Abstract 1900 Investigating substrate promiscuity of 6-hydroxynicotinate 3-monooxygenase (NicC): NicC activity with 5-Cl-coumalate

6-Hydroxynicotinate 3-monooxygenase (NicC) catalyzes the decarboxylative hydroxylation of 6HNA, a key intermediate involved in the degradation of nicotinic acid by aerobic bacteria. As a N-heterocyclic aromatic compound, the biodegradation of nicotinic acid serves as a model for exploring the mechanisms and specificity of critical enzymes in the biodegradation of environmental pollutants. Earlier studies of NicC have demonstrated its ability to bind and catalyze the hydroxylation and decarboxylation of chlorinated substrate analogues.