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Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation

Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l‐phenylalanine (l‐Phe) metabolism and is active as a homotetramer. Biochemical and biophysical work has demonstrated that it cycles between two states with a variably low and a high activity, and that the substrate l‐Phe is the key player...

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Autors principals: João Leandro, Anne J. Stokka, Knut Teigen, Ole A. Andersen, Torgeir Flatmark
Format: Artigo
Idioma:Inglês
Publicat: Wiley 2017-07-01
Col·lecció:FEBS Open Bio
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Accés en línia:https://doi.org/10.1002/2211-5463.12243
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