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

Robert J. Miller; Stephen J. Benkovic

doi:10.1021/bi00410a021

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

Robert J. Miller
, Stephen J. Benkovic

Chemistry

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

The phenylalanine analogue L-[2,5-H₂]phenylalanine (1) was found to be a viable substrate (K_M= 0.45 mM, k_cat= 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 language	English (US)
Pages (from-to)	3658-3663
Number of pages	6
Journal	Biochemistry
Volume	27
Issue number	10
DOIs	https://doi.org/10.1021/bi00410a021
State	Published - May 1 1988

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi00410a021

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

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.",

author = "Miller, \{Robert J.\} and Benkovic, \{Stephen J.\}",

year = "1988",

month = may,

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doi = "10.1021/bi00410a021",

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volume = "27",

pages = "3658--3663",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

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T1 - L-[2,5-H2]Phenylalanine, an Alternate Substrate for Rat Liver Phenylalanine Hydroxylase

AU - Miller, Robert J.

AU - Benkovic, Stephen J.

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Y1 - 1988/5/1

N2 - 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.

AB - 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.

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UR - https://www.scopus.com/pages/publications/0024290401#tab=citedBy

U2 - 10.1021/bi00410a021

DO - 10.1021/bi00410a021

M3 - Article

C2 - 3408719

AN - SCOPUS:0024290401

SN - 0006-2960

VL - 27

SP - 3658

EP - 3663

JO - Biochemistry

JF - Biochemistry

IS - 10

ER -

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

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