PMID:10903950
| Citation |
Safo, MK, Mathews, I, Musayev, FN, di Salvo, ML, Thiel, DJ, Abraham, DJ and Schirch, V (2000) X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution. Structure 8:751-62 |
|---|---|
| Abstract |
Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high degree of sequence homology among the 15 known members of the PNPOx family suggests that all members of this group have similar three-dimensional folds. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Chymotrypsin/chemistry; Crystallography, X-Ray; Desulfovibrio vulgaris/enzymology; Dimerization; Electron Transport; Escherichia coli/enzymology; Flavin Mononucleotide/chemistry; Flavin Mononucleotide/metabolism; Models, Molecular; Molecular Sequence Data; Phosphates/metabolism; Protein Binding; Protein Conformation; Protein Structure, Secondary; Pyridoxaminephosphate Oxidase/chemistry; Pyridoxaminephosphate Oxidase/metabolism; Recombinant Fusion Proteins/chemistry; Saccharomyces cerevisiae/enzymology; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.