2pah

From Proteopedia

Revision as of 15:31, 30 October 2007

TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE

Overview

Phenylalanine hydroxylase (PheOH) catalyzes the conversion of, L-phenylalanine to L-tyrosine, the rate-limiting step in the oxidative, degradation of phenylalanine. Mutations in the human PheOH gene cause, phenylketonuria, a common autosomal recessive metabolic disorder that in, untreated patients often results in varying degrees of mental retardation., We have determined the crystal structure of human PheOH (residues, 118-452). The enzyme crystallizes as a tetramer with each monomer, consisting of a catalytic and a tetramerization domain. The, tetramerization domain is characterized by the presence of a domain, swapping arm that interacts with the other monomers forming an, antiparallel coiled-coil. The structure is the first report of a, tetrameric PheOH and displays an overall ... [(full description)]

About this Structure

2PAH is a [Single protein] structure of sequence from [Homo sapiens] with FE as [ligand]. The following page contains interesting information on the relation of 2PAH with [Phenylalanine Hydroxylase]. Active as [Phenylalanine 4-monooxygenase], with EC number [1.14.16.1]. Structure known Active Site: FE. Full crystallographic information is available from [OCA].

Reference

Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria., Fusetti F, Erlandsen H, Flatmark T, Stevens RC, J Biol Chem. 1998 Jul 3;273(27):16962-7. PMID:9642259

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