Abstract
Pseudomonas aeruginosa possesses a multigene operon that includes phenylalanine hydroxylase (PhhA; phenylalanine 4-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-carbinolamine dehydratase/homeodomain protein transregulator, and phhC encodes an aromatic aminotransferase (M(r) = 43,237). The reading frames specifying phhB and phhC overlap by 2 bases. The P. aeruginosa PhhA appears to contain iron and is pterin dependent. Unlike the multimeric mammalian hydroxylase, the native P. aeruginosa enzyme is a monomer. The P. aeruginosa PhhA is homologous with mammalian PhhA, tryptophan hydroxylase, and tyrosine hydroxylase. Expression of PhhA from its native promoter required phhB. This may suggest a positive regulatory role for phhB, consistent with the dual catalytic and regulatory roles of the corresponding mammalian homologue.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cloning, Molecular
Genes, Bacterial/genetics
Hydro-Lyases/genetics
Molecular Sequence Data
Multigene Family/genetics
Operon/genetics
Phenylalanine Hydroxylase/genetics
Pseudomonas aeruginosa/genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Transaminases/genetics
Chemicals
Phenylalanine Hydroxylase
Transaminases
Hydro-Lyases
pterin-4a-carbinolamine dehydratase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Zhao G
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
Xia T
Song J
Jensen R A
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