A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries - PubMed (original) (raw)
. 2005 Dec 21;127(50):17618-9.
doi: 10.1021/ja0561690.
Affiliations
- PMID: 16351087
- DOI: 10.1021/ja0561690
A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries
Hai Yu et al. J Am Chem Soc. 2005.
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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