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1,4-dihydroxy-2-naphthoate + O2
?
1-hydroxy-2-naphthoate + O2
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
3,4-dichlorosalicylate + O2
?
3,4-dimethylgentisate + O2
?
3,5-dibromosalicylate + O2
?
3,6-dichlorogentisate + O2
?
3-aminosalicylate + O2
(2E,4Z)-2-amino-6-oxohepta-2,4-dienoate
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
3-bromosalicylate + O2
(2E,4Z)-2-bromo-6-oxohepta-2,4-dienoate
low activity
-
-
?
3-bromosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-chlorogentisate + O2
3-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
3-chlorosalicylate + O2
(2E,4Z)-2-chloro-6-oxohepta-2,4-dienoate
low activity
-
-
?
3-chlorosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
3-hydroxysalicylate + O2
(2E,4Z)-2-hydroxy-6-oxohepta-2,4-dienoate
low activity
-
-
?
3-hydroxysalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-isopropyl-gentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
3-isopropylgentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
3-methylgentisate + O2
3-methyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax is 10.1% of Vmax for gentisate
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
3-methylsalicylate + O2
(2Z,4Z)-2-methyl-6-oxohepta-2,4-dienoate
low activity
-
-
?
3-methylsalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-O-methylgentisate + O2
?
4-aminosalicylate + O2
(2Z,4E)-3-amino-6-oxohepta-2,4-dienoate
-
-
-
?
4-bromosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
4-chlorosalicylate + O2
(2Z,4E)-3-chloro-6-oxohepta-2,4-dienoate
low activity
-
-
?
4-chlorosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
4-fluorogentisate + O2
2-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
4-hydroxysalicylate + O2
(2Z,4E)-3-hydroxy-6-oxohepta-2,4-dienoate
low activity
-
-
?
4-hydroxysalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
4-isopropylgentisate + O2
4-hydroxy-2-isopropyl-6-oxo-hepta-2,4-dienedioic acid
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
4-methylsalicylate + O2
(2Z,4Z)-3-methyl-6-oxohepta-2,4-dienoate
low activity
-
-
?
4-methylsalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
4-O-methylgentisate + O2
?
5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
5-bromosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
5-chlorosalicylate + O2
(2Z,4E)-4-chloro-6-oxohepta-2,4-dienoate
low activity
-
-
?
5-chlorosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
5-fluorosalicylate + O2
(2Z,4E)-4-fluoro-6-oxohepta-2,4-dienoate
low activity
-
-
?
5-fluorosalicylate + O2
?
5-methylsalicylate + O2
(2Z,4Z)-4-methyl-6-oxohepta-2,4-dienoate
low activity
-
-
?
5-methylsalicylate + O2
?
benzoate + O2
3-hydroxy-6-oxoheptadienoic acid
-
-
-
-
?
cinnamate + O2
?
-
-
-
-
?
gentisate + O2
maleylpyruvate
phenylpropionate + O2
?
-
-
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
salicylate + O2
?
-
-
-
-
?
additional information
?
-
1,4-dihydroxy-2-naphthoate + O2
?
-
-
-
-
?
1,4-dihydroxy-2-naphthoate + O2
?
-
-
-
-
?
1,4-dihydroxy-2-naphthoate + O2
?
-
-
-
?
1,4-dihydroxy-2-naphthoate + O2
?
-
-
-
?
1-hydroxy-2-naphthoate + O2
?
-
-
-
-
?
1-hydroxy-2-naphthoate + O2
?
-
-
-
-
?
1-hydroxy-2-naphthoate + O2
?
weak activity
-
-
?
1-hydroxy-2-naphthoate + O2
?
weak activity
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
the enzyme is highly specific for 2,5-dihydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
the enzyme is highly specific for 2,5-dihydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
the enzyme is involbved in the 3-phenylpropionic acid deg´radation pathway
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
ir
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
ir
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
i.e. gentisate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
i.e. gentisate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
i.e. gentisate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
i.e. gentisate
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
i.e. gentisic acid
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
ir
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
ir
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
ir
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
narrow substrate specificity
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
narrow substrate specificity
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-dihydroxybenzoate + O2
maleylpyruvate
-
-
-
?
2,5-xylenol + O2
?
-
-
-
-
?
2,5-xylenol + O2
?
-
-
-
-
?
3,4-dichlorosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3,4-dichlorosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3,4-dimethylgentisate + O2
?
-
-
-
-
?
3,4-dimethylgentisate + O2
?
-
-
-
-
?
3,5-dibromosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3,5-dibromosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3,6-dichlorogentisate + O2
?
-
-
-
-
?
3,6-dichlorogentisate + O2
?
-
-
-
-
?
3-aminosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-aminosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax is 48.5% of Vmax for gentisate
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-bromogentisate + O2
3-bromo-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-chlorogentisate + O2
3-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-chlorogentisate + O2
3-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-chlorogentisate + O2
3-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax is 39.7% of Vmax for gentisate
-
-
?
3-ethylgentisate + O2
3-ethyl-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax is 39.7% of Vmax for gentisate
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax of recombinant enzyme is 20.5% higher compared to gentisate
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-fluorogentisate + O2
3-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
Vmax of recombinant enzyme is 20.5% higher compared to gentisate
-
-
?
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
-
minor pathway
-
-
?
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
-
main pathway
-
-
?
3-hydroxybenzoate + O2
3,4-dihydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-hydroxybenzoate + O2
?
-
-
-
-
?
3-hydroxybenzoate + O2
?
-
-
-
-
?
3-isopropyl-gentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropyl-gentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropyl-gentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropyl-gentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropylgentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropylgentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropylgentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-isopropylgentisate + O2
4-hydroxy-3-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
Vmax is 57.1% of Vmax for gentisate
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-methylgentisate + O2
4-hydroxy-3-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
3-O-methylgentisate + O2
?
-
-
-
-
?
3-O-methylgentisate + O2
?
-
-
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-chlorogentisate + O2
2-chloro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-fluorogentisate + O2
2-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-fluorogentisate + O2
2-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-fluorogentisate + O2
2-fluoro-4-hydroxy-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-hydroxybenzoate + O2
?
-
-
-
-
?
4-hydroxybenzoate + O2
?
-
-
-
-
?
4-isopropylgentisate + O2
4-hydroxy-2-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-isopropylgentisate + O2
4-hydroxy-2-isopropyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-methylgentisate + O2
4-hydroxy-2-methyl-6-oxo-hepta-2,4-dienedioic acid
-
-
-
-
?
4-O-methylgentisate + O2
?
-
-
-
-
?
4-O-methylgentisate + O2
?
-
-
-
-
?
5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
-
-
-
?
5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
-
-
-
?
5-aminosalicylate + O2
?
-
-
-
?
5-aminosalicylate + O2
?
-
-
-
?
5-aminosalicylate + O2
?
-
-
-
-
?
5-aminosalicylate + O2
?
-
a gentisate 1,2-dioxygenase with an extremely relaxed substrate specificity is responsible for the unusual oxidation of salicylate by Pseudoaminobacter salicylatoxidans BN12. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
5-aminosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
5-aminosalicylate + O2
?
-
-
-
-
?
5-aminosalicylate + O2
?
-
a gentisate 1,2-dioxygenase with an extremely relaxed substrate specificity is responsible for the unusual oxidation of salicylate by Pseudoaminobacter salicylatoxidans BN12. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
5-aminosalicylate + O2
?
-
kcat/KM is less than 1% of the kcat/Km for gentisate
-
-
?
5-aminosalicylate + O2
?
partly preferred substrate
-
-
?
5-aminosalicylate + O2
?
partly preferred substrate
-
-
?
5-fluorosalicylate + O2
?
-
-
-
?
5-fluorosalicylate + O2
?
-
-
-
?
5-fluorosalicylate + O2
?
-
-
-
-
?
5-fluorosalicylate + O2
?
-
kcat/KM is 1.4% of the kcat/Km for gentisate
-
-
?
5-fluorosalicylate + O2
?
-
-
-
-
?
5-methylsalicylate + O2
?
-
-
-
-
?
5-methylsalicylate + O2
?
-
kcat/KM is 1.5% of the kcat/Km for gentisate
-
-
?
gentisate + O2
?
-
-
-
-
?
gentisate + O2
?
-
-
-
-
?
gentisate + O2
?
-
-
-
-
?
gentisate + O2
?
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
preferred substrate
-
-
?
gentisate + O2
maleylpyruvate
-
gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
gentisate + O2
maleylpyruvate
-
preferred substrate
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
gentisate + O2
maleylpyruvate
-
-
-
-
?
lactate + O2
?
-
-
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
-
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
a gentisate 1,2-dioxygenase with an extremely relaxed substrate specificity is responsible for the unusual oxidation of salicylate by Pseudoaminobacter salicylatoxidans BN12. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
kcat/KM is 6.6% of the kcat/Km for gentisate
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
a gentisate 1,2-dioxygenase with an extremely relaxed substrate specificity is responsible for the unusual oxidation of salicylate by Pseudoaminobacter salicylatoxidans BN12. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
-
-
-
?
salicylate + O2
2-oxohepta-3,5-dienedioic acid
-
-
-
?
additional information
?
-
no activity with salicylate, 3-methylsalicylate, 4-methylsalicylate, 5-methylsalicylate, 3-bromosalicylate, 4-bromosalicylate, 5-iodosalicylate, and 1-hydroxy-2-naphthoate
-
-
?
additional information
?
-
-
no activity with salicylate, 3-methylsalicylate, 4-methylsalicylate, 5-methylsalicylate, 3-bromosalicylate, 4-bromosalicylate, 5-iodosalicylate, and 1-hydroxy-2-naphthoate
-
-
?
additional information
?
-
no activity with salicylate, 3-methylsalicylate, 4-methylsalicylate, 5-methylsalicylate, 3-bromosalicylate, 4-bromosalicylate, 5-iodosalicylate, and 1-hydroxy-2-naphthoate
-
-
?
additional information
?
-
-
broad substrate specificity
-
-
?
additional information
?
-
methyl 2,5-dihydroxybenzoate, 1,4-benzoquinone, 2,5-dihydroxybenzaldehyde, 4,5-dihydroxy-1,3-benzene-disulphonic acid and 2,3,5,6-tetrachloro-1,4-benzenediol give no substrate activity
-
-
?
additional information
?
-
-
methyl 2,5-dihydroxybenzoate, 1,4-benzoquinone, 2,5-dihydroxybenzaldehyde, 4,5-dihydroxy-1,3-benzene-disulphonic acid and 2,3,5,6-tetrachloro-1,4-benzenediol give no substrate activity
-
-
?
additional information
?
-
-
benzoate does not serve as substrate
-
-
?
additional information
?
-
-
benzoate does not serve as substrate
-
-
?
additional information
?
-
-
broad substrate specificity
-
-
?
additional information
?
-
-
no activity with: 6-methylgentisate, 3,4-dimethylgentisate
-
-
?
additional information
?
-
-
the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans strain BN12 is a versatile gentisate 1,2-dioxygenase that converts both gentisate (2,5-dihydroxybenzoate) and various monohydroxylated substrates
-
-
?
additional information
?
-
the purified enzyme is able to convert various salicylates that carried methyl-, fluoro-, chloro-, bromo-, or iodo-substituents in the 3-, 4-, or 5-position, although in general with much lower specific activities than observed with 5-amino- or 5-hydroxysalicylate. No activity with 6-hydroxysalicylate, 5-carboxysalicylate, 5-sulfosalicylate, 5-nitrosalicylate, 3,5-dibromosalicylate, 3,5-diiodosalicylate, or 3,4-dihydroxysalicylate
-
-
?
additional information
?
-
-
the purified enzyme is able to convert various salicylates that carried methyl-, fluoro-, chloro-, bromo-, or iodo-substituents in the 3-, 4-, or 5-position, although in general with much lower specific activities than observed with 5-amino- or 5-hydroxysalicylate. No activity with 6-hydroxysalicylate, 5-carboxysalicylate, 5-sulfosalicylate, 5-nitrosalicylate, 3,5-dibromosalicylate, 3,5-diiodosalicylate, or 3,4-dihydroxysalicylate
-
-
?
additional information
?
-
-
the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans strain BN12 is a versatile gentisate 1,2-dioxygenase that converts both gentisate (2,5-dihydroxybenzoate) and various monohydroxylated substrates
-
-
?
additional information
?
-
the purified enzyme is able to convert various salicylates that carried methyl-, fluoro-, chloro-, bromo-, or iodo-substituents in the 3-, 4-, or 5-position, although in general with much lower specific activities than observed with 5-amino- or 5-hydroxysalicylate. No activity with 6-hydroxysalicylate, 5-carboxysalicylate, 5-sulfosalicylate, 5-nitrosalicylate, 3,5-dibromosalicylate, 3,5-diiodosalicylate, or 3,4-dihydroxysalicylate
-
-
?
additional information
?
-
-
GDO-II is strictly inducible by aromatic substrates such as 3-hydroxybenzoate and gentisate
-
-
?
additional information
?
-
-
GDO-II is unable to utilize gentisate that is substituted at the carbon-4 position (i.e., 4-chloro- and 4-methylgentisate)
-
-
?
additional information
?
-
-
GDO-II is strictly inducible by aromatic substrates such as 3-hydroxybenzoate and gentisate
-
-
?
additional information
?
-
-
GDO-II is unable to utilize gentisate that is substituted at the carbon-4 position (i.e., 4-chloro- and 4-methylgentisate)
-
-
?
additional information
?
-
-
no activity with 3,6-dichlorogentisate or 6-chlorogentisate
-
-
-
additional information
?
-
-
no activity with 3,6-dichlorogentisate or 6-chlorogentisate
-
-
-
additional information
?
-
no activity against catechol, benzoate, 5-methylsalicylate, 5-chlorosalicylate, and homogentisate
-
-
?
additional information
?
-
no activity against catechol, benzoate, 5-methylsalicylate, 5-chlorosalicylate, and homogentisate
-
-
?
additional information
?
-
-
no activity against catechol, benzoate, 5-methylsalicylate, 5-chlorosalicylate, and homogentisate
-
-
?
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A112D
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112I
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112S
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112D
-
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
-
A112G
-
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
-
A112I
-
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
-
A112S
-
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
-
H108D
-
complete loss of activity
H110D
-
complete loss of activity
H118D
-
complete loss of activity
H120D
-
complete loss of activity
H149D
-
complete loss of activity
H151D
-
complete loss of activity
H159D
-
complete loss of activity
H161D
-
complete loss of activity
H108D
-
complete loss of activity
-
H110D
-
complete loss of activity
-
H149D
-
complete loss of activity
-
H151D
-
complete loss of activity
-
H161D
-
complete loss of activity
-
F159Y
-
site-directed mutagenesis
G106A
-
site-directed mutagenesis, in contrast to the wild-type enzyme, mutant G106A oxidizes only gentisate, while 1-hydroxy-2-naphthoate and salicylate are not converted. The mutant shows slightly decreased activity with salicylate, but shows a higher affinity to this substratecompared to the wild-type. Salicylate is coordinated in the G106A variant with the catalytically active Fe(II) ion in an unusual and unproductive manner because of the inability of salicylate to displace a hydrogen bond that is formed between Trp104 and Asp174 in the G106A variant
G111A
-
site-directed mutagenesis
M103L
-
site-directed mutagenesis
R113G
-
site-directed mutagenesis
S147R
-
site-directed mutagenesis
G106A
-
site-directed mutagenesis, in contrast to the wild-type enzyme, mutant G106A oxidizes only gentisate, while 1-hydroxy-2-naphthoate and salicylate are not converted. The mutant shows slightly decreased activity with salicylate, but shows a higher affinity to this substratecompared to the wild-type. Salicylate is coordinated in the G106A variant with the catalytically active Fe(II) ion in an unusual and unproductive manner because of the inability of salicylate to displace a hydrogen bond that is formed between Trp104 and Asp174 in the G106A variant
-
G111A
-
site-directed mutagenesis
-
M103L
-
site-directed mutagenesis
-
R113G
-
site-directed mutagenesis
-
S147R
-
site-directed mutagenesis
-
D120K
-
complete loss of activity
E223A
-
102% relative activity compared to the wild type enzyme
G123N
-
75% relative activity compared to the wild type enzyme
G164T
-
complete loss of activity
H108D
-
no enzymatic activity
H110D
-
no enzymatic activity
H149D
-
no enzymatic activity
H151D
-
no enzymatic activity
K338Y
-
156% relative activity compared to the wild type enzyme
M146T
-
complete loss of activity
M169T
-
complete loss of activity
N153H
-
183% relative activity compared to the wild type enzyme
N43T
-
317% relative activity compared to the wild type enzyme
S113P
-
complete loss of activity
T260C
-
complete loss of activity
V326Q
-
complete loss of activity
V36A
-
complete loss of activity
Y17C
-
161% relative activity compared to the wild type enzyme
Y181D
-
68% relative activity compared to the wild type enzyme
Y181F
-
mutant demonstrates 4-, 3-, 6-, and 16fold increase in relative activity towards 2,5-dihydroxybenzoate, 3-fluoro-, 4-methyl-, and 3-methylgentisate, respectively, and shows 464% relative activity compared to the wild type enzyme for 2,5-dihydroxybenzoate
Y181H
-
98% relative activity compared to the wild type enzyme
Y284I
-
260% relative activity compared to the wild type enzyme
D120K
-
complete loss of activity
-
G123N
-
75% relative activity compared to the wild type enzyme
-
N43T
-
317% relative activity compared to the wild type enzyme
-
Y17C
-
161% relative activity compared to the wild type enzyme
-
Y181F
-
mutant demonstrates 4-, 3-, 6-, and 16fold increase in relative activity towards 2,5-dihydroxybenzoate, 3-fluoro-, 4-methyl-, and 3-methylgentisate, respectively, and shows 464% relative activity compared to the wild type enzyme for 2,5-dihydroxybenzoate
-
H108D
-
complete loss of activity
H110D
-
complete loss of activity
H118D
-
complete loss of activity
H120D
-
complete loss of activity
H149D
-
complete loss of activity
H151D
-
complete loss of activity
H159D
-
complete loss of activity
H161D
-
complete loss of activity
H108D
-
complete loss of activity
-
H110D
-
complete loss of activity
-
H149D
-
complete loss of activity
-
H151D
-
complete loss of activity
-
H161D
-
complete loss of activity
-
D175N
inactive mutant enzyme
D225N
activity is comparable to wild-type activity
E47Q
activity is comparable to wild-type activity
H119A/H121A
despite its wild-type like structural propertie, the mutant shows extremely low gentisate 1,2-dioxygenase activity
H290A/H292A
mutant can not be expressed in a soluble form
L39T
activity is comparable to wild-type activity
P253_Y254del
mutation reduces the activity to 30%
Q108E
inactive mutant enzyme
Q108E/D175N
activity is near zero
A112G
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112G
-
mutation does not alter the nature of the Fe-substrate-O2 ternary complex
additional information
-
construction of individual knockout mutants of all three nagI genes via 2 bp unmarked gene deletion mutagenesis, all three nagI knockout mutants still contain stop codons within their nagI genes. Mutant CJ2DELTAnagI3 shows severely diminished GDO activity and grows slowest on aromatic substrates
additional information
-
double mutant Phe3Leu, Val334Ala, doubled enzymatic activity, mutants in conserved core regions with less activity
additional information
-
knockout mutant G56
additional information
-
knockout mutant G56
-
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Jones, D.C.N.; Cooper, R.A.
Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
Arch. Microbiol.
154
489-495
1990
Klebsiella pneumoniae
brenda
Sugiyama, S.; Yano, K.; Komagata, K.; Arima, K.
Metabolism of aromatic compounds by microbes: Part VII. Gentisic acid oxidase
Bull. Agric. Chem. Soc. Jpn
24
243-248
1960
Pseudomonas putida
-
brenda
Goetz, F.E.; Joo, J.
Gentisate dioxygenase activity in immobilized cell-free exracts prepared from salmonella typhimurium
Biotechnol. Tech.
4
113-116
1990
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Crawford, R.I.; Hutton, S.W.; Chapman, P.J.
Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis
J. Bacteriol.
121
794-799
1975
Moraxella osloensis
brenda
Harpel, M.R.; Lipscomb, J.D.
Gentisate 1,2-dioxygenase from pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans
J. Biol. Chem.
265
6301-6311
1990
Comamonas testosteroni, Delftia acidovorans
brenda
Harpel, M.R.; Lipscomb, J.D.
Gentisate 1,2-dioxygenase from Pseudomonas. Substrate coordination to active site Fe2+ and mechanism of turnover
J. Biol. Chem.
265
22187-22196
1990
Delftia acidovorans, Comamonas testosteroni
brenda
Harpel, M.R.; Lipscomb, J.D.
Gentisate 1,2-dioxygenase from Pseudomonas acidovorans
Methods Enzymol.
188
101-107
1990
Delftia acidovorans
brenda
Wittich, R.M.; Wilkes, H.; Sinnwell, V.; Francke, W.; Fortnagel, P.
Metabolism of dibenzo-p-dioxin by Sphingomonas sp. strain RW1
Appl. Environ. Microbiol.
58
1005-1010
1992
Sphingomonas sp.
brenda
Suarez, M.; Ferrer, E.; Martin, M.
Purification and biochemical characterization of gentisate 1,2-dioxygenase from Klebsiella pneumoniae M5a1
FEMS Microbiol. Lett.
143
89-95
1996
Klebsiella pneumoniae
brenda
Chua, C.H.; Feng, Y.; Yeo, C.C.; Khoo, H.E.; Poh, C.L.
Identification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867
FEMS Microbiol. Lett.
204
141-146
2001
Pseudomonas alcaligenes
brenda
Suemori, A.; Kurane, R.; Tomizuka, N.
Purification and properties of gentisate 1,2-dioxygenase from Rhodococcus erythropolis S-1
Biosci. Biotechnol. Biochem.
57
1781-1783
1993
Rhodococcus erythropolis
-
brenda
Fu, W.; Oriel, P.
Gentisate 1,2-dioxygenase from Haloferax sp. D1227
Extremophiles
2
439-446
1998
Haloferax sp.
brenda
Kiemer, P.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase
Biol. Fertil. Soils
23
307-313
1996
Geobacillus stearothermophilus, Geobacillus stearothermophilus PK1
brenda
Werwath, J.; Arfmann, H.A.; Pieper, D.H.; Timmis, K.N.; Wittich, R.M.
Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5
J. Bacteriol.
180
4171-4176
1998
Sphingomonas sp., Sphingomonas sp. RW5
brenda
Feng, Y.; Khoo, H.E.; Poh, C.L.
Purification and characterization of gentisate 1,2-dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869
Appl. Environ. Microbiol.
65
946-950
1999
Pseudomonas alcaligenes, Pseudomonas putida, Pseudomonas alcaligenes NCIB 9867, Pseudomonas putida NCIB 9869
brenda
Yeo, C.C.; Wong, M.V.; Feng, Y.; Song, K.P.; Poh, C.L.
Molecular characterization of an inducible gentisate 1,2-dioxygenase gene, xlnE, from Pseudomonas alcaligenes NCIMB 9867
Gene
312
239-248
2003
Pseudomonas alcaligenes, Pseudomonas alcaligenes P25X
brenda
Shen, X.H.; Jiang, C.Y.; Huang, Y.; Liu, Z.P.; Liu, S.J.
Functional identification of novel genes involved in the glutathione-independent gentisate pathway in Corynebacterium glutamicum
Appl. Environ. Microbiol.
71
3442-3452
2005
Corynebacterium glutamicum, Corynebacterium glutamicum RES167
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Swetha, V.P.; Phale, P.S.
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Expansion of the substrate range of the gentisate 1,2-dioxygenase from Corynebacterium glutamicum for the conversion of monohydroxylated benzoates
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Corynebacterium glutamicum
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