Study of Phosphofructokinase from Setaria cervi
Author Information
Author(s): Bechan Sharma
Primary Institution: University of Allahabad
Hypothesis
The kinetic properties of phosphofructokinase (PFK) from Setaria cervi differ from those of vertebrates, suggesting adaptation to anaerobic metabolism.
Conclusion
The study found that the phosphofructokinase from Setaria cervi exhibits unique allosteric properties and is inhibited by ATP, indicating its adaptation to anaerobic conditions.
Supporting Evidence
- The K_m values for F-6-P and ATP were found to be 1.05 mM and 3 μM, respectively.
- The enzyme exhibited sigmoidal kinetics at higher ATP concentrations.
- Product inhibition studies indicated competitive inhibition by FDP and PEP.
Takeaway
This study looks at an enzyme from a type of worm that helps it get energy. The enzyme works differently than similar ones in other animals, which helps the worm survive in low-oxygen places.
Methodology
The enzyme was purified and characterized using steady state kinetic methods, measuring its activity with various substrates and inhibitors.
Limitations
The study primarily focuses on a single enzyme from one species, which may limit the generalizability of the findings.
Digital Object Identifier (DOI)
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