Abstract
Protocatechuate 4,5-dioxygenase has been purified 100-fold from 4-hydroxybenzoate grown cells of Rhizobium leguminosarum biovar viceae. The purification yielded a homogeneous preparation with specific activity of 321 Units · mg-1 protein. The molecular weight of the homodimeric native protein was 120,000, with subunit molecular weight of 62,000. The optimum pH for catalytic activity was 9.5 and the K m for protocatechuate was 20 μM. Physical and catalytic properties of the R. leguminosarum protocatechuate 4,5-dioxygenase were different from the published characteristics of isofunctional enzymes from Pseudomonas paucimobilis and Comamonas testosteroni.
Published Version
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