A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries

Hai Yu, Harshal Chokhawala, Rebekah Karpel, Hui Yu, Bingyuan Wu, Jianbo Zhang, Yingxin Zhang, Qiang Jia, Xi Chen

Research output: Contribution to journalArticle

224 Scopus citations

Abstract

A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an α2,3-sialyltransferase (main function), (2) an α2,6-sialyltransferase, (3) an α2,3-sialidase, and (4) an α2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

Original languageEnglish (US)
Pages (from-to)17618-17619
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number50
DOIs
StatePublished - Dec 21 2005

ASJC Scopus subject areas

  • Chemistry(all)

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