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Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase
Author(s) -
Kobe Bostjan,
House Colin M.,
Feil Susanne C.,
Michell Belinda J.,
Tiganis Tony,
Parker Michael W.,
Kemp Bruce E.,
Cotton Richard G.H.,
Jennings Ian G.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060626
Subject(s) - phenylalanine hydroxylase , phosphorylation , phenylalanine , crystallization , chemistry , biochemistry , enzyme , microbiology and biotechnology , biology , amino acid , organic chemistry
Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme.