Structural and kinetic characterisation of Trypanosoma congolense pyruvate kinase

Joar Esteban Pinto Torres; Meng Yuan; Julie Goossens; Wim Versées; Guy Caljon; Paul A. Michels; Malcolm D. Walkinshaw; Stefan Magez; Yann G.-j. Sterckx

doi:10.1016/j.molbiopara.2020.111263

Structural and kinetic characterisation of Trypanosoma congolense pyruvate kinase

Joar Esteban Pinto Torres, Meng Yuan, Julie Goossens, Wim Versées, Guy Caljon, Paul A. Michels, Malcolm D. Walkinshaw, Stefan Magez, Yann G.-j. Sterckx

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Article number	111263
Journal	Molecular and Biochemical Parasitology
Volume	236
Early online date	19 Feb 2020
DOIs	https://doi.org/10.1016/j.molbiopara.2020.111263
Publication status	E-pub ahead of print - 19 Feb 2020

Keywords

X-ray crystallography
Enzyme kinetics
Trypanosomes
glycolysis
pyruvate kinase

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10.1016/j.molbiopara.2020.111263

SterckxEtalMBP2020StructuralAndKineticCharacterisationOfTypanosomaAccepted author manuscript, 11.4 MB

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title = "Structural and kinetic characterisation of Trypanosoma congolense pyruvate kinase",

abstract = "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.",

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doi = "10.1016/j.molbiopara.2020.111263",

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TY - JOUR

T1 - Structural and kinetic characterisation of Trypanosoma congolense pyruvate kinase

AU - Pinto Torres, Joar Esteban

AU - Yuan, Meng

AU - Goossens, Julie

AU - Versées, Wim

AU - Caljon, Guy

AU - Michels, Paul A.

AU - Walkinshaw, Malcolm D.

AU - Magez, Stefan

AU - Sterckx, Yann G.-j.

PY - 2020/2/19

Y1 - 2020/2/19

N2 - 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.

AB - 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.

KW - X-ray crystallography

KW - Enzyme kinetics

KW - Trypanosomes

KW - glycolysis

KW - pyruvate kinase

U2 - 10.1016/j.molbiopara.2020.111263

DO - 10.1016/j.molbiopara.2020.111263

M3 - Article

VL - 236

JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

SN - 0166-6851

M1 - 111263

ER -

Structural and kinetic characterisation of Trypanosoma congolense pyruvate kinase

Abstract

Keywords

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