Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,3,4-trihydroxybenzoate + NADH + H+ + O2
2,3,4,6-tetrahydroxybenzoate + NAD+ + H2O
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + H+ + O2
2,3,6-trihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+ + O2
?
-
very poor substrate
-
-
?
3,4-dihydroxybenzoate + NADH + O2
2,4,5-trihydroxybenzoate + NAD+ + H2O
3,5-dihydroxybenzoate + NADH + H+ + O2
2,3,5,6-tetrahydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3,5-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
3-aminobenzoate + NAD(P)H + O2
?
3-bromobenzoate + NAD(P)H + O2
?
3-chlorobenzoate + NAD(P)H + O2
?
-
-
-
?
3-fluorobenzoate + NAD(P)H + O2
?
-
-
-
?
3-hydroxy-3-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-3-methylbenzoate + NAD(P)+ + H2O
-
-
-
?
3-hydroxy-4-aminobenzoate + NADH + H+ + O2
4-amino-2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxy-4-methoxybenzoate + NADH + H+ + O2
4-methoxy-2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxy-4-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-4-methylbenzoate + NAD(P)+ + H2O
the substrate is an intermediate in the degradation of 2,5-xylenol, higher activity with the recombinant His-tagged enzyme compared to the native enzyme
-
-
?
3-hydroxy-4-methylbenzoate + NADH + H+ + O2
4-methyl-2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxy-5-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-3-methylbenzoate + NAD(P)+ + H2O
the substrate is an intermediate in the degradation of 3,5-xylenol, higher activity with the recombinant His-tagged enzyme compared to the native enzyme, preferred substrate
-
-
?
3-hydroxy-5-methylbenzoate + NADH + O2
2,5-dihydroxy-3-methylbenzoate + NAD+ + H2O
3-hydroxybenzoate + NAD(P)H + H+ + O2
gentisate + NAD(P)+ + H2O
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
3-methylthiobenzoate + NAD(P)H + O2
?
-
-
-
?
4-fluoro-3-hydroxybenzoate + NADH + O2
4-fluoro-2,5-dihydroxybenzoate + NAD+ + H2O
-
36% of the reaction with 3-hydroxybenzoate
-
?
additional information
?
-
2,3-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
-
10.5% of the reaction with 3-hydroxybenzoate
-
?
2,3-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
-
10.5% of the reaction with 3-hydroxybenzoate
-
?
3,4-dihydroxybenzoate + NADH + O2
2,4,5-trihydroxybenzoate + NAD+ + H2O
-
9% of the reaction with 3-hydroxybenzoate
-
?
3,4-dihydroxybenzoate + NADH + O2
2,4,5-trihydroxybenzoate + NAD+ + H2O
-
9% of the reaction with 3-hydroxybenzoate
-
?
3,5-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
-
7% of the reaction with 3-hydroxybenzoate
-
?
3,5-dihydroxybenzoate + NADH + O2
2,3,5-trihydroxybenzoate + NAD+ + H2O
-
7% of the reaction with 3-hydroxybenzoate
-
?
3-aminobenzoate + NAD(P)H + O2
?
-
-
-
?
3-aminobenzoate + NAD(P)H + O2
?
-
-
-
?
3-bromobenzoate + NAD(P)H + O2
?
-
-
-
?
3-bromobenzoate + NAD(P)H + O2
?
-
-
-
?
3-hydroxy-5-methylbenzoate + NADH + O2
2,5-dihydroxy-3-methylbenzoate + NAD+ + H2O
-
31% of the reaction with 3-hydroxybenzoate
-
?
3-hydroxy-5-methylbenzoate + NADH + O2
2,5-dihydroxy-3-methylbenzoate + NAD+ + H2O
-
31% of the reaction with 3-hydroxybenzoate
-
?
3-hydroxybenzoate + NAD(P)H + H+ + O2
gentisate + NAD(P)+ + H2O
-
-
i.e. 2,5-dihydroxybenzoate
-
?
3-hydroxybenzoate + NAD(P)H + H+ + O2
gentisate + NAD(P)+ + H2O
-
the small catabolic gene cluster nagR2-orf2I''KL in strain CJ2 may be multifunctional and is essential for the degradation of 3-hydroxybenzoate
i.e. 2,5-dihydroxybenzoate
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
the enzyme is involved in the degradation of 2,5-xylenol and 3,5-xylenol via the gentisate pathway, overview
-
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
the enzyme is involved in the degradation of 2,5-xylenol and 3,5-xylenol via the gentisate pathway, overview
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
the enzyme clearly prefers NADH as external electron donor over NADPH
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
NarX shows activity on 3-hydroxybenzoate rather than on salicylate
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
NarX shows activity on 3-hydroxybenzoate rather than on salicylate
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
strictly specific for 3-hydroxybenzoate
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
key role in metabolism of aromatic compounds
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
r
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
the enzyme clearly prefers NADH as external electron donor over NADPH
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
additional information
?
-
-
not: salicylate
-
-
?
additional information
?
-
-
acts also on a number of analogs of 3-hydroxybenzoate substituted in the 2, 3, 5 and 6 positions
-
-
?
additional information
?
-
-
not: p-hydroxybenzoate
-
-
?
additional information
?
-
-
the enzyme shows no salicylate 5-hydroxylase activity
-
-
?
additional information
?
-
degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
-
-
?
additional information
?
-
degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
-
-
?
additional information
?
-
-
no activity with 2,5-dihydroxybenzoate
-
-
?
additional information
?
-
the purified H6-NarX protein shows no detectable activity against the 3HBA structural analogues, including 2-hydroxybenzoate, i.e. salicylate, 4-hydroxybenzoate, or 4-substituted derivatives (4-CH3, 4-NH2, and 4-NO2) of 3-hydroxybenzoate
-
-
?
additional information
?
-
-
the purified H6-NarX protein shows no detectable activity against the 3HBA structural analogues, including 2-hydroxybenzoate, i.e. salicylate, 4-hydroxybenzoate, or 4-substituted derivatives (4-CH3, 4-NH2, and 4-NO2) of 3-hydroxybenzoate
-
-
?
additional information
?
-
the purified H6-NarX protein shows no detectable activity against the 3HBA structural analogues, including 2-hydroxybenzoate, i.e. salicylate, 4-hydroxybenzoate, or 4-substituted derivatives (4-CH3, 4-NH2, and 4-NO2) of 3-hydroxybenzoate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxybenzoate + NAD(P)H + H+ + O2
gentisate + NAD(P)+ + H2O
-
the small catabolic gene cluster nagR2-orf2I''KL in strain CJ2 may be multifunctional and is essential for the degradation of 3-hydroxybenzoate
i.e. 2,5-dihydroxybenzoate
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
additional information
?
-
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
the enzyme is involved in the degradation of 2,5-xylenol and 3,5-xylenol via the gentisate pathway, overview
-
-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
the enzyme is involved in the degradation of 2,5-xylenol and 3,5-xylenol via the gentisate pathway, overview
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
the enzyme clearly prefers NADH as external electron donor over NADPH
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
NarX shows activity on 3-hydroxybenzoate rather than on salicylate
-
-
?
3-hydroxybenzoate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
NarX shows activity on 3-hydroxybenzoate rather than on salicylate
-
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
key role in metabolism of aromatic compounds
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
i.e. gentisate
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
3-hydroxybenzoate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
additional information
?
-
degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
-
-
?
additional information
?
-
degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.051
2,3-Dihydroxybenzoate
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.14
2,5-Dihydroxybenzoate
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.25
3,5-Dihydroxybenzoate
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.071 - 0.095
3-hydroxy-4-methylbenzoate
0.027 - 0.19
3-hydroxybenzoate
additional information
additional information
-
0.071
3-hydroxy-4-methylbenzoate
pH 7.5, 23°C, recombinant enzyme, cofactor NADPH
0.095
3-hydroxy-4-methylbenzoate
pH 7.5, 23°C, recombinant enzyme, cofactor NADH
0.027
3-hydroxybenzoate
wild type enzyme, at pH 8.0 and 25°C
0.038
3-hydroxybenzoate
-
pH 8.0, 30°C, mutant A308G
0.046
3-hydroxybenzoate
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.046
3-hydroxybenzoate
pH 8, 25°C, native enzyme
0.0463
3-hydroxybenzoate
-
pH 8.0, 30°C, mutant Y306H
0.0534
3-hydroxybenzoate
recombinant enzyme, with NADH, pH 7.5, 25°C
0.063
3-hydroxybenzoate
-
cosubstrate NADH
0.065
3-hydroxybenzoate
-
pH 8.0, 30°C, recombinant NagX, with NADH
0.0726
3-hydroxybenzoate
-
pH 8.0, 30°C, recombinant wild-type enzyme
0.079
3-hydroxybenzoate
pH 7.5, 23°C, recombinant enzyme, cofactor NADH
0.0913
3-hydroxybenzoate
-
pH 8.0, 30°C, mutant Q305P
0.108
3-hydroxybenzoate
pH 7.5, 23°C, recombinant enzyme, cofactor NADPH
0.142
3-hydroxybenzoate
pH 8, 25°C, enzyme immobilized onto surface-functionalized electrospun polycaprolactone (PCL) fibers
0.162
3-hydroxybenzoate
-
cosubstrate NADH
0.1642
3-hydroxybenzoate
-
pH 8.0, 30°C, mutant Y221F
0.168
3-hydroxybenzoate
-
cosubstrate NADPH
0.186
3-hydroxybenzoate
mutant enzyme Y105F, at pH 8.0 and 25°C
0.19
3-hydroxybenzoate
-
-
0.0337
NADH
-
pH 8.0, 30°C, mutant A308G
0.04
NADH
-
cosubstrate 3-hydroxybenzoate
0.048
NADH
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.0867
NADH
-
pH 8.0, 30°C, mutant Y221F
0.0959
NADH
-
pH 8.0, 30°C, mutant Q305P
0.1037
NADH
-
pH 8.0, 30°C, mutant Y306H
0.1041
NADH
-
pH 8.0, 30°C, recombinant enzyme
0.493
NADH
-
pH 8.0, 30°C, recombinant NagX
2.5
NADH
pH 8, 25°C, native enzyme
0.064
NADPH
-
cosubstrate 3-hydroxybenzoate
0.39
NADPH
-
in 50 mM Tris-SO4 (pH 8.0), at 25°C
0.86
NADPH
-
pH 8.0, 30°C, recombinant NagX
additional information
additional information
-
Km at various pH values
-
additional information
additional information
-
purified 3HB6H displays typical Michaelis-Menten kinetics, Lineweaver-Burk plots
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
You, K.S.; Arnold, L.J.; Kaplan, N.O.
The stereospecificity of bacterial external flavoprotein monooxygenases for nicotinamide adenine dinucleotide
Arch. Biochem. Biophys.
180
550-554
1977
Pseudomonas aeruginosa, Pseudomonas aeruginosa T1
brenda
Groseclose, E.E.; Ribbons, D.W.
3-Hydroxybenzoate 6-hydroxylase from Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
55
897-903
1973
Pseudomonas aeruginosa, Pseudomonas aeruginosa T1
brenda
Wang, L.H.; Hamzah, R.Y.; Yu, Y.; Tu, S.C.
Pseudomonas cepacia 3-hydroxybenzoate 6-hydroxylase: induction, purification, and characterization
Biochemistry
26
1099-1104
1987
Burkholderia cepacia
brenda
Yu, Y.; Wang, L.H.; Tu, S.C.
Pseudomonas cepacia 3-hydroxybenzoate 6-hydroxylase: stereochemistry, isotope effects, and kinetic mechanism
Biochemistry
26
1105-1110
1987
Burkholderia cepacia
brenda
Rajasekharan, S.; Rajasekharan, R.; Vaidyanathan, C.S.
Substrate-mediated purification and characterization of a 3-hydroxybenzoic acid-6-hydroxylase from Micrococcus
Arch. Biochem. Biophys.
278
21-25
1990
Micrococcus sp.
brenda
Suarez, M.; Ferrer, E.; Garrido-Pertierra, A.; Martin, M.
Purification and characterization of the 3-hydroxybenzoate-6-hydroxylase from Klebsiella pneumoniae
FEMS Microbiol. Lett.
126
283-290
1995
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
brenda
Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
Physicochemical and immunochemical characterization of salicylate 5-hydroxylase, m-hydroxybenzoate 6-hydroxylase and p-hydroxybenzoate 3-hydroxylase from Rhodococcus erythropolis
Biotechnol. Lett.
17
1063-1068
1995
Rhodococcus erythropolis, Rhodococcus erythropolis S1
-
brenda
Sumathi, S.; Dasgupta, D.; Vaidyanathan, C.S.
Chemical modification of 3-HBA-6-hydroxylase by phenylglyoxal: kinetic and physicochemical studies on the modified enzyme
Indian J. Biochem. Biophys.
35
266-272
1998
Micrococcus sp.
brenda
Sumathi, S.; Dasgupta, D.
Reactivity of 3-HBA-6-hydroxylase with diethylpyrocarbonate and N-bromosuccinimide: Effect of chemical modifications on kinetic and spectral properties of the enzyme
Biotechnol. Prog.
16
577-582
2000
Micrococcus sp.
brenda
Suresh, S.; Dasgupta, D.
Interaction of 3-hydroxybenzoate with 3-hydroxybenzoate-6-hydroxylase
Biotechnol. Prog.
17
1026-1031
2001
Micrococcus sp.
brenda
Liu, D.Q.; Liu, H.; Gao, X.L.; Leak, D.J.; Zhou, N.Y.
Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1
Microbiol. Res.
160
53-59
2005
Klebsiella oxytoca (Q5EXK1)
brenda
Gao, X.; Tan, C.L.; Yeo, C.C.; Poh, C.L.
Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867
J. Bacteriol.
187
7696-7702
2005
Pseudomonas alcaligenes (Q9F131), Pseudomonas alcaligenes P25X (Q9F131)
brenda
Park, M.; Jeon, Y.; Jang, H.H.; Ro, H.S.; Park, W.; Madsen, E.L.; Jeon, C.O.
Molecular and biochemical characterization of 3-hydroxybenzoate 6-hydroxylase from Polaromonas naphthalenivorans CJ2
Appl. Environ. Microbiol.
73
5146-5152
2007
Polaromonas naphthalenivorans
brenda
Liu, T.T.; Xu, Y.; Liu, H.; Luo, S.; Yin, Y.J.; Liu, S.J.; Zhou, N.Y.
Functional characterization of a gene cluster involved in gentisate catabolism in Rhodococcus sp. strain NCIMB 12038
Appl. Microbiol. Biotechnol.
90
671-678
2010
Rhodococcus sp. (E7CYP8), Rhodococcus sp., Rhodococcus sp. NCIMB 12038 (E7CYP8)
brenda
Yang, Y.F.; Zhang, J.J.; Wang, S.H.; Zhou, N.Y.
Purification and characterization of the ncgl2923-encoded 3-hydroxybenzoate 6-hydroxylase from Corynebacterium glutamicum
J. Basic Microbiol.
50
599-604
2010
Corynebacterium glutamicum (Q8NLB6), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q8NLB6), Corynebacterium glutamicum ATCC 13032
brenda
Sucharitakul, J.; Wongnate, T.; Montersino, S.; van Berkel, W.J.; Chaiyen, P.
Reduction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1
Biochemistry
51
4309-4321
2012
Rhodococcus jostii
brenda
Montersino, S.; van Berkel, W.J.
Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1
Biochim. Biophys. Acta
1824
433-442
2012
Rhodococcus jostii
brenda
Montersino, S.; Orru, R.; Barendregt, A.; Westphal, A.H.; van Duijn, E.; Mattevi, A.; van Berkel, W.J.
Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid-assisted flavoprotein strategy for regioselective aromatic hydroxylation
J. Biol. Chem.
288
26235-26245
2013
Rhodococcus jostii (Q0SFK6)
brenda
Sucharitakul, J.; Tongsook, C.; Pakotiprapha, D.; van Berkel, W.J.; Chaiyen, P.
The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodoccocus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle
J. Biol. Chem.
288
35210-35221
2013
Rhodococcus jostii
brenda
Holesova, Z.; Jakubkova, M.; Zavadiakova, I.; Zeman, I.; Tomaska, L.; Nosek, J.
Gentisate and 3-oxoadipate pathways in the yeast Candida parapsilosis: identification and functional analysis of the genes coding for 3-hydroxybenzoate 6-hydroxylase and 4-hydroxybenzoate 1-hydroxylase
Microbiology
157
2152-2163
2011
Candida parapsilosis, Candida parapsilosis CDU1
brenda
Sucharitakul, J.; Medhanavyn, D.; Pakotiprapha, D.; van Berkel, W.J.; Chaiyen, P.
Tyr217 and His213 are important for substrate binding and hydroxylation of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1
FEBS J.
283
860-881
2016
Rhodococcus jostii (Q0SFK6)
brenda
Montersino, S.; Te Poele, E.; Orru, R.; Westphal, A.H.; Barendregt, A.; Heck, A.J.R.; van der Geize, R.; Dijkhuizen, L.; Mattevi, A.; van Berkel, W.J.H.
3-Hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 contains a phosphatidylinositol cofactor
Front. Microbiol.
8
1110
2017
Rhodococcus jostii (Q0SFK6), Rhodococcus jostii
brenda
Srisook, T.; Vongsetskul, T.; Sucharitakul, J.; Chaiyen, P.; Tangboriboonrat, P.
Immobilization of 3-hydroxybenzoate 6-hydroxylase onto functionalized electrospun polycaprolactone ultrafine fibers A novel heterogeneous catalyst
React. Funct. Polym.
82
41-46
2014
Rhodococcus jostii (Q0SFK6)
-
brenda
Westphal, A.H.; Tischler, D.; van Berkel, W.J.H.
Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases
Arch. Biochem. Biophys.
702
108820
2021
Rhodococcus jostii
brenda
Chen, X.; Tang, H.; Liu, Y.; Xu, P.; Xue, Y.; Lin, K.; Cui, C.
Purification and initial characterization of 3-hydroxybenzoate 6-hydroxylase from a halophilic Martelella strain AD-3
Front. Microbiol.
9
1335
2018
Martelella sp. AD-3
brenda