Synthetic reduced pterin cofactor for nitric oxide synthetase, and for phenylalanine, tyrosine, and tryptophan hydroxylases; less active than the natural cofactor, tetrahydrobiopterin (BH4).
Biulleten' eksperimental'noi biologii i meditsiny, 91(5), 553-554 (1981-05-01)
Activity and KM of hypothalamic tyrosine hydroxylase (TH) were studied in rats preliminarily tested for predisposition to high ethanol consumption. It was shown that as regards cofactor of DMPH4 enzymatic reaction, KM of hypothalamic TH of animals with an initially
5-Hydroxy-l-tryptophan (5-HTP) is a naturally occurring aromatic amino acid present in the seeds of the African plant Griffonia simplicifolia. Although 5-HTP has therapeutic effects in various symptoms, efficient method of producing 5-HTP has not been established. In this study, we
To elucidate the early steps required during biosynthesis of a broad class of 7-deazapurine-containing natural products, we have studied the reaction catalyzed by Escherichia coli QueD, a 6-pyruvoyl-5,6,7,8-tetrahydropterin synthase (PTPS) homologue possibly involved in queuosine biosynthesis. While mammalian PTPS homologues
The Journal of biological chemistry, 265(4), 1885-1889 (1990-02-05)
BALB/c mice were immunized with a synthetic co-factor of the aromatic amino acid hydroxylases, 6,7-dimethyl-5,6,7,8-tetrahydropterin, conjugated to albumin. Hybridoma cell lines isolated from the immunized mice secreted monoclonal antibodies reacting specifically with the pterin molecule and monoclonal antibodies which were
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
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