| Literature DB >> 16351087 |
Hai Yu1, Harshal Chokhawala, Rebekah Karpel, Hui Yu, Bingyuan Wu, Jianbo Zhang, Yingxin Zhang, Qiang Jia, Xi Chen.
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.Entities:
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Year: 2005 PMID： 16351087 DOI： 10.1021/ja0561690
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419