Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains.

@article{Yonus2008CrystalSO,
  title={Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains.},
  author={Huma Yonus and Piotr Neumann and Stephan Zimmermann and J{\"u}rgen J. May and Mohamed A. Marahiel and Milton T Stubbs},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 47},
  pages={32484-91}
}
DltA, the D-alanine:D-alanyl carrier protein ligase responsible for the initial step of lipoteichoic acid D-alanylation in Gram-positive bacteria, belongs to the adenylation domain superfamily, which also includes acetyl-CoA synthetase and the adenylation domains of non-ribosomal synthetases. The two-step reaction catalyzed by these enzymes (substrate adenylation followed by transfer to the reactive thiol group of CoA or the phosphopantheinyl prosthetic group of peptidyl carrier proteins) has… CONTINUE READING
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