A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries |
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| Authors: | Yu Hai Chokhawala Harshal Karpel Rebekah Yu Hui Wu Bingyuan Zhang Jianbo Zhang Yingxin Jia Qiang Chen Xi |
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| Institution: | Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA. |
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| 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 alpha2,3-sialyltransferase (main function), (2) an alpha2,6-sialyltransferase, (3) an alpha2,3-sialidase, and (4) an alpha2,3-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. |
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