An alternative broad-specificity pathway for glycan breakdown in bacteria-Reference-Cited by-同舟云学术

An alternative broad-specificity pathway for glycan breakdown in bacteria

Published:2024-06-19 Issue:8019 Volume:631 Page:199-206
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Nasseri Seyed Amirhossein^ORCID,Lazarski Aleksander C.^ORCID,Lemmer Imke L.,Zhang Chloe Y.^ORCID,Brencher Eva^ORCID,Chen Hong-Ming,Sim Lyann,Panwar Deepesh,Betschart Leo^ORCID,Worrall Liam J.,Brumer Harry^ORCID,Strynadka Natalie C. J.^ORCID,Withers Stephen G.^ORCID

Publisher

Springer Science and Business Media LLC

Link

https://www.nature.com/articles/s41586-024-07574-y.pdf

Reference65 articles.

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3. Wolfenden, R., Lu, X. & Young, G. Spontaneous hydrolysis of glycosides. J. Am. Chem. Soc. 120, 6814–6815 (1998).

4. Watts, A. G. et al. Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile. J. Am. Chem. Soc. 125, 7532–7533 (2003).

5. Vocadlo, D. J. & Withers, S. G. Detailed comparative analysis of the catalytic mechanisms of β-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases. Biochemistry 44, 12809–12818 (2005).

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