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Pseudomonas aeruginosa possesses a multigeneoperon that includes phenylalanine hydroxylase (PhhA; phenylalanine4-monooxygenase, EC 1.14.16.1). phhA encodes PhhA (M(r) = 30,288), phhB (M(r) =13,333) encodes a homologue of mammalian 4 alpha-carbinolaminedehydratase/homeodomain protein transregulator, and phhC encodes an aromaticaminotransferase (M(r) = 43,237). The reading frames specifying phhB and phhCoverlap by 2 bases. The P. aeruginosa PhhA appears to contain iron and is pterindependent. Unlike the multimeric mammalian hydroxylase, the native P. aeruginosaenzyme is a monomer. The P. aeruginosa PhhA is homologous with mammalian PhhA,tryptophan hydroxylase, and tyrosine hydroxylase. Expression of PhhA from itsnative promoter required phhB. This may suggest a positive regulatory role forphhB, consistent with the dual catalytic and regulatory roles of thecorresponding mammalian homologue.

proceedings of the national academy of sciences of the united states of america

Pseudomonas aeruginosa possesses homologues ofmammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoHas part of a three-component gene cluster.