ATP, cyclic AMP, and magnesium increase the affinity of rat striatal tyrosine hydroxylase for its cofactor.

Abstract
Treatment of rat striatal tyrosine hydroxylase [tyrosine 3-monooxygenase; L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating); EC 1.14.16.2] with conditions optimal for protein phosphorylation results in the reduction of the tyrosine hydroxylase Km for the cofactor 6-methyltetrahydropterin from 0.50 mM to 0.16 mM. This reaction is dependent upon ATP, 3'':5''-cyclicAMP, and Mg2+ and causes a marked decrease in the sensitivity to end-product inhibition. Other brain regions and the adrenal gland show a similar response.