We have identified an aromatic amino acid hydroxylase gene from the nematod
e C. elegans that likely encodes the worm phenylalanine hydroxylase (PheH).
The predicted amino acid sequence is most similar to that of other PheH an
d TrpA proteins. Reporter gene fusions and staining with an antibody to mam
malian PheH indicate the gene is expressed in hypodermal cells. A fusion pr
otein expressed in bacteria can convert phenylalanine to tyrosine, and, to
a lesser extent, tryptophan to 5-hydroxytryptophan. We hypothesize that the
protein is necessary to produce additional tyrosine for protein crosslinki
ng in the nematode cuticle.