Native and Phosphorylated Bovine Adrenal Tyrosine 3-Monooxygenase. Interactions with Tetrahydropterins and Substrate and Stability of the Formed 4a-Hydroxy-Tetrahydrobiopterin
| Autor: | Haavik Jan, Andersson Kristoffer K., Flatmark Torgeir, Petersson Leif |
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| Jazyk: | angličtina |
| Rok vydání: | 1989 |
| Předmět: | |
| Zdroj: | Pteridines, Vol 1, Iss 1, Pp 11-16 (1989) |
| Druh dokumentu: | article |
| ISSN: | 0933-4807 2195-4720 |
| DOI: | 10.1515/pteridines.1989.1.1.11 |
| Popis: | The catalytic activity of tyrosine 3-monooxygenase (tyrosine hydroxylase) is dependent on a tetrahydropterin cofactor and ezyme-bound iron. The oxidation of tetrahydrobiopterin by bovine adrenal tyrosine hydroxylase was studied by high performance liquid chromatography (HPLC). The first pterin product detected during catalytic turnover, 4a-hydroxy-tetrahydrobiopterin, was isolated by HPLC and the pseudo first-order rate constant of its dehydration to quinonoid dihydrobiopterin was estimated. The tl /2 was found to be 45 and 72 s in 100 and 5 mmol/L Tris-HCl, respectively, at pH 7.5 and 23 °C. |
| Databáze: | Directory of Open Access Journals |
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