Crystal Structure of α-Xylosidase from
Journal
ACS sustainable chemistry & engineering
ISSN: 2168-0485
Titre abrégé: ACS Sustain Chem Eng
Pays: United States
ID NLM: 101608852
Informations de publication
Date de publication:
17 Feb 2020
17 Feb 2020
Historique:
received:
02
12
2019
revised:
16
01
2020
entrez:
13
3
2020
pubmed:
13
3
2020
medline:
13
3
2020
Statut:
ppublish
Résumé
Glycoside hydrolase family 31 (GH31) enzymes show both highly conserved folds and catalytic residues. Yet different members of GH31 show very different substrate specificities, and it is not obvious how these specificities arise from the protein sequences. The fungal α-xylosidase, AxlA, was originally isolated from a commercial enzyme mixture secreted by
Identifiants
pubmed: 32161692
doi: 10.1021/acssuschemeng.9b07073
pmc: PMC7059301
doi:
Types de publication
Journal Article
Langues
eng
Pagination
2540-2547Informations de copyright
Copyright © 2020 American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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