ArticleBioscience reports2023
Expression and characterisation of human glycerol kinase: the role of solubilising agents and molecular chaperones.
Article in Bioscience reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Hologenomics Reveals Specialized Dietary Adaptations in the Mengla Snail-Eating Snake.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Biochemical properties of glycerol kinase from the hypersaline-adapted archaeonApplied and environmental microbiology · 2025Article
- Functional and Biochemical Analyses of Glycerol Kinase and Glycerol 3-phosphate Dehydrogenase in HEK293 Cells.The protein journal · 2025Article
- TRIP6 a potential diagnostic marker for colorectal cancer with glycolysis and immune infiltration association.Scientific reports · 2024Article
- Glycylglycine promotes the solubility and antigenic utility of recombinant HCV structural proteins in a point-of-care immunoassay for detection of active viremia.Microbial cell factories · 2024Article
- Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent.Current issues in molecular biology · 2024Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundGlycerol kinase (GK; EC 2.7.1.30) facilitates the entry of glycerol into pathways of glucose and triglyceride metabolism and may play a potential role in Type 2 diabetes mellitus (T2DM). However, the detailed regulatory mechanisms and structure of the human GK are unknown.
methodsThe human GK gene was cloned into the pET-24a(+) vector and over-expressed in Escherichia coli BL21 (DE3). Since the protein was expressed as inclusion bodies (IBs), various culture parameters and solubilising agents were used but they did not produce bioactive His-GK; however, co-expression of His-GK with molecular chaperones, specifically pKJE7, achieved expression of bioactive His-GK. The overexpressed bioactive His-GK was purified using coloumn chromatography and characterised using enzyme kinetics.
resultsThe overexpressed bioactive His-GK was purified apparently to homogeneity (∼295-fold) and characterised. The native His-GK was a dimer with a monomeric molecular weight of ∼55 kDa. Optimal enzyme activity was observed in TEA buffer (50 mM) at 7.5 pH. K+ (40 mM) and Mg2+ (2.0 mM) emerged as prefered metal ions for His-GK activity with specific activity 0.780 U/mg protein. The purified His-GK obeyed standard Michaelis-Menten kinetics with Km value of 5.022 µM (R2=0.927) for its substrate glycerol; whereas, that for ATP and PEP was 0.767 mM (R2=0.928) and 0.223 mM (R2=0.967), respectively. Other optimal parameters for the substrate and co-factors were also determined.
conclusionThe present study demonstrates that co-expression of molecular chaperones assists with the expression of bioactive human GK for its characterisation.
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