Abstract
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.
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