The main types are competitive, non-competitive, uncompetitive, and mixed inhibition.
What is competitive inhibition in enzymes?
Competitive inhibition involves an inhibitor binding to the active site of an enzyme, preventing substrate binding.
How do non-competitive inhibitors affect enzyme activity?
Non-competitive inhibitors bind to an enzyme at a site other than the active site, changing its shape and function.
Define uncompetitive inhibition.
Uncompetitive inhibition occurs when the inhibitor binds only to the enzyme-substrate complex, preventing the conversion to product.
What is mixed inhibition?
Mixed inhibition is when an inhibitor can bind to both the enzyme alone and the enzyme-substrate complex, affecting both Km and Vmax.
How can competitive inhibition be experimentally identified?
Competitive inhibition can be identified by observing an increase in Km without a change in Vmax as substrate concentration rises.
Why doesn't non-competitive inhibition affect Km?
Non-competitive inhibition does not affect Km because it does not compete with the substrate for the active site binding.
How do mixed and non-competitive inhibition differ?
Mixed inhibition impacts both Km and Vmax, while non-competitive impacts only Vmax.
What is the effect of an inhibitor on enzyme activity?
An inhibitor decreases enzyme activity by interfering with substrate binding or catalytic action.
Which type of inhibition is reversible and how?
Most enzyme inhibition types, including competitive, non-competitive, and uncompetitive, can be reversible depending on the inhibitor's compound nature.
What can cause enzyme inhibition besides inhibitors?
Factors like temperature, pH, and genetic mutations can also inhibit enzyme activity.
How are enzymes critical to biochemical reactions?