Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.

@article{Duangpan2010ProbingTC,
  title={Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.},
  author={Saowapa Duangpan and Sarawut Jitrapakdee and A Adina-zada and Lindsay T. Byrne and Tonya N Zeczycki and Martin St. Maurice and W. Wallace Cleland and J. C. Wallace and Paul V. Attwood},
  journal={Biochemistry},
  year={2010},
  volume={49 15},
  pages={
          3296-304
        }
}
The roles of Arg548 and Gln552 residues in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase were investigated using site-directed mutagenesis. Mutation of Arg548 to alanine or glutamine resulted in the destabilization of the quaternary structure of the enzyme, suggesting that this residue has a structural role. Mutations R548K, Q552N, and Q552A resulted in a loss of the ability to catalyze pyruvate carboxylation, biotin-dependent decarboxylation of… CONTINUE READING

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Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli

  • TN Zeczycki, M StMaurice, S Jitrapakdee, JC Wallace, PV Attwood, WW Cleland
  • Biochemistry
  • 2009

A symmetrical tetramer

  • LP Yu, S Xiang, G Lasso, D Gil, M Valle, L. Tong
  • reaction. Nat. Struct. Mol. Biol. ;25:295–302
  • 2008