ArticleEukaryotic cell2006
Activity of a second Trypanosoma brucei hexokinase is controlled by an 18-amino-acid C-terminal tail.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Post-transcriptional reprogramming by thousands of mRNA untranslated regions in trypanosomes.Nature communications · 2024Article
- FP-MAP: an extensive library of fingerprint-based molecular activity prediction tools.Frontiers in chemistry · 2023Article
- Characterization of Glucokinases from Pathogenic Free-Living Amoebae.Antimicrobial agents and chemotherapy · 2022Article
- Nucleotide sugar biosynthesis occurs in the glycosomes of procyclic and bloodstream form Trypanosoma brucei.PLoS neglected tropical diseases · 2021Article
- Glucose Utilization in the Regulation of Chitin Synthesis in Brown Planthopper.Journal of insect science (Online) · 2019Article
- Enzymatic and Structural Characterization of theAntimicrobial agents and chemotherapy · 2019Article
- Heterologous overexpression of active hexokinases from microsporidia Nosema bombycis and Nosema ceranae confirms their ability to phosphorylate host glucose.Parasitology research · 2019Article
- Glucose Signaling Is Important for Nutrient Adaptation during Differentiation of Pleomorphic African Trypanosomes.mSphere · 2018Article
- A FRET flow cytometry method for monitoring cytosolic and glycosomal glucose in living kinetoplastid parasites.PLoS neglected tropical diseases · 2018Article
- Optimization and Evaluation of Antiparasitic Benzamidobenzoic Acids as Inhibitors of Kinetoplastid Hexokinase 1.ChemMedChem · 2017Article
- Molecular and biochemical characterization of Eimeria tenella hexokinase.Parasitology research · 2016Article
- Exploring the mode of action of ebselen in Trypanosoma brucei hexokinase inhibition.International journal for parasitology. Drugs and drug resistance · 2013Article
- Interrogating a hexokinase-selected small-molecule library for inhibitors of Plasmodium falciparum hexokinase.Antimicrobial agents and chemotherapy · 2013Article
- Environmentally regulated glycosome protein composition in the African trypanosome.Eukaryotic cell · 2013Article
- Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2.International journal for parasitology · 2012Article
- Glycerol 3-phosphate alters Trypanosoma brucei hexokinase activity in response to environmental change.The Journal of biological chemistry · 2011Article
- Quercetin, a fluorescent bioflavanoid, inhibits Trypanosoma brucei hexokinase 1.Experimental parasitology · 2011Article
- Glycolysis in the african trypanosome: targeting enzymes and their subcellular compartments for therapeutic development.Molecular biology international · 2011Article
- State of the art in African trypanosome drug discovery.Current topics in medicinal chemistry · 2011Review
- A target-based high throughput screen yields Trypanosoma brucei hexokinase small molecule inhibitors with antiparasitic activity.PLoS neglected tropical diseases · 2010Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trypanosoma brucei expresses two hexokinases that are 98% identical, namely, TbHK1 and TbHK2. Homozygous null TbHK2-/- procyclic-form parasites exhibit an increased doubling time, a change in cell morphology, and, surprisingly, a twofold increase in cellular hexokinase activity. Recombinant TbHK1 enzymatic activity is similar to that of other hexokinases, with apparent Km values for glucose and ATP of 0.09 +/- 0.02 mM and 0.28 +/- 0.1 mM, respectively. The k(cat) value for TbHK1 is 2.9 x 10(4) min(-1). TbHK1 can use mannose, fructose, 2-deoxyglucose, and glucosamine as substrates. In addition, TbHK1 is inhibited by fatty acids, with lauric, myristic, and palmitic acids being the most potent (with 50% inhibitory concentrations of 75.8, 78.4, and 62.4 microM, respectively). In contrast to TbHK1, recombinant TbHK2 lacks detectable enzymatic activity. Seven of the 10 amino acid differences between TbHK1 and TbHK2 lie within the C-terminal 18 amino acids of the polypeptides. Modeling of the proteins maps the C-terminal tails near the interdomain cleft of the enzyme that participates in the conformational change of the enzyme upon substrate binding. Replacing the last 18 amino acids of TbHK2 with the corresponding residues of TbHK1 yields an active recombinant protein with kinetic properties similar to those of TbHK1. Conversely, replacing the C-terminal tail of TbHK1 with the TbHK2 tail inactivates the enzyme. These findings suggest that the C-terminal tail of TbHK1 is important for hexokinase activity. The altered C-terminal tail of TbHK2, along with the phenotype of the knockout parasites, suggests a distinct function for the protein.
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