Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.
EaFAH
Exiguobacterium antarcticum
Fumarylacetoacetate hydrolase
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
12 02 2019
12 02 2019
Historique:
received:
26
12
2018
accepted:
30
12
2018
pubmed:
12
1
2019
medline:
5
11
2019
entrez:
12
1
2019
Statut:
ppublish
Résumé
Fumarylacetoacetate hydrolase (FAH) is essential for the degradation of aromatic amino acids as well as for the cleavage of carbon-carbon bonds in metabolites or small organic compounds. Here, the X-ray crystal structure of EaFAH, a dimeric fumarylacetoacetate hydrolase from Exiguobacterium antarcticum, was determined, and its functional properties were investigated using biochemical methods. EaFAH adopts a mixed β-sandwich roll fold with a highly flexible lid region (Val
Identifiants
pubmed: 30630595
pii: S0006-291X(18)32870-5
doi: 10.1016/j.bbrc.2018.12.183
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Hydrolases
EC 3.-
fumarylacetoacetase
EC 3.7.1.2
Magnesium
I38ZP9992A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
773-778Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.