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VPg unlinkase is an unusual eukaryotic enzyme that catalyzes hydrolysis of the phosphodiester bond between residues of the unique tyrosine of VPg (viral protein genome-linked) and the 5"-terminal uridylic acid of picornavirus RNA. Cellular targets of the VPg unlinking enzyme are yet unknown. To determine an essential nucleic part of the covalent linkage unit that is necessary for the VPg unlinkase...
The substrate specificity of the “unlinking” enzyme from ascites carcinoma Krebs II cells has been investigated. The enzyme specifically splits the interpolymeric phosphodiester bond between Kp and the 5´-terminal phosphate group of the uridylic acid residue in the Kp–pUpUpGp complex.
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