X-ray crystallographic structural studies of α-amylase I from Eisenia fetida.
Eisenia fetida
amylase
cold-active enzymes
glycine-rich loop
structural flexibility
substrate complex
substrate recognition
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Sep 2020
01 Sep 2020
Historique:
received:
09
03
2020
accepted:
23
07
2020
entrez:
3
9
2020
pubmed:
3
9
2020
medline:
10
7
2021
Statut:
ppublish
Résumé
The earthworm Eisenia fetida possesses several cold-active enzymes, including α-amylase, β-glucanase and β-mannanase. E. fetida possesses two isoforms of α-amylase (Ef-Amy I and II) to digest raw starch. Ef-Amy I retains its catalytic activity at temperatures below 10°C. To identify the molecular properties of Ef-Amy I, X-ray crystal structures were determined of the wild type and of the inactive E249Q mutant. Ef-Amy I has structural similarities to mammalian α-amylases, including the porcine pancreatic and human pancreatic α-amylases. Structural comparisons of the overall structures as well as of the Ca
Identifiants
pubmed: 32876059
pii: S2059798320010165
doi: 10.1107/S2059798320010165
doi:
Substances chimiques
alpha-Amylases
EC 3.2.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
834-844Subventions
Organisme : Japan Society for the Promotion of Science
ID : 19H03090
Organisme : Japan Society for the Promotion of Science
ID : 16K08116