Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylase

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چکیده

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Phosphorylation and mutations of Ser(16) in human phenylalanine hydroxylase. Kinetic and structural effects.

Phosphorylation of phenylalanine hydroxylase (PAH) at Ser(16) by cyclic AMP-dependent protein kinase is a post-translational modification that increases its basal activity and facilitates its activation by the substrate l-Phe. So far there is no structural information on the flexible N-terminal tail (residues 1-18), including the phosphorylation site. To get further insight into the molecular b...

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ژورنال

عنوان ژورنال: Protein Science

سال: 2004

ISSN: 0961-8368,1469-896X

DOI: 10.1110/ps.03595904