Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.
Enzyme kinetics
Glycolysis
Pyruvate kinase
Trypanosomes
X-ray crystallography
Journal
Molecular and biochemical parasitology
ISSN: 1872-9428
Titre abrégé: Mol Biochem Parasitol
Pays: Netherlands
ID NLM: 8006324
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
01
12
2019
revised:
13
01
2020
accepted:
29
01
2020
pubmed:
23
2
2020
medline:
12
1
2021
entrez:
22
2
2020
Statut:
ppublish
Résumé
Trypanosoma are blood-borne parasites and are the causative agents of neglected tropical diseases (NTDs) affecting both humans and animals. These parasites mainly rely on glycolysis for their energy production within the mammalian host, which is why trypanosomal glycolytic enzymes have been pursued as interesting targets for the development of trypanocidal drugs. The structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania) have been well-studied within this context. In this paper, we describe the structural and enzymatic characterization of PYK from T. congolense (TcoPYK), the main causative agent of Animal African Trypanosomosis (AAT), by employing a combination of enzymatic assays, thermal unfolding studies and X-ray crystallography.
Identifiants
pubmed: 32084384
pii: S0166-6851(19)30179-3
doi: 10.1016/j.molbiopara.2020.111263
pii:
doi:
Substances chimiques
Protozoan Proteins
0
Pyruvate Kinase
EC 2.7.1.40
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
111263Subventions
Organisme : Medical Research Council
ID : MC_PC_16043
Pays : United Kingdom
Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.