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 220.127.116.11) (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.
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