This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), syringate and 3,4,5-trihydroxybenzoate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate .
This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), syringate and 3,4,5-trihydroxybenzoate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate [4].
strain CNB-1 grows on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources, but does not grow on resorcinol, 2,4-dihydroxybenzoate, 4-cresol, and phenylacetate
strain CNB-1 grows on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources, but does not grow on resorcinol, 2,4-dihydroxybenzoate, 4-cresol, and phenylacetate
strain CNB-1 grows on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources, but does not grow on resorcinol, 2,4-dihydroxybenzoate, 4-cresol, and phenylacetate
strain CNB-1 grows on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources, but does not grow on resorcinol, 2,4-dihydroxybenzoate, 4-cresol, and phenylacetate
a pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
a pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
the enzyme is active in the protocatechuate 4,5-cleavage pathway. Gene pmdU encodes an 4-oxalomesaconate tautomerase and catalyzes conversion of 4-oxalomesaconate-keto into 4-oxalomesaconate-enol, which is the only substrate of 4-oxalomesaconate hydratase. Pathway overview
the enzyme is active in the protocatechuate 4,5-cleavage pathway. Gene pmdU encodes an 4-oxalomesaconate tautomerase and catalyzes conversion of 4-oxalomesaconate-keto into 4-oxalomesaconate-enol, which is the only substrate of 4-oxalomesaconate hydratase. Pathway overview
the enzyme in strain CNB-1 is essential for growth on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources
the enzyme in strain CNB-1 is essential for growth on phenol, gentisate, vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon and energy sources
kcat/Km for 4-oxalomesaconate is 1.9fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 16% higher than wild-type value, mutant enzyme is more stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 29% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6
Functional annotation of LigU as a 1,3-allylic isomerase during the degradation of lignin in the protocatechuate 4,5-cleavage pathway from the soil bacterium Sphingobium sp. SYK-6