SUMMARY: Mutants of NCIB10015 were isolated which produced catechol 2,3-oxygenase and the subsequent enzymes of the -cleavage pathway constitutively, and were defective in phenol hydroxylase activity. All revertants of one mutant (C), and most revertants of a second mutant (C), regained wild-type characteristics with respect to inducibility of phenol hydroxylase and the other -cleavage enzymes. Their behaviour was consistent with them being regulatory mutants.

Other mutants deficient in phenol hydroxylase activity were not constitutive for catechol 2,3-oxygenase and other enzymes of the pathway. Their properties were consistent with mutations in a structural gene.

A model in which phenol hydroxylase is under positive control and catechol 2,3-oxygenase and subsequent enzymes are under negative control is proposed for the regulation of enzymes of the -cleavage pathway in .


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