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)
 
 
 
 
 

A homogeneous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides.

A homogeneous preparation of cyclic CMP phosphodiesterase (Helfman, D. M., Shoji, M., and Kuo, J. F. (1981) J. Biol. Chem. 256, 6327-6334) was found to catalyze the hydrolysis of both pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides. Hydrolysis of cyclic 2':3'-nucleotides resulted in the formation of both 2'- and 3'-nucleotides, although relative amounts of the products were variable. Hydrolysis of cyclic 2':3'-CMP or cyclic 2':3'-UMP yielded predominantly 3'-nucleotides. In contrast, hydrolysis of cyclic 2':3'-AMP produced equal amounts of 2'- and 3'-nucleotides, while the major product formed from cyclic 2':3'-GMP was 2'-nucleotide. When conventional pyrimidine and purine cyclic 3:5'-nucleotides were used as substrates, the enzyme hydrolyzed specifically the 3'-bond to yield only 5'-nucleotides. The relative rate of hydrolysis of cyclic 2':3'-nucleotides was cyclic CMP greater than cyclic UMP greater than cyclic GMP greater than or equal to cyclic AMP, respectively, whereas that for cyclic 3':5'-nucleotides was cyclic CMP greater than cyclic UMP greater than or equal to cyclic AMP greater than cyclic GMP, respectively. Furthermore, kinetic analysis suggested a single species of catalytic site on the enzyme may be involved in the hydrolysis of both pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides. These findings indicate that the present enzyme is the first multifunctional phosphodiesterase reported to date that is capable of hydrolyzing such a diversity of cyclic nucleotides.[1]

References

 
WikiGenes - Universities