Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications.

Almås, B; Le Bourdelles, B; Flatmark, T; Mallet, J; Haavik, J

Almås, B; Le Bourdelles, B; Flatmark, T; Mallet, J; Haavik, J.

Affiliation

Almås B; Department of Biochemistry, University of Bergen, Norway.

Eur J Biochem ; 209(1): 249-55, 1992 Oct 01.

Article in En | MEDLINE | ID: mdl-1356768

Subject(s)

Catecholamines/metabolism; Isoenzymes/metabolism; Tyrosine 3-Monooxygenase/metabolism; Binding Sites; Binding, Competitive; Biopterins/analogs & derivatives; Biopterins/metabolism; Cyclic AMP/pharmacology; Dopamine/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Humans; Iron/metabolism; Kinetics; Phosphorylation; Protein Kinases/metabolism; Spectrophotometry; Structure-Activity Relationship; Tyrosine 3-Monooxygenase/chemistry; Tyrosine 3-Monooxygenase/genetics

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Collection: 01-internacional Database: MEDLINE Main subject: Tyrosine 3-Monooxygenase / Catecholamines / Isoenzymes Limits: Humans Language: En Journal: Eur J Biochem Year: 1992 Document type: Article Affiliation country: Norway Country of publication: United kingdom

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