Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.

@article{Rangarajan2005CrystallographicTO,
  title={Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.},
  author={Erumbi S. Rangarajan and Yunge Li and Eunice Ajamian and Pietro Iannuzzi and Stephanie D Kernaghan and Marie E. Fraser and Miroslaw Cygler and Allan Matte},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 52},
  pages={42919-28}
}
Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl… CONTINUE READING

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