Allosteric regulation of phenylalanine hydroxylase

Paul F. Fitzpatrick

doi:10.1016/j.abb.2011.09.012

Allosteric regulation of phenylalanine hydroxylase

Paul F. Fitzpatrick

Department of Biochemistry & Structural Biology

Research output: Contribution to journal › Review article › peer-review

57 Scopus citations

Abstract

The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.

Original language	English (US)
Pages (from-to)	194-201
Number of pages	8
Journal	Archives of Biochemistry and Biophysics
Volume	519
Issue number	2
DOIs	https://doi.org/10.1016/j.abb.2011.09.012
State	Published - Mar 15 2012

Keywords

Allostery
Phenylalanine hydroxylase
Phosphorylation
Regulation
Tetrahydrobiopterin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/j.abb.2011.09.012

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title = "Allosteric regulation of phenylalanine hydroxylase",

abstract = "The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.",

keywords = "Allostery, Phenylalanine hydroxylase, Phosphorylation, Regulation, Tetrahydrobiopterin",

author = "Fitzpatrick, {Paul F.}",

note = "Funding Information: This work was supported in part by NIH grants GM047291 and GM098140. ",

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AU - Fitzpatrick, Paul F.

N1 - Funding Information: This work was supported in part by NIH grants GM047291 and GM098140.

PY - 2012/3/15

Y1 - 2012/3/15

N2 - The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.

AB - The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.

KW - Allostery

KW - Phenylalanine hydroxylase

KW - Phosphorylation

KW - Regulation

KW - Tetrahydrobiopterin

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U2 - 10.1016/j.abb.2011.09.012

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M3 - Review article

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SN - 0003-9861

VL - 519

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EP - 201

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 2

ER -

Allosteric regulation of phenylalanine hydroxylase

Abstract

Keywords

ASJC Scopus subject areas

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