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Redox-Controlled Site-Specific ?2-6-Sialylation.

ABSTRACT: The first bacterial ?2-6-sialyltransferase cloned from Photobacterium damselae (Pd2,6ST) has been widely applied for the synthesis of various ?2-6-linked sialosides. However, the extreme substrate flexibility of Pd2,6ST makes it unsuitable for site-specific ?2-6-sialylation of complex substrates containing multiple galactose and/or N-acetylgalactosamine units. To tackle this problem, a general redox-controlled site-specific sialylation strategy using Pd2,6ST is described. This approach features site-specific enzymatic oxidation of galactose units to mask the unwanted sialylation sites and precisely controlling the site-specific ?2-6-sialylation at intact galactose or N-acetylgalactosamine units.

SUBMITTER: Lu N

PROVIDER: S-EPMC7239639 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Redox-Controlled Site-Specific α2-6-Sialylation.

Lu Na N Ye Jinfeng J Cheng Jiansong J Sasmal Aniruddha A Liu Chang-Cheng CC Yao Wenlong W Yan Jun J Khan Naazneen N Yi Wen W Varki Ajit A Cao Hongzhi H

Journal of the American Chemical Society 20190311 11

The first bacterial α2-6-sialyltransferase cloned from Photobacterium damselae (Pd2,6ST) has been widely applied for the synthesis of various α2-6-linked sialosides. However, the extreme substrate flexibility of Pd2,6ST makes it unsuitable for site-specific α2-6-sialylation of complex substrates containing multiple galactose and/or N-acetylgalactosamine units. To tackle this problem, a general redox-controlled site-specific sialylation strategy using Pd2,6ST is described. This approach features ...[more]

PMID: 30843692

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