Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase

Volume: 291, Issue: 14, Pages: 7418 - 7425
Published: Apr 1, 2016
Abstract
Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme that requires activation by phenylalanine for full activity. The location of the allosteric site for phenylalanine has not been established. NMR spectroscopy of the isolated regulatory domain (RDPheH(25–117) is the regulatory domain of PheH lacking residues 1–24) of the rat enzyme in the presence of phenylalanine is consistent with formation of a side-by-side ACT dimer. Six residues...
Paper Details
Title
Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase
Published Date
Apr 1, 2016
Volume
291
Issue
14
Pages
7418 - 7425
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