Abstract:
:The effects of phenylalanine and tetrahydrobiopterin on the limited proteolysis of rat liver phenylalanine hydroxylase by chymotrypsin have been examined. The presence of tetrahydrobiopterin inhibits the proteolytic activation of native phenylalanine hydroxylase. In contrast, phenylalanine causes a stimulation of proteolytic activation under these conditions. Neither phenylalanine nor tetrahydrobiopterin affect the rate of hydrolysis of a synthetic substrate by chymotrypsin. Both tetrahydrobiopterin and phenylalanine inhibit the release of soluble radioactivity from [32P]phosphorylated phenylalanine hydroxylase. These results confirm the existence of multiple conformational states of phenylalanine hydroxylase.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Phillips RS,Iwaki M,Kaufman Sdoi
10.1016/0006-291x(83)91050-1subject
Has Abstractpub_date
1983-02-10 00:00:00pages
919-25issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(83)91050-1journal_volume
110pub_type
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