作者: M Gupta , C.X. Zhu , Y.C. Tse-Dinh
DOI: 10.1016/S0021-9258(18)35746-6
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摘要: Although highly homologous to the other eukaryotic type I DNA topoisomerases, vaccinia virus topoisomerase is distinct in its resistance anti-cancer drug camptothecin. After comparison of available sequences sensitive and resistant aspartic acid at position 221 mutated a valine. The resulting mutant protein partially active. In contrast wild enzyme, relaxation supercoiled inhibited by Its cleavage reaction with enhanced camptothecin due inhibition religation DNA. This demonstrates that even though size only about one-third camptothecin-sensitive it has potential interaction site for