Phenylalanine Hydroxylase: Absolute Configuration and Source of Oxygen of the 4a-Hydroxytetrahydropterin Species

Thomas A. Dix, Gideon E. Bollag, Paul L. Domanico, Stephen J. Benkovic

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Abstract

The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. As indicated by its circular dichroism (CD) spectrum, the optical activity of the adduct generated from racemic 6-methyltetrahydropterin requires stereoselectivity of the oxygenation. The absolute configuration of this new stereocenter is 4a(S)-hydroxy-6(RS)-methyltetrahydropterin by analogy to the CD spectrum of one of the four stereoisomers of 5-deaza-4a-hydroxy-6-methyltetrahydropterin. The source of the 4a-hydroxy oxygen is 02, as demonstrated by the observation of a 18O-induced 13C shift in the 13C NMR spectrum of the adduct when generated from [4a-13C]-6-methyltetrahydropterin and 1802.

Original languageEnglish (US)
Pages (from-to)2955-2958
Number of pages4
JournalBiochemistry
Volume24
Issue number12
DOIs
StatePublished - Jun 1 1985

All Science Journal Classification (ASJC) codes

  • Biochemistry

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