Next Article in Journal
The Role of Lipids in Legionella-Host Interaction
Next Article in Special Issue
A Human Cellular Model for Colorectal Anastomotic Repair: The Effect of Localization and Transforming Growth Factor-β1 Treatment on Collagen Deposition and Biomarkers
Previous Article in Journal
Inflammatory Response Mechanisms of the Dentine–Pulp Complex and the Periapical Tissues
Previous Article in Special Issue
The Human Tissue-Engineered Cornea (hTEC): Recent Progress
Open AccessArticle

Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic
*
Author to whom correspondence should be addressed.
Current address: Biomedical Centre, Faculty of Medicine in Pilsen, Charles University in Prague, Alej Svobody 1655/76, 323 00 Pilsen, Czech Republic.
Academic Editor: Christophe Morisseau
Int. J. Mol. Sci. 2021, 22(3), 1483; https://doi.org/10.3390/ijms22031483
Received: 14 January 2021 / Revised: 28 January 2021 / Accepted: 29 January 2021 / Published: 2 February 2021
(This article belongs to the Collection 20th Anniversary of IJMS: Advances in Biochemistry)
Tuberculosis (TB) remains one of the major health concerns worldwide. Mycobacterium tuberculosis (Mtb), the causative agent of TB, can flexibly change its metabolic processes during different life stages. Regulation of key metabolic enzyme activities by intracellular conditions, allosteric inhibition or feedback control can effectively contribute to Mtb survival under different conditions. Phosphofructokinase (Pfk) is one of the key enzymes regulating glycolysis. Mtb encodes two Pfk isoenzymes, Pfk A/Rv3010c and Pfk B/Rv2029c, which are differently expressed upon transition to the hypoxia-induced non-replicating state of the bacteria. While pfkB gene and protein expression are upregulated under hypoxic conditions, Pfk A levels decrease. Here, we present biochemical characterization of both Pfk isoenzymes, revealing that Pfk A and Pfk B display different kinetic properties. Although the glycolytic activity of Pfk A is higher than that of Pfk B, it is markedly inhibited by an excess of both substrates (fructose-6-phosphate and ATP), reaction products (fructose-1,6-bisphosphate and ADP) and common metabolic allosteric regulators. In contrast, synthesis of fructose-1,6-bisphosphatase catalyzed by Pfk B is not regulated by higher levels of substrates, and metabolites. Importantly, we found that only Pfk B can catalyze the reverse gluconeogenic reaction. Pfk B thus can support glycolysis under conditions inhibiting Pfk A function. View Full-Text
Keywords: Mycobacterium tuberculosis; glycolysis; phosphofructokinase A and B; allosteric regulation; enzyme kinetics Mycobacterium tuberculosis; glycolysis; phosphofructokinase A and B; allosteric regulation; enzyme kinetics
Show Figures

Graphical abstract

MDPI and ACS Style

Snášel, J.; Machová, I.; Šolínová, V.; Kašička, V.; Krečmerová, M.; Pichová, I. Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation. Int. J. Mol. Sci. 2021, 22, 1483. https://doi.org/10.3390/ijms22031483

AMA Style

Snášel J, Machová I, Šolínová V, Kašička V, Krečmerová M, Pichová I. Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation. International Journal of Molecular Sciences. 2021; 22(3):1483. https://doi.org/10.3390/ijms22031483

Chicago/Turabian Style

Snášel, Jan; Machová, Iva; Šolínová, Veronika; Kašička, Václav; Krečmerová, Marcela; Pichová, Iva. 2021. "Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation" Int. J. Mol. Sci. 22, no. 3: 1483. https://doi.org/10.3390/ijms22031483

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop