EC Number   |
General Information |
Reference |
|---|
    1.13.11.3 | evolution |
phylogenetically distantly related to heterodimeric bacterial protocatechuate 3,4-dioxygenases |
763959 |
| 1.13.11.3 | malfunction |
a knockout of the BuP34O gene to generate S-M1 mutant strain causes a marked reduction in 2,4,6-trinitrotoluene (TNT) degradation efficiency compared to the S19-1 strain |
765860 |
| 1.13.11.3 | metabolism |
PCA 3,4-dioxygenase is essential for vanillate, 4-hydroxybenzoate, and protocatechuate assimilation |
712295 |
| 1.13.11.3 | metabolism |
protocatechuate 3,4-dioxygenase is the key enzyme of protocatechuate breakdown |
-, 704290 |
| 1.13.11.3 | metabolism |
the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate |
-, 742982 |
| 1.13.11.3 | more |
enzyme immobilized on calcium alginate gel binds to the carrier by electrostatic interaction while glyoxyl agarose is linked with the enzyme by covalent bonds. Since positively charged amino acids are localized at the entrance of crevasse, the electrostatic interaction plays the key role in modulation of enzyme activity. Significant increase of enzyme activity after its immobilization in calcium alginate is probably caused by strong electrostatic interactions between positively charged amino acid residues of the enzyme and negatively charged groups of alginate. High activity of immobilized protocatechuate 3,4-dioxygenase towards 2,3-dihydroxybenzoate, 2,5-dihydroxybenzoate, and 3,5-dihydroxybenzoate can be connected with modification of its catalytic mechanism as only 2,3-dihydroxybenzoate is in configuration typical for protocatechuate 3,4-dioxygenase's substrate |
-, 742046 |
| 1.13.11.3 | physiological function |
key enzyme in the 2-ketoadipate pathway. The involvement of the enzyme in bacterial degradation of 2,4,6-trinitrotoluene (TNT) and its metabolites |
765860 |
