Regulation of the Enzymes of the β-Ketoadipate Pathway in Moraxella calcoacetica

Abstract

The inducible enzymes responsible for the dissimilation of aromatic compounds through the β-ketoadipate pathway by Moraxella calcoacetica are subject to a high degree of coordinate control. The five enzymes which catalyze the conversion of protocatechuate to β-ketoadipyl-CoA are coordinately synthesized, the probable inducer being protocatechuate. In the conversion of catechol to β-ketoadipyl-CoA, there are two separate inductive events, though both are mediated by one metabolite-inducer, cis,cis-muconate. One is the induction of catechol oxygenase; the other is the coordinate induction of the four enzymes that catalyze conversion of cic,cis-muconate to β-ketoadipyl-CoA.