A single amino acid change is responsible for evolution of acyltransferase specificity in bacterial methionine biosynthesis.

@article{Zubieta2008ASA,
  title={A single amino acid change is responsible for evolution of acyltransferase specificity in bacterial methionine biosynthesis.},
  author={Chloe Zubieta and Kiani A J Arkus and Rebecca E Cahoon and Joseph M Jez},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 12},
  pages={7561-7}
}
Bacteria and yeast rely on either homoserine transsuccinylase (HTS, metA) or homoserine transacetylase (HTA; met2) for the biosynthesis of methionine. Although HTS and HTA catalyze similar chemical reactions, these proteins are typically unrelated in both sequence and three-dimensional structure. Here we present the 2.0 A resolution x-ray crystal structure of the Bacillus cereus metA protein in complex with homoserine, which provides the first view of a ligand bound to either HTA or HTS… CONTINUE READING