Cation induced differential effect on structural and functional properties of Mycobacterium tuberculosis α-Isopropylmalate synthase
2007
Effects of Cations on Mycobacterium tuberculosis Enzyme
publication
Evidence: moderate
Author Information
Author(s): Singh Kulwant, Bhakuni Vinod
Primary Institution: Central Drug Research Institute
Hypothesis
Different cations induce varying effects on the structure and function of Mycobacterium tuberculosis α-Isopropylmalate synthase.
Conclusion
Different cations bind at different sites in the enzyme, leading to their differential effects on the structure and functional activity of the enzyme.
Supporting Evidence
- Cations induce differential effects on the secondary structure of MtαIPMS.
- Divalent cations induce significant interaction between the regulatory and catalytic domains of MtαIPMS.
- The isolated TIM barrel domain can carry out catalytic function but requires the C-terminal domain for optimum activity.
Takeaway
This study shows that different salts can change how a specific enzyme works and its shape, which is important for understanding how to fight tuberculosis.
Methodology
The study involved over-expression and purification of the enzyme, followed by functional and structural analysis using various cations.
Digital Object Identifier (DOI)
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