X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.

@article{Jozic2003XraySO,
  title={X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.},
  author={Daniela Jozic and Jens T. Kaiser and Robert Huber and Wolfram Bode and Klaus Maskos},
  journal={Journal of molecular biology},
  year={2003},
  volume={332 1},
  pages={243-56}
}
L-aspartyl and L-asparaginyl residues in proteins spontaneously undergo intra-residue rearrangements forming isoaspartyl/beta-aspartyl residues linked through their side-chain beta-carboxyl group with the following amino acid. In order to avoid accumulation of isoaspartyl dipeptides left over from protein degradation, some bacteria have developed specialized isoaspartyl/beta-aspartyl zinc dipeptidases sequentially unrelated to other peptidases, which also poorly degrade alpha-aspartyl… CONTINUE READING
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