1nrg

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spinqualitylabelsall models 1nrg, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the, synthesis of pyridoxal 5'-phosphate. The cDNA for the human enzyme has, been cloned and expressed in Escherichia coli. The purified human enzyme, is a homodimer that exhibits a low catalytic rate constant of, approximately 0.2 sec(-1) and K(m) values in the low micromolar range for, both pyridoxine 5'phosphate and pyridoxamine 5'-phosphate. Pyridoxal, 5'-phosphate is an effective product inhibitor. The three-dimensional fold, of the human enzyme is very similar to those of the E. coli and yeast, enzymes. The human and E. coli enzymes share 39% sequence identity, but, the binding sites for the tightly bound FMN and substrate are highly, conserved. As observed with the E. coli enzyme, the human enzyme binds one, molecule of pyridoxal 5'-phosphate tightly on each subunit.

Disease

Known disease associated with this structure: Pyridoxamine 5 -phosphate oxidase deficiency OMIM:[603287]

About this Structure

1NRG is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase., Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK, Protein Sci. 2003 Jul;12(7):1455-63. PMID:12824491

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