PMID:10425677
| Citation |
Mattevi, A, Tedeschi, G, Bacchella, L, Coda, A, Negri, A and Ronchi, S (1999) Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure 7:745-56 |
|---|---|
| Abstract |
Given the vital role of NAD+ in cell metabolism, the enzymes involved in bacterial de novo NAD+ biosynthesis are possible targets for drug design against pathogenic bacteria. The first reaction in the pathway is catalysed by L-aspartate oxidase (LASPO), a flavoenzyme that converts aspartate to iminoaspartate using either molecular oxygen or fumarate as electron acceptors. LASPO has considerable sequence homology with the flavoprotein subunits of succinate dehydrogenase (SDH) and fumarate reductase (FRD). |
| Links | |
| Keywords |
Amino Acid Oxidoreductases/chemistry; Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Succinate Dehydrogenase/chemistry |
| 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.