Dispensability of glutamic acid 48 and aspartic acid 134 for Mn2+-dependent activity of Escherichia coli ribonuclease HI.

@article{Tsunaka2003DispensabilityOG,
  title={Dispensability of glutamic acid 48 and aspartic acid 134 for Mn2+-dependent activity of Escherichia coli ribonuclease HI.},
  author={Yasuo Tsunaka and Mitsuru Haruki and Masaaki Morikawa and Motohisa Oobatake and Shigenori Kanaya},
  journal={Biochemistry},
  year={2003},
  volume={42 11},
  pages={3366-74}
}
The activities of the eight mutant proteins of Escherichia coli RNase HI, in which the four carboxylic amino acids (Asp(10), Glu(48), Asp(70), and Asp(134)) involved in catalysis are changed to Asn (Gln) or Ala, were examined in the presence of Mn(2+). Of these proteins, the E48A, E48Q, D134A, and D134N proteins exhibited the activity, indicating that Glu… CONTINUE READING