Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D-glutamate ligase (MurD).

@article{Bouhss1999RoleOT,
  title={Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D-glutamate ligase (MurD).},
  author={Ahmed Bouhss and S{\'e}bastien Dementin and Claudine Parquet and Dominique Mengin-Lecreulx and Jay A. Bertrand and Dominique Le Beller and Otto Dideberg and Jean van Heijenoort and Didier Blanot},
  journal={Biochemistry},
  year={1999},
  volume={38 38},
  pages={12240-7}
}
To evaluate their role in the active site of the UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) from Escherichia coli, 12 residues conserved either in the Mur superfamily [Eveland, S. S., Pompliano, D. L., and Anderson, M. S. (1997) Biochemistry 36, 6223-6229; Bouhss, A., Mengin-Lecreulx, D., Blanot, D., van Heijenoort, J., and Parquet, C. (1997) Biochemistry 36, 11556-11563] or in the sequences of 26 MurD orthologs were submitted to site-directed mutagenesis. All these residues lay… CONTINUE READING

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