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Article

A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating LewisX.

ACS chemical biology - 20 Jul 2012

Sugiarto Go, Lau Kam, Qu Jingyao, Li Yanhong, Lim Sunghyuk, Mu Shengmao, Ames James B, Fisher Andrew J, Chen Xi

Abstract excerpt

Glycosyltransferases are important catalysts for enzymatic and chemoenzymatic synthesis of complex carbohydrates and glycoconjugates. The glycosylation efficiencies of wild-type glycosyltransferases vary considerably when different acceptor substrates are used. Using a multifunctional Pasteurella multocida sialyltransferase 1 (PmST1) as an example, we show here that the sugar nucleotide donor hydrolysis activity...

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Identifiers

PMID: 22583967
DOI: 10.1021/cb300125k
PMCID: PMC3521065

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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