A novel structurally characterized haloacid dehalogenase superfamily phosphatase from Thermococcus thioreducens with diverse substrate specificity.


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
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

743-752

Subventions

Organisme : Grantová Agentura České Republiky
ID : 17-24321S
Organisme : Jihočeská Univerzita v Českých Budějovicích
ID : GAJU 04-149/2016/P

Auteurs

Petra Havlickova (P)

Institute of Chemistry, Faculty of Science, University of South Bohemia, Branisovska 1760, CZ-370 05 Ceske Budejovice, Czech Republic.

Vitezslav Brinsa (V)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, CZ-166 10 Prague, Czech Republic.

Jiri Brynda (J)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, CZ-166 10 Prague, Czech Republic.

Petr Pachl (P)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, CZ-166 10 Prague, Czech Republic.

Tatyana Prudnikova (T)

Institute of Chemistry, Faculty of Science, University of South Bohemia, Branisovska 1760, CZ-370 05 Ceske Budejovice, Czech Republic.

Jeroen R Mesters (JR)

Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany.

Barbora Kascakova (B)

Institute of Chemistry, Faculty of Science, University of South Bohemia, Branisovska 1760, CZ-370 05 Ceske Budejovice, Czech Republic.

Michal Kuty (M)

Institute of Chemistry, Faculty of Science, University of South Bohemia, Branisovska 1760, CZ-370 05 Ceske Budejovice, Czech Republic.

Marc L Pusey (ML)

Department of Biologial Sciences, University of Alabama in Huntsville, 301 Sparkman Drive, Huntsville, AL 35899, USA.

Joseph D Ng (JD)

Department of Biologial Sciences, University of Alabama in Huntsville, 301 Sparkman Drive, Huntsville, AL 35899, USA.

Pavlina Rezacova (P)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, CZ-166 10 Prague, Czech Republic.

Ivana Kuta Smatanova (I)

Institute of Chemistry, Faculty of Science, University of South Bohemia, Branisovska 1760, CZ-370 05 Ceske Budejovice, Czech Republic.

Articles similaires

alpha-Synuclein Humans Animals Mice Lewy Body Disease
Adenosine Triphosphate Adenosine Diphosphate Mitochondrial ADP, ATP Translocases Binding Sites Mitochondria

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics

Classifications MeSH