Simulation · Biology · Class 11
Malonate against succinate
From the lesson Factors affecting enzyme activity in Biomolecules. Change the values and watch what happens.
Malonate against succinateBiology · Class 11
The idea behind it
NCERT §9.8.4
- Conditions that alter a protein's tertiary structure change enzyme activity: temperature, pH, substrate concentration, and the binding of specific chemicals that regulate it.
- Enzymes work within a narrow range of temperature and pH. Each shows its highest activity at an optimum temperature and an optimum pH, and activity falls on either side of the optimum.
- Low temperature keeps an enzyme temporarily inactive, while high temperature destroys its activity because heat denatures proteins.
- As substrate concentration rises, reaction velocity rises at first and then levels off at a maximum velocity (Vmax) that more substrate cannot exceed. There are fewer enzyme molecules than substrate molecules, and once all are occupied no free enzyme is left for the extra substrate.
- When a chemical that binds to the enzyme shuts off its activity, the process is inhibition and the chemical is an inhibitor.
- A competitive inhibitor closely resembles the substrate and competes with it for the substrate-binding site, so the substrate cannot bind and activity falls. Malonate inhibits succinic dehydrogenase because it closely resembles the substrate, succinate.
- Competitive inhibitors are often used to control bacterial pathogens.