Ontology highlight
ABSTRACT:
SUBMITTER: Patel D
PROVIDER: S-EPMC4822156 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Patel Dipali D Kopec Jolanta J Fitzpatrick Fiona F McCorvie Thomas J TJ Yue Wyatt W WW
Scientific reports 20160406
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 the PAH N-terminal regulatory domain (PAH-RD), to ...[more]