Inhibition of Diaminopimelic Acid Decarboxylase Activity in Mycobacterium tuberculosis by Isonicotinic Acid Hydrazide.

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Abstract
Cell-free extracts of M. tuberculosis contain an enzyme which decarboxylates a, -diaminopimelic acid (DAP) to CO2 and lysine. Rate of decarboxylation of DAP was increased by the addition of pyridoxal phosphate. DAP decarboxylase activity was markedly inhibited by isonicotinic acid hydrazide (INH). This inhibition was greater if the drug was preincubated with the enzyme before addition of substrate. The inhibition could be prevented by pre-incubation of the reaction mixture with pyridoxal phosphate prior to addition of INH.