A novel structurally characterized haloacid dehalogenase superfamily phosphatase from Thermococcus thioreducens with diverse substrate specificity.
HAD superfamily
crystal structure
docking
hypothetical phosphatase
phosphatase assay
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 Aug 2019
01 Aug 2019
Historique:
received:
29
11
2018
accepted:
03
07
2019
entrez:
3
8
2019
pubmed:
3
8
2019
medline:
27
11
2019
Statut:
ppublish
Résumé
The haloacid dehalogenase (HAD) superfamily is one of the largest known groups of enzymes and the majority of its members catalyze the hydrolysis of phosphoric acid monoesters into a phosphate ion and an alcohol. Despite the fact that sequence similarity between HAD phosphatases is generally very low, the members of the family possess some characteristic features, such as a Rossmann-like fold, HAD signature motifs or the requirement for Mg
Identifiants
pubmed: 31373573
pii: S2059798319009586
doi: 10.1107/S2059798319009586
doi:
Substances chimiques
Hydrolases
EC 3.-
Phosphoric Monoester Hydrolases
EC 3.1.3.2
2-haloacid dehalogenase
EC 3.8.1.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
743-752Subventions
Organisme : Grantová Agentura České Republiky
ID : 17-24321S
Organisme : Jihočeská Univerzita v Českých Budějovicích
ID : GAJU 04-149/2016/P