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2.7.7.3
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the enzyme is allosteric in nature and regulated by coenzyme A through feedback inhibition. Structure-function analysis, and analysis of catalytic, allosteric and inhibitory mechanisms involved in regulation of PPAT. Changes in side chains R90 and D94 are responsible for transition between catalytic and allosteric inhibitory states. Diphosphate binds in close vicinity of ATP and produces a 10 A flip in the adenine ring of coenzyme A moiety. Transition of PPAT in Pseudomonas aeruginosa from substrate binding to inhibitory states is triggered by an arginine switch
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