Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1987541 | International Journal of Biological Macromolecules | 2010 | 12 Pages |
Abstract
In the present work the effect of a mutation on tyrosine 33 residue (Y33G) of human cytidine deaminase (CDA) was investigated with regard to protein solubility and specific activity. Osmolytes and CDA ligands were used to increase the yield and the specific activity of the protein. The mutant enzyme was purified and subjected to a kinetic characterization and to stability studies. These investigations reinforced the hypothesis that in human CDA the side chain of Y33 is involved in intersubunit interactions with four glutamate residues (E108) forming a double latch that connects each of the two pairs of monomers of the tetrameric CDA.
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Authors
Daniela Micozzi, Stefania Pucciarelli, Francesco M. Carpi, Stefano Costanzi, Giampiero De Sanctis, Valeria Polzonetti, Paolo Natalini, Ivano F. Santarelli, Alberto Vita, Silvia Vincenzetti,