Journal
ACS CATALYSIS
Volume 8, Issue 8, Pages 7222-7227Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.8b01993
Keywords
sialic acid; alpha 2,6-sialyltransferase; A200Y/S232Y; sialoside; bump-hole
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Funding
- National Natural Science Foundation of China [21372130, 21672128, 81302682]
- State Key Laboratory of Microbial Technology [M2016-06]
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A beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damselae (Pd2,6ST) that is capable of sialylating both terminal and internal galactose and N-acetylgalactosamine was herein redesigned for regioselectively producing terminal a2,6-sialosides. Guided by a recently developed bump-hole strategy, a series of mutations at Ala200 and Ser232 sites were created for reshaping the acceptor binding pocket. Finally, a Pd2,6ST double mutant A200Y/S232Y with an altered L-shaped acceptor binding pocket was identified to be a superior alpha 2,6-sialyltransferase which can efficiently catalyze the regioselective alpha 2,6-sialylation of galactose or N-acetylgalactosamine at the nonreducing end of a series of glycans. Meanwhile, A200Y/S232Y remains flexible donor substrate specificity and is able to transfer Neu5Ac, Neu5Gc, and KDN.
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