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

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 the PAH N-terminal regulatory domain (PAH-RD), ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/srep23748

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More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Publisher:
Nature Publishing Group
Journal:
Scientific Reports More from this journal
Volume:
6
Pages:
23748-23748
Publication date:
2016-04-06
Acceptance date:
2016-03-08
DOI:
EISSN:
2045-2322
Pubs id:
pubs:616195
UUID:
uuid:62d5d77f-fd7b-4fc6-b0f7-9639c05ce11b
Local pid:
pubs:616195
Source identifiers:
616195
Deposit date:
2016-04-18

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