The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.

l -Phenylalanine, d -phenylalanine, ( S )-2-amino-3-phenyl-1-propanol, l -norleucine, and l -methionine all activated PheH ∼7-fold. Lower levels of activation were seen with l -4-aminophenylalanine, 3-phenylpropionate, l -leucine, and l -isoleucine; this is consistent with the very low affinities of these compounds. The activation by valine is barely significant, consistent with the small effects of this amino acid on fluorescence and dimerization.

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