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)

Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.

The high-resolution structure of l-aspartate ammonia-lyase from Escherichia coli has recently been determined [Shi, W., Dunbar, J., Jayasekera, M. M. K., Viola, R. E., & Farber, G. K. (1997) Biochemistry 36, 9136-9144]. An examination of the putative active site has been carried out, with the active site located in a cleft that contains the functionally significant lysine 327. A list of potential active site residues has been generated based on their proximity to this active site lysine, sequence homology comparisons with other members of the aspartase-fumarase enzyme family, and the necessity for chemically reasonable functionalities for the proposed roles. The five most likely candidates in the putative active site cleft have been examined by site-directed mutagenesis to test their feasibility for either substrate binding or acid-base catalytic roles. Arginine and lysine residues have been identified that appear to function in the orientation and binding of aspartic acid at the enzyme active site. Some tentative assignments have also been made of the acid and base catalytic groups that are proposed to be involved in the deamination reaction.[1]


  1. Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli. Jayasekera, M.M., Shi, W., Farber, G.K., Viola, R.E. Biochemistry (1997) [Pubmed]
WikiGenes - Universities