Abstract:
:The enzyme phenylalanine hydroxylase catalyzes the hydroxylation of excess phenylalanine in the liver to tyrosine. The enzyme is regulated allosterically by phenylalanine and by phosphorylation of Ser16. Hydrogen/deuterium exchange monitored by mass spectrometry has been used to gain insight into any structural change upon phosphorylation. Peptides in both the catalytic and regulatory domains show increased deuterium incorporation into the phosphorylated protein. Deuterium is incorporated into fewer peptides than when the enzyme is activated by phenylalanine, and the incorporation is slower. This establishes that the conformational change upon phosphorylation of phenylalanine hydroxylase is different from and less extensive than that upon phenylalanine activation.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Li J,Fitzpatrick PFdoi
10.1016/j.abb.2013.03.006subject
Has Abstractpub_date
2013-07-15 00:00:00pages
115-9issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(13)00094-5journal_volume
535pub_type
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