Aspergillus oryzae α-l-rhamnosidase: Crystal structure and insight into the substrate specificity.
Aspergillus oryzae
N-glycosylation
Pichia pastoris
crystal structure
substrate specificity
α-l-rhamnosidase
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
11 Oct 2023
11 Oct 2023
Historique:
revised:
16
09
2023
received:
10
07
2023
accepted:
28
09
2023
medline:
11
10
2023
pubmed:
11
10
2023
entrez:
11
10
2023
Statut:
aheadofprint
Résumé
The subsequent biochemical and structural investigations of the purified recombinant α-l-rhamnosidase from Aspergillus oryzae expressed in Pichia pastoris, designated as rAoRhaA, were performed. The specific activity of the rAoRhaA wild-type was higher toward hesperidin and narirutin, where the l-rhamnose residue was α-1,6-linked to β-d-glucoside, than toward neohesperidin and naringin with an α-1,2-linkage to β-d-glucoside. However, no activity was detected toward quercitrin, myricitrin, and epimedin C. rAoRhaA kinetic analysis indicated that K
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : YU-COE Program of Yamagata University
Organisme : JSPS KAKENHI
ID : 22H01873
Informations de copyright
© 2023 Wiley Periodicals LLC.
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