Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain

Volume: 6, Issue: 1
Published: Apr 1, 2016
Abstract
The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine. Inherited mutations that result in PAH enzyme deficiency are the genetic cause of the autosomal recessive disorder phenylketonuria. Phe is the substrate for the PAH active site, but also an allosteric ligand that increases enzyme activity. Phe has been proposed to bind, in addition to the catalytic domain, a site at...
Paper Details
Title
Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain
Published Date
Apr 1, 2016
Volume
6
Issue
1
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