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Proto catechuate 3 4 di oxygenase ec 1.13.11.3 inhibitor studies and mechanistic implications



Proto catechuate 3 4 di oxygenase ec 1.13.11.3 inhibitor studies and mechanistic implications



Biochimica et Biophysica Acta 485(1): 60-74



Protocatechuate 3,4-dioxygenase (EC 1.13.11.3) from Pseudomonas aeruginosa catalyzes the cleavage of 3,4-dihydroxybenzoate (protocatechuate) into .beta.-carboxy-cis,cis-muconate. The inhibition constants, Ki, of a series of substrate analoges were measured to assess the relative importance of the various functional groups on the substrate. Though important for binding, the carboxylate group is not essential for activity. Compounds with para hydroxy groups are better inhibitors than their meta isomers. Studies of the enzyme .cntdot. inhibitor complexes indicate that the 4-OH group of the substrate binds to the active-site Fe. Taken together, Moessbauer, EPR and kinetic data suggest a mechanism where substrate reaction with O2 is preceded by metal activation of substrate.

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