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)
 
Chemical Compound Review

CHEBI:2247     7,8-diaminononanoic acid

Synonyms: AG-K-95805, CTK4E7598, AR-1H2925, AKOS006283697, AC1L19PQ, ...
 
 
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 DIAMINONONANOATE

 

High impact information on DIAMINONONANOATE

 

Biological context of DIAMINONONANOATE

 

Associations of DIAMINONONANOATE with other chemical compounds

 

Analytical, diagnostic and therapeutic context of DIAMINONONANOATE

  • Strong additional electron density close to the N7 nitrogen atom of the 7,8-diaminononanoic acid substrate in some complexes indicates that, even in the absence of added bicarbonate in the crystallization mixture, the carbamylated intermediate is formed in the crystal.(ABSTRACT TRUNCATED AT 400 WORDS)[10]

References

  1. Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis. Sandmark, J., Eliot, A.C., Famm, K., Schneider, G., Kirsch, J.F. Biochemistry (2004) [Pubmed]
  2. Spectral and kinetic characterization of 7,8-diaminopelargonic acid synthase from Mycobacterium tuberculosis. Bhor, V.M., Dev, S., Vasanthakumar, G.R., Surolia, A. IUBMB Life (2006) [Pubmed]
  3. Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies. Bhor, V.M., Dev, S., Vasanthakumar, G.R., Kumar, P., Sinha, S., Surolia, A. J. Biol. Chem. (2006) [Pubmed]
  4. Isolation and characterization of the Erwinia herbicola bio operon and the sequences of the bioA and bioB genes. Wu, C.H., Chen, H.Y., Shiuan, D. Gene (1996) [Pubmed]
  5. In vitro synthesis and and regulation of the biotin enzymes of Escherichia coli K-12. Prakash, O., Eisenberg, M.A. J. Bacteriol. (1978) [Pubmed]
  6. Complementation of an Arabidopsis thaliana biotin auxotroph with an Escherichia coli biotin biosynthetic gene. Patton, D.A., Volrath, S., Ward, E.R. Mol. Gen. Genet. (1996) [Pubmed]
  7. The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Eliot, A.C., Sandmark, J., Schneider, G., Kirsch, J.F. Biochemistry (2002) [Pubmed]
  8. Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum. Hatakeyama, K., Hohama, K., Vertès, A.A., Kobayashi, M., Kurusu, Y., Yukawa, H. DNA Seq. (1993) [Pubmed]
  9. Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Alexeev, D., Baxter, R.L., Sawyer, L. Structure (1994) [Pubmed]
  10. Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Huang, W., Jia, J., Gibson, K.J., Taylor, W.S., Rendina, A.R., Schneider, G., Lindqvist, Y. Biochemistry (1995) [Pubmed]
 
WikiGenes - Universities