L-[2,5-H2]Phenylalanine, an Alternate Substrate for Rat Liver Phenylalanine Hydroxylase

Robert J. Miller, Stephen J. Benkovic

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19 Scopus citations

Abstract

The phenylalanine analogue L-[2,5-H2]phenylalanine (1) was found to be a viable substrate (KM= 0.45 mM, kcat= 8 s-1) for L-phenylalanine-activated, rat liver phenylalanine hydroxylase (EC 1.14.16.1) (PAH). the PAH-catalyzed oxidation of 1 was stoichiometric with the oxidation of cofactor, 6-methyl-tetrahydropterin. Spectral and chromatographic data of the product from the oxidation of 1 by PAH were found to be in accord with a 3,4-epoxide. the enzymatic epoxidation of 1 is consistent with the hypothesis of an intermediate arene oxide on the reaction coordinate for PAH hydroxylation of L-phenylalanine.

Original languageEnglish (US)
Pages (from-to)3658-3663
Number of pages6
JournalBiochemistry
Volume27
Issue number10
DOIs
StatePublished - May 1 1988

All Science Journal Classification (ASJC) codes

  • Biochemistry

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