Journal
MOLECULAR BIOSYSTEMS
Volume 7, Issue 11, Pages 3021-3027Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1mb05182b
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Funding
- NSF [CHE1012511]
- NIH [R01GM076360, R01HD065122]
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [R01HD065122] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM076360] Funding Source: NIH RePORTER
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Pasteurella multocida alpha 2-3-sialyltransferase 1 (PmST1) is a multifunctional enzyme which has alpha 2-6-sialyltransferase, alpha 2-3-sialidase, and alpha 2-3-trans-sialidase activities in addition to its major alpha 2-3-sialyltransferase activity. The presence of the alpha 2-3-sialidase activity of PmST1 complicates its application in enzymatic synthesis of alpha 2-3-linked sialosides as the product formed can be hydrolyzed by the enzyme. Herein we show that the alpha 2-3-sialidase activity of PmST1 can be significantly decreased by protein crystal structure-based site-directed mutagenesis. A PmST1 double mutant E271F/R313Y showed a significantly (6333-fold) decreased sialidase activity without affecting its alpha 2-3-sialyltransferase activity. The double mutant E271F/R313Y, therefore, is a superior enzyme for enzymatic synthesis of alpha 2-3-linked sialosides.
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