1nrg

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|PDB= 1nrg |SIZE=350|CAPTION= <scene name='initialview01'>1nrg</scene>, resolution 1.95&Aring;
|PDB= 1nrg |SIZE=350|CAPTION= <scene name='initialview01'>1nrg</scene>, resolution 1.95&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= Human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= Human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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[[Category: pyridoxine-5'-phosphate]]
[[Category: pyridoxine-5'-phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:00:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:56:46 2008''

Revision as of 10:56, 23 March 2008

Image:1nrg.jpg


PDB ID 1nrg

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , , and
Gene: Human (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



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


Contents

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. 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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