The contribution of syringopeptin and syringomycin to virulence of Pseudomonas syringae pv. syringae strain B301D on the basis of sypA and syrB1 biosynthesis mutant analysis.

@article{ScholzSchroeder2001TheCO,
  title={The contribution of syringopeptin and syringomycin to virulence of Pseudomonas syringae pv. syringae strain B301D on the basis of sypA and syrB1 biosynthesis mutant analysis.},
  author={Brenda K. Scholz-Schroeder and Michael L. Hutchison and Ingeborg Grgurina and Dennis C. Gross},
  journal={Molecular plant-microbe interactions : MPMI},
  year={2001},
  volume={14 3},
  pages={
          336-48
        }
}
Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this… CONTINUE READING

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