Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base?

@article{Courtois2005EscherichiaCC,
  title={Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base?},
  author={Fabienne Courtois and Olivier Ploux},
  journal={Biochemistry},
  year={2005},
  volume={44 41},
  pages={13583-90}
}
Cyclopropane synthases catalyze the cyclopropanation of unsaturated fatty acid using S-adenosyl-L-methionine as the methylene donor. The crystal structure of three cyclopropane synthases from Mycobacterium tuberculosis showed a bicarbonate ion bound in the active site that was proposed to act as a general base in the reaction mechanism [Huang, C., Smith, V., Glickman, M. S., Jacobs, W. R., and Sacchettini, J. C. (2002) J. Biol. Chem. 277, 11559-11569]. Because the in vitro activity of M… CONTINUE READING

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