Rutinosidase from Aspergillus niger: crystal structure and insight into the enzymatic activity.
SIRAS
X-ray crystallography
catalytic mechanism
diglycosidase
rutin
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
25
09
2019
revised:
13
12
2019
accepted:
09
01
2020
pubmed:
17
1
2020
medline:
14
5
2021
entrez:
17
1
2020
Statut:
ppublish
Résumé
Rutinosidases (α-l-rhamnosyl-β-d-glucosidases) catalyze the cleavage of the glycosidic bond between the aglycone and the disaccharide rutinose (α-l-rhamnopyranosyl-(1→6)-β-d-glucopyranose) of specific flavonoid glycosides such as rutin (quercetin 3-O-rutinoside). Microbial rutinosidases are part of the rutin catabolic pathway, enabling the microorganism to utilize rutin and related plant phenolic glycosides. Here, we report the first three-dimensional structure of a rutinosidase determined at 1.27-Å resolution. The rutinosidase from Aspergillus niger K2 (AnRut), a member of glycoside hydrolase family GH-5, subfamily 23, was heterologously produced in Pichia pastoris. The X-ray structure of AnRut is represented by a distorted (β/α)
Substances chimiques
Fungal Proteins
0
Rutin
5G06TVY3R7
Glycoside Hydrolases
EC 3.2.1.-
Banques de données
GENBANK
['MN393234']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3315-3327Informations de copyright
© 2020 Federation of European Biochemical Societies.
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