Chakraborty A K, Majumder H K
Molecular Parasitology Laboratory, Indian Institute of Chemical Biology, Calcutta.
Mol Biochem Parasitol. 1987 Dec;26(3):215-24. doi: 10.1016/0166-6851(87)90074-0.
An enzyme from Leishmania donovani that decatenates kinetoplast DNA networks into covalently closed monomeric circles has been isolated and characterized. The enzyme also relaxes supercoiled plasmid pBR322. The decatenation and relaxation reactions both require ATP and Mg2+. In both reactions the formation of topological isomers of unique linking numbers suggests that the enzyme is a type II DNA topoisomerase. Both the relaxation and decatenating activities are inhibited by novobiocin at a very high concentration.
已分离并鉴定出一种来自杜氏利什曼原虫的酶，该酶可将动质体DNA网络解连环成共价闭合的单体环。该酶还能使超螺旋质粒pBR322松弛。解连环反应和松弛反应均需要ATP和Mg2+。在这两种反应中，具有独特连接数的拓扑异构体的形成表明该酶是一种II型DNA拓扑异构酶。松弛活性和解连环活性在非常高的新霉素浓度下均受到抑制。
