A Conserved Acidic Motif Is Crucial for Enzymatic Activity of Protein O-Mannosyltransferases*

@article{Lommel2011ACA,
  title={A Conserved Acidic Motif Is Crucial for Enzymatic Activity of Protein O-Mannosyltransferases*},
  author={Mark Lommel and Andrea Schott and Thomas Jank and Verena Simone Hofmann and Sabine Strahl},
  journal={The Journal of Biological Chemistry},
  year={2011},
  volume={286},
  pages={39768 - 39775}
}
Background: Dimerization is a prerequisite for protein O-mannosyltransferase activity. Results: Transferase activity depends on an intact Asp-Glu motif located in a region crucial for acceptor binding/catalysis in both complex partners. Conclusion: Complex formation leads to the assembly of a composite catalytic center. Significance: Defining the role of complex formation is crucial for understanding the catalytic mechanism of protein O-mannosyltransferases. Protein O-mannosylation is an… 

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