Journal article
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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Authors
Bibliographic Details
- Publisher:
- Nature Publishing Group Publisher's website
- Journal:
- Scientific Reports Journal website
- Volume:
- 6
- Pages:
- 23748-23748
- Publication date:
- 2016-04-06
- Acceptance date:
- 2016-03-08
- DOI:
- EISSN:
-
2045-2322
Item Description
- Pubs id:
-
pubs:616195
- UUID:
-
uuid:62d5d77f-fd7b-4fc6-b0f7-9639c05ce11b
- Local pid:
- pubs:616195
- Source identifiers:
-
616195
- Deposit date:
- 2016-04-18
Terms of use
- Copyright holder:
- Patel et al
- Copyright date:
- 2016
- Notes:
- Copyright Patel et al. This work is licensed under a Creative Commons Attribution 4.0 International License. This is the final version of the article. This is available online from Nature at: https://doi.org/10.1038/srep23748
- Licence:
- CC Attribution (CC BY)
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