An α2,3-Sialyltransferase from Photobacterium phosphoreum with Broad Substrate Scope: Controlling Hydrolytic Activity by Directed Evolution.
biocatalysis
carbohydrates
enzyme promiscuity
protein engineering
sialoconjugates
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
04 Sep 2020
04 Sep 2020
Historique:
received:
07
05
2020
pubmed:
1
7
2020
medline:
2
3
2021
entrez:
30
6
2020
Statut:
ppublish
Résumé
Defined sialoglycoconjugates are important molecular probes for studying the role of sialylated glycans in biological systems. We show that the α2,3-sialyltransferase from Photobacterium phosphoreum JT-ISH-467 (2,3SiaT
Identifiants
pubmed: 32596832
doi: 10.1002/chem.202002277
pmc: PMC7540698
doi:
Substances chimiques
Sialyltransferases
EC 2.4.99.-
N-Acetylneuraminic Acid
GZP2782OP0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
11614-11624Informations de copyright
© 2020 The Authors. Published by Wiley-VCH GmbH.
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