4.6 Article

Structural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuni

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JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 41, 页码 35922-35932

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ELSEVIER
DOI: 10.1074/jbc.M111.261172

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  1. Canadian Institutes of Health Research
  2. Howard Hughes Medical Institute
  3. Michael Smith Foundation for Health Research
  4. Canada Foundation for Innovation
  5. B.C. Knowledge Development Fund
  6. Kwanjeong Educational Foundation (Republic of Korea)
  7. University of British Columbia

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Background: The transfer of sialic acids is catalyzed by a set of sialyltransferases with defined specificities. Results: We solved the ternary complex of the sialyltransferase Cst-II and kinetically characterized its mechanism. Conclusion: Our analysis gives insights into the acceptor specificity and proposes the iso-ordered Bi Bi mechanism. Significance: This work improves our understanding of sialyltransferase structure/function.

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