A Multifunctional Pasteurella multocida Sialyltransferase: A Powerful Tool for the Synthesis of Sialoside Libraries
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- 作者：Hai Yu ; Harshal Chokhawala ; Rebekah Karpel ; Hui Yu ; Bingyuan Wu ; Jianbo Zhang ; Yingxin Zhang ; Qiang Jia ; and Xi Chen
- 刊名：Journal of the American Chemical Society
- 出版年：2005
- 出版时间：December 21, 2005
- 年：2005
- 卷：127
- 期：50
- 页码：17618 - 17619
- 全文大小：89K
- 年卷期：v.127,no.50(December 21, 2005)
- ISSN：1520-5126
文摘
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 
2,3-sialyltransferase (main function), (2) an 2,6-sialyltransferase, (3) an 2,3-sialidase, and (4) an 2,3-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.
2,3-sialyltransferase (main function), (2) an 2,6-sialyltransferase, (3) an 2,3-sialidase, and (4) an 2,3-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.