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Article

Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides.

Proteins - 1 May 2017

Kulkarni Tejas S, Khan Samiullah, Villagomez Rodrigo, Mahmood Tahir, Lindahl Sofia, Logan Derek T, Linares-Pastén Javier A, Nordberg Karlsson Eva

Abstract excerpt

The β-glucosidase TnBgl1A catalyses hydrolysis of O-linked terminal β-glycosidic bonds at the nonreducing end of glycosides/oligosaccharides. Enzymes with this specificity have potential in lignocellulose conversion (degrading cellobiose to glucose) and conversion of bioactive flavonoids (modification of glycosylation results in modulation of bioavailability). Previous work has shown TnBgl1A to hydrolyse 3, 4'...

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Identifiers

PMID: 28142197
DOI: 10.1002/prot.25256

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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