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Article

Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.

FEBS letters - 25 Aug 2014

Schmölzer Katharina, Luley-Goedl Christiane, Czabany Tibor, Ribitsch Doris, Schwab Helmut, Weber Hansjörg, Nidetzky Bernd

Abstract excerpt

Bacterial sialyltransferases of the glycosyltransferase family GT-80 exhibit pronounced hydrolase activity toward CMP-activated sialyl donor substrates. Using in situ proton NMR, we show that hydrolysis of CMP-Neu5Ac by Pasteurella dagmatis α2,3-sialyltransferase (PdST) occurs with axial-to-equat...

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Identifiers

PMID: 24945729
DOI: 10.1016/j.febslet.2014.05.053

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24945729-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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