How do inhibitors regulate enzymes?

Answer 1

Competitive inhibition: Where an inhibitor, which has a similar molecular shape to the enzyme's substrate, competes with substrate to fit to the enzymes active site. In the end all substrate can be broken down because the competitive inhibitors are not permanently bonded to the enzymes active site. If there is a higher concentration of substrate the amount of time it will take for all the substrate to be broken down will be less than if there is a higher concentration of inhibitor. Non-competitive inhibition: Where the inhibitor attaches itself to the enzyme at a site which is NOT the active site. This causes the enzymes shape to be changed slightly which would mean that the substrate is unable to fit to the active site. Non-competitive inhibitors do no compete with the substrate for the active site, hence their name. Non-competitive inhibitors may be permanent or not. Because the inhibitor and substrate are not competing for the same site an incrase in substrate concentration does not decrease the inhibitors effect.

Answer 2

Enzyme activity can be inhibited by both temperature and pH. Enzymes function ideally at a specified temperature. For example, human enzymes function best at a body temperature of 37°C. At temperatures that are too high or too low, the enzyme is distorted and no longer works. Similarly, if pH levels are not at the ideal level, they too become distorted and no longer work. Most human enzymes are most efficient at the neutral pH of 7.

Answer 3

You have to look at the word "inhibit". Inhibit means to prevent or hold back an action. If enzymes are biological catalysts, which work to speed up reactions at relatively low temperatures, then something that would inhibit an enzyme would decrease reaction rate. Enzyme inhibitors work by preventing the substrate (like a polypeptide) from attaching to the active site (where the reaction occurs on the enzyme).

There are competitive inhibitors and non-competitive inhibitors. Competitive inhibitors prevent the substrate from binding to the active site by simply "getting in the way". They lodge in the active site (don't necessarily have to fit perfectly) and bounce the substrate right back. Non-competitive inhibitors are not involved with the active site. They bind somewhere on the enzyme and cause the enzyme to change shape. Enzymes are very selective when choosing which substrates it will accept. This, among other factors, ensures the diversity of enzymes. Much like denaturation, the change in shape caused by the non-competitive inhibitor causes the active site to not be a perfect match for the substrate. Even if the R-groups on the enzyme line up with the positive/negative charges of the substrate, geometrically it won't work.

Answer 4

By Competitive , non competitive and uncompetitive inhibition .

Answer 5

2 major methods

Take the slot that substrate would normally bind to

Change the shape of the slot that the substrate would normally bind to