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Enzyme Reaction
Enzyme-substrate complex
An enzyme-substrate complex is formed when one or more substrates interact with the active site of an enzyme. Here we have an enzyme with a unique shape. The region of this enzyme where substrate molecules bind and complete a chemical reaction is called the active site. Coming into vision are the substrates. The substrates are going to bind onto the enzyme at the active site.
Competitive Inhibition:
Similar to substrates, an inhibitor can bind noncovalently to the active site of an enzyme, but no chemical reaction will occur. This is sort of like a key that can fit in a lock but cannot turn it. When an inhibitor binds to the active site of an enzyme, the natural substrate cannot enter the active site and the enzyme is unable to function
Non Competitive Inhibition:
The difference between a competitive inhibitor and a non competitive inhibitor is that a non competitive inhibitor does not compete with the natural substrate for the active site of an enzyme. Instead, the non competitive inhibitor binds to an enzyme at a site distinct from the active site. This binding causes a change in the shape of the enzyme that alters its activity. As a result, the active site may no longer bind the substrate, or if it does, the rate of product formation may be reduced.
Allosteric Regulation:
Allosteric Regulation is very similar to non competitive inhibition. While non competitive inhibition is when an inhibitor bound to the enzyme at a site other than the active site does not allow for the substrate to bind to the active site anymore, allosteric regulation is when a non-substrate molecule also binds onto the enzyme, but now the enzyme changes its shape.
Feedback Inhibition:
Feedback inhibition is a way of regulating a metabolic pathway. The final product inhibits the enzyme that catalyzes the commitment step. When there is a high concentration of the end product, some of it binds to a site on the commitment step enzyme, causing it to become inactive. The final product may bind on to the active site on the enzyme as a competitive inhibitor, or at an all allosteric site as a noncompetitive inhibitor.
Denaturing of an enzyme:
When enzymes denature, they are no longer active and cannot function. Extreme temperature and the wrong levels of pH can cause enzymes to become denatured.
Enzyme-substrate complex
An enzyme-substrate complex is formed when one or more substrates interact with the active site of an enzyme. Here we have an enzyme with a unique shape. The region of this enzyme where substrate molecules bind and complete a chemical reaction is called the active site. Coming into vision are the substrates. The substrates are going to bind onto the enzyme at the active site.
Competitive Inhibition:
Similar to substrates, an inhibitor can bind noncovalently to the active site of an enzyme, but no chemical reaction will occur. This is sort of like a key that can fit in a lock but cannot turn it. When an inhibitor binds to the active site of an enzyme, the natural substrate cannot enter the active site and the enzyme is unable to function
Non Competitive Inhibition:
The difference between a competitive inhibitor and a non competitive inhibitor is that a non competitive inhibitor does not compete with the natural substrate for the active site of an enzyme. Instead, the non competitive inhibitor binds to an enzyme at a site distinct from the active site. This binding causes a change in the shape of the enzyme that alters its activity. As a result, the active site may no longer bind the substrate, or if it does, the rate of product formation may be reduced.
Allosteric Regulation:
Allosteric Regulation is very similar to non competitive inhibition. While non competitive inhibition is when an inhibitor bound to the enzyme at a site other than the active site does not allow for the substrate to bind to the active site anymore, allosteric regulation is when a non-substrate molecule also binds onto the enzyme, but now the enzyme changes its shape.
Feedback Inhibition:
Feedback inhibition is a way of regulating a metabolic pathway. The final product inhibits the enzyme that catalyzes the commitment step. When there is a high concentration of the end product, some of it binds to a site on the commitment step enzyme, causing it to become inactive. The final product may bind on to the active site on the enzyme as a competitive inhibitor, or at an all allosteric site as a noncompetitive inhibitor.
Denaturing of an enzyme:
When enzymes denature, they are no longer active and cannot function. Extreme temperature and the wrong levels of pH can cause enzymes to become denatured.