chem.
261
13203-13209
1986
Agaricus bisporus
brenda
Tsuji, H.; Ogawa, T.; Bando, N.; Sasaoka, K.
Stereospecificity of NAD(P)H oxidation catalyzed by 4-aminobenzoate hydroxylase from Agaricus bisporus
Biochim. Biophys. Acta
991
380-382
1989
Agaricus bisporus
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brenda
Tsuji, H.; Ogawa, T.; Bando, N.; Sasaoka, K.
A unique enzyme catalyzing the formation of 4-hydroxyaniline from 4-amino-benzoic acid in Agaricus bisporus
Biochem. Biophys. Res. Commun.
130
633-639
1985
Agaricus bisporus
brenda
Mizutani, Y.; Narikawa, T.; Satoh, T.; Sakurai, N.; Kaji, H.; Yamada, S.; Samejima, T.
A new UV method for serum gamma-glutamyltransferase assay using recombinant 4-aminobenzoate hydroxylase as a coupling enzyme
J. Biochem.
126
347-353
1999
Agaricus bisporus
brenda
Tsuji, H.; Kimoto, M.; Watanabe, H.; Sasagawa, T.; Oka, T.; Yamashita, H.; Okita, M.
Epitope mapping of monoclonal antibodies against 4-aminobenzoate hydroxylase from Agaricus bisporus
Biochim. Biophys. Acta
1425
628-631
1998
Agaricus bisporus
brenda
Tsuji, H.; Oka, T.; Kimoto, M.; Hong, Y.M.; Natori, Y.; Ogawa, T.
Cloning and sequencing of cDNA encoding 4-aminobenzoate hydroxylase from Agaricus bisporus
Biochim. Biophys. Acta
1309
31-36
1996
Agaricus bisporus
brenda
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