Abstract
Gentisate 1,2-dioxygenase (E.C.I.14.13) was purified to homogeneity from Klebsiella pneumoniae M5a1, a soil bacterium able to degrade a great variety of aromatic compounds. The molecular mass of the purified holoenzyme was 159 kDa and its structure was deduced to be a tetramer with 38 kDa per subunit. Gentisate 1,2-dioxygenase appears to contain Fe 2+ in its active site. The optimum temperature for enzyme activity was estimated to be 30 °C, the optimum pH values varied between 8 and 9 and the isoelectric point was 4.7. Gentisate dioxygenase exhibited typical saturation kinetics and had an apparent K m of 52 μM for gentisate. Its amino acid content was determined to be very similar to that of the enzyme from Pseudomonas acidovorans.
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