Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria

H Erlandsen; F Fusetti; A Martinez; E Hough; T Flatmark; R C Stevens

doi:10.1038/nsb1297-995

Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria

Nat Struct Biol. 1997 Dec;4(12):995-1000. doi: 10.1038/nsb1297-995.

Authors

H Erlandsen, F Fusetti, A Martinez, E Hough, T Flatmark, R C Stevens

PMID: 9406548
DOI: 10.1038/nsb1297-995

Abstract

The 2.0 A crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydroxylase. It provides the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria.

Publication types

Comparative Study
Letter
Research Support, Non-U.S. Gov't
Review

MeSH terms

Amino Acid Sequence
Animals
Binding Sites / genetics
Crystallization
Humans
Models, Molecular
Molecular Sequence Data
Mutation
Phenylalanine Hydroxylase / chemistry*
Phenylalanine Hydroxylase / genetics
Phenylketonurias / enzymology*
Phenylketonurias / genetics
Protein Folding
Tyrosine 3-Monooxygenase / chemistry
Tyrosine 3-Monooxygenase / genetics

Substances

Phenylalanine Hydroxylase
Tyrosine 3-Monooxygenase