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)
 
 
 
 
 
 

Pteroylpoly(gamma-glutamate) synthesis by Corynebacterium species. Studies on the mechanism of folypoly(gamma-glutamate) synthetase.

The mechanism of action of folylpolyglutamate synthetase from Corynebacterium sp. was investigated using tetrahydrofolate, MgATP, and glutamate as the substrates. Initial velocity, product inhibition, and competitive inhibition studies were consistent with an Ordered Ter Ter mechanism with MgATP binding first to the enzyme, tetrahydrofolate second, and glutamate last. The order of dissociation from the enzyme was ADP, folate, and Pi. This mechanism precludes the sequential addition of glutamate moieties to enzyme-bound folate. The Michaelis constants for (dl)-tetrahydrofolate, MgATP, and glutamate were 2,1 muM, 18 MUM, and 160 muM, respectively. Beta, gamma-Methylene-ATP was a very effective inhibitor of the reaction with an affinity for the enzyme 1 order of magnitude greater than that of ATP.[1]

References

 
WikiGenes - Universities