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Article

Mutation Hotspot for Changing the Substrate Specificity of β-N-Acetylhexosaminidase: A Library of GlcNAcases.

International journal of molecular sciences - 18 Oct 2022

Nekvasilová Pavlína, Kulik Natalia, Kotik Michael, Petrásková Lucie, Slámová Kristýna, Křen Vladimír, Bojarová Pavla

Abstract excerpt

β-N-Acetylhexosaminidase from Talaromyces flavus (TfHex; EC 3.2.1.52) is an exo-glycosidase with dual activity for cleaving N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) units from carbohydrates. By targeting a mutation hotspot of the active site residue Glu332, we prepared a library of ten mutant variants with their substrate specificity significantly shifted towards GlcNAcase activity....

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Identifiers

PMID: 36293310
DOI: 10.3390/ijms232012456
PMCID: PMC9604439

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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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