DNA topoisomerase I from Mycobacterium smegmatis. An enzyme with distinct features.

@article{Bhaduri1998DNATI,
  title={DNA topoisomerase I from Mycobacterium smegmatis. An enzyme with distinct features.},
  author={T. J. Bhaduri and T K Bagui and D Sikder and Valakunja Nagaraja},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 22},
  pages={13925-32}
}
A type I topoisomerase has been purified to homogeneity from Mycobacterium smegmatis. It is the largest single subunit enzyme of this class having molecular mass of 110 kDa. The enzyme is Mg2+ dependent and can relax negatively supercoiled DNA, catenate, and knot single-stranded DNA, thus having typical properties of type I topoisomerases. Furthermore, the enzyme makes single-stranded nicks and the 5'-phosphoryl end of the nicked DNA gets covalently linked with a tyrosine residue of the enzyme… CONTINUE READING

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