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)
 
 
 
 
 

Evidence for involvement of 2 histidine residues in the reaction of ampicillin acylase.

The chemical modification of purified ampicillin acylase by N-bromosuccinimide and diethylpyrocarbonate resulted in time-dependent inactivation of the enzyme. Both substrates, ampicillin and 6-aminopenicillanic acid, protected the enzyme against inactivation, suggesting that the modification occurred near or at the active site. Amino acid analyses and other data indicated that two histidyl residues per subunit molecule were essential for catalytic activity.[1]

References

  1. Evidence for involvement of 2 histidine residues in the reaction of ampicillin acylase. Kim, D.J., Byun, S.M. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
 
WikiGenes - Universities