Evidence from EPR spectroscopy that phosphorylation of Ser‐40 in bovine adrenal tyrosine hydroxylase facilitates the reduction of high‐spin Fe(III) under turnover conditions

FEBS Letters

Flatmark, Torgeir²  Petersson, Leif¹  Haavik, Jan²  Andersson, Kristoffer K.²  Martinez, Aurora² 

[1] Department of Biophysics, University of Stockholm, Stockholm, Sweden;Department of Biochemistry, University of Bergen, Bergen, Norway

关键词: Tyrosine hydroxylase;    Phosphorylation;    Electron paramagnetic resonance;    Cyclic AMP-dependent protein kinase;    Non-heme iron;    Catecholamine;    Pteridine;    (Bovine adrenal);    TH;    tyrosine hydroxylase;    EPR;    electron paramagnetic resonance;    DOPA;    3;    4-dihydroxyphenylalanine;    HPLC;    high-performance liquid chromatography;    6-MPH4;    6-methyltetrahydropterin;   

DOI  :  10.1016/0014-5793(89)81603-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The tetrahydrobiopterin-dependent iron-enzyme tyrosine hydroxylase (TH) catalyses the rate-limiting step in catecholamine biosynthesis. Electron paramagnetic resonance (EPR) data show that following phosphorylation of Ser-40 by protein kinase A, the enzyme-bound Fe(III), coordinated to catecholamines, can be reduced by 6-methyl-tetrahydropterin under turnover conditions. The 8-fold increase in product formation upon phosphorylation can partly be explained by an increase in the fraction of active TH, by dissociation of the endogenous catecholamine inhibitors.

【 授权许可】

Unknown