Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain
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 act...
Váldodahkkit: | Patel, D, Kopec, J, Fitzpatrick, F, McCorvie, T, Yue, W |
---|---|
Materiálatiipa: | Journal article |
Almmustuhtton: |
Nature Publishing Group
2016
|
Geahča maid
-
Structural features of the regulatory ACT domain of phenylalanine hydroxylase.
Dahkki: Carla Carluccio, et al.
Almmustuhtton: (2013-01-01) -
Dynamic regulation of phenylalanine hydroxylase
Dahkki: Fuchs Julian E., et al.
Almmustuhtton: (2014-07-01) -
Structural basis of prolyl hydroxylase domain inhibition by Molidustat
Dahkki: Figg, WD, et al.
Almmustuhtton: (2021) -
Genotypes of patients with phenylalanine hydroxylase deficiency in the Wisconsin Amish
Dahkki: Jessica Scott Schwoerer, et al.
Almmustuhtton: (2018-06-01) -
High Protein Diet and Phenylalanine Hydroxylase Activities in Rats
Dahkki: Carty Michael P., et al.
Almmustuhtton: (1989-11-01)