Role of tyrosine 33 residue for the stabilization of the tetrameric structure of human cytidine deaminase

Add time:07/31/2019    Source:sciencedirect.com

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.

We also recommend Trading Suppliers and Manufacturers of Cytidine 5'-(hydrogen sulfate) (cas 13435-43-3). Pls Click Website Link as below: cas 13435-43-3 suppliers

Prev:Human cytidine deaminase: A biochemical characterization of its naturally occurring variants
Next:Design, synthesis, and biological evaluation of new N4-Substituted 2′-deoxy-2′-fluoro-4′-azido cytidine derivatives as potent anti-HBV agents)