Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase.

نویسندگان

  • D B Fisher
  • S Kaufman
چکیده

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منابع مشابه

7-Tetrahydrobiopterin is an uncoupled cofactor for rat hepatic phenylalanine hydroxylase.

Rat hepatic phenylalanine hydroxylase requires both a tetrahydropterin cofactor and molecular oxygen to convert phenylalanine to tyrosine. During the physiological hydroxylation, a single mol of the natural cofactor, tetrahydrobiopterin, is oxidized for each mol of phenylalanine converted to tyrosine. Artificial conditions have been devised in which the oxidation of the tetrahydropterin is unco...

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Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase.

In the presence of phenylalanine and molecular oxygen, activated phenylalanine hydroxylase catalyzes the oxidation of tetrahydrobiopterin. The oxidation of this tetrahydropterin cofactor also proceeds if the substrate, phenylalanine, is replaced by its product, tyrosine, in the initial reaction mixture. These two reactions have been defined as coupled and uncoupled, respectively, because in the...

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Studies on the Phenylalanine Hydroxylase System in Liver Slices

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Studies on the Phenylalanine Hydroxylase System in Liver Slices

A method was developed to study the unsupplemented phenylalanine hydroxylase system in rat liver slices. All of the components of the systemtetrahydrobiopterin, dihydropteridine reductase, and the hydroxylase itself-are present under conditions which should be representative of the actual physiological state of the animal. The properties of the system in liver slices have been compared to those...

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 248 12  شماره 

صفحات  -

تاریخ انتشار 1973