Synthetic reduced pterin cofactor for nitric oxide synthetase, and for phenylalanine, tyrosine, and tryptophan hydroxylases; less active than the natural cofactor, tetrahydrobiopterin (BH4).
Biochimica et biophysica acta, 789(2), 111-118 (1984-09-11)
A new microbial inhibitor for rat-liver phenylalanine hydroxylase (L-phenylalanine, tetrahydropteridine: oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1) was isolated from a culture medium of Fomes tasmanicus, and its structure was determined as 3,4-dihydroxystyrene. This compound inhibited the enzyme by 50% at a
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 8(1-2), 121-128 (2002-12-03)
Phenylalanine hydroxylase (PAH) is a pterin-dependent non-heme metalloenzyme that catalyzes the oxidation of phenylalanine to tyrosine, which is the rate-limiting step in the catabolism of Phe. Chromobacterium violaceum phenylalanine hydroxylase (cPAH) has been prepared and its steady-state mechanism has been
Proceedings of the National Academy of Sciences of the United States of America, 88(13), 5734-5738 (1991-07-01)
A monoclonal anti-idiotype antibody, NS7, previously shown to mimic the binding of the pterin cofactor of phenylalanine hydroxylase (phenylalanine 4-monooxygenase, EC 1.14.16.1) has been used to localize the cofactor binding site within the phenylalanine hydroxylase catalytic domain to a 27-amino-acid
Journal of biochemistry, 90(2), 567-569 (1981-08-01)
A simple and rapid method for isolating tryptophan 5-monooxygenase [L-tryptophan, tetrahydropteridine:oxygen oxidoreductase (5-hydroxylating), EC 1.14.16.4] was reported. The method involves adsorption on calcium phosphate gel and affinity chromatography on agarose coupled with dimethyltetrahydropteridine. Tryptophan 5-monooxygenase was purified 1,100-fold from a
Acta physiologica et pharmacologica latinoamericana : organo de la Asociacion Latinoamericana de Ciencias Fisiologicas y de la Asociacion Latinoamericana de Farmacologia, 34(3), 235-243 (1984-01-01)
Cholinergic modulation on the regulation of tyrosine hydroxylase was studied in guinea pig atria depolarized with high potassium concentration. In these conditions there was an increment in tyrosine hydroxylase activity as well as in the release of radioactivity from atria
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