Initial kinetic and mechanistic characterization of Escherichia coli fumarase A.

@article{Flint1994InitialKA,
  title={Initial kinetic and mechanistic characterization of Escherichia coli fumarase A.},
  author={Dennis H. Flint},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={311 2},
  pages={509-16}
}
The protein encoded by the fumA gene in Escherichia coli is shown herein to be a highly efficient and specific catalyst of the fumarase reaction. In an investigation of 21 substrate analogs, this protein only had substantial activity as a hydro-lyase on fumarate, malate, acetylene dicarboxylate, fluorofumarate, and 2(S),3(S)-tartrate. The kcat and kcat/Km for the hydration of fumarate by this protein are 3100 s-1 and 5 x 10(6) mol-1 s-1, respectively. It is likely that one physiological role of… CONTINUE READING