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Article

Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition.

Communications biology - 10 Jan 2020

Yang Lin, Chen Tian-Jiao, Wang Fen, Li Li, Yu Wen-Bo, Si Yi-Kang, Chen Jing-Jing, Liu Wan-Cang, Zhu Ping, Gong Weimin

Abstract excerpt

LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex...

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Identifiers

PMID: 31925310
DOI: 10.1038/s42003-019-0744-4
PMCID: PMC6954215

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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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