The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

nadB  -  quinolinate synthase, L-aspartate oxidase...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2572, JW2558, nic, nicB
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of nadB

 

High impact information on nadB

 

Chemical compound and disease context of nadB

 

Biological context of nadB

 

Associations of nadB with chemical compounds

 

Other interactions of nadB

  • Adjacent to cooA are two genes, nadB and nadC, with predicted products similar to proteins in other bacteria that catalyze reactions in the de novo synthesis of NAD.(ABSTRACT TRUNCATED AT 250 WORDS)[13]
  • We describe the identification of the Yersinia enterocolitica rpoE gene, which encodes the alternative sigma factor sigmaE, and the divergently transcribed nadB gene, as genes that are expressed during infection of mice [3].
 

Analytical, diagnostic and therapeutic context of nadB

References

  1. Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Flachmann, R., Kunz, N., Seifert, J., Gütlich, M., Wientjes, F.J., Läufer, A., Gassen, H.G. Eur. J. Biochem. (1988) [Pubmed]
  2. Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase. Seifert, J., Kunz, N., Flachmann, R., Läufer, A., Jany, K.D., Gassen, H.G. Biol. Chem. Hoppe-Seyler (1990) [Pubmed]
  3. Identification of rpoE and nadB as host responsive elements of Yersinia enterocolitica. Heusipp, G., Schmidt, M.A., Miller, V.L. FEMS Microbiol. Lett. (2003) [Pubmed]
  4. L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. Nasu, S., Wicks, F.D., Gholson, R.K. J. Biol. Chem. (1982) [Pubmed]
  5. Nicking activity of TrwC directed against the origin of transfer of the IncW plasmid R388. Llosa, M., Grandoso, G., de la Cruz, F. J. Mol. Biol. (1995) [Pubmed]
  6. Probing the active site of L-aspartate oxidase by site-directed mutagenesis: role of basic residues in fumarate reduction. Tedeschi, G., Ronchi, S., Simonic, T., Treu, C., Mattevi, A., Negri, A. Biochemistry (2001) [Pubmed]
  7. Redox potentials and quinone reductase activity of L-aspartate oxidase from Escherichia coli. Tedeschi, G., Zetta, L., Negri, A., Mortarino, M., Ceciliani, F., Ronchi, S. Biochemistry (1997) [Pubmed]
  8. Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis. Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F., Fontecave, M. FEBS Lett. (2005) [Pubmed]
  9. L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity. Tedeschi, G., Negri, A., Mortarino, M., Ceciliani, F., Simonic, T., Faotto, L., Ronchi, S. Eur. J. Biochem. (1996) [Pubmed]
  10. Characterization of an efficient gene cloning strategy for Aspergillus niger based on an autonomously replicating plasmid: cloning of the nicB gene of A. niger. Verdoes, J.C., Punt, P.J., van der Berg, P., Debets, F., Stouthamer, A.H., van den Hondel, C.A. Gene (1994) [Pubmed]
  11. Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. Tedeschi, G., Negri, A., Ceciliani, F., Mattevi, A., Ronchi, S. Eur. J. Biochem. (1999) [Pubmed]
  12. L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Mortarino, M., Negri, A., Tedeschi, G., Simonic, T., Duga, S., Gassen, H.G., Ronchi, S. Eur. J. Biochem. (1996) [Pubmed]
  13. Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators. Shelver, D., Kerby, R.L., He, Y., Roberts, G.P. J. Bacteriol. (1995) [Pubmed]
  14. Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD. Bacchella, L., Lina, C., Todone, F., Negri, A., Tedeschi, G., Ronchi, S., Mattevi, A. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
 
WikiGenes - Universities