Abstract:
:To determine the regulatory mechanism for human tyrosine hydroxylase, we examined modulations of the activity of the enzyme from human pheochromocytoma by cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion. The most remarkable activation was observed when the enzyme was assayed at physiological pH (pH 7) after being subjected to phosphorylation by cyclic AMP-dependent protein kinase. Calmodulin-dependent protein kinase II and polyanion also modulated the enzyme activity. The results suggest that tyrosine hydroxylase may be regulated similarly in both human and rat.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Okuno S,Kanayama Y,Fujisawa Hdoi
10.1016/0014-5793(89)80927-5subject
Has Abstractpub_date
1989-08-14 00:00:00pages
52-4issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(89)80927-5journal_volume
253pub_type
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