0% found this document useful (0 votes)
197 views3 pages

Introduction To Enzymes

Enzyme inhibitors alter the catalytic action of enzymes and slow down or stop catalysis. There are three main types of inhibition: competitive, non-competitive, and substrate inhibition. Competitive inhibition occurs when a substrate and inhibitor resembling the substrate compete for the enzyme's active site. The lock and key theory explains this as the inhibitor occupies the active site but cannot open the lock to start the reaction. Non-competitive inhibitors alter the enzyme so it cannot accept the substrate. Substrate inhibition can occur with excessive substrate, which blocks active sites and prevents reaction.

Uploaded by

Yohan_N
Copyright
© Attribution Non-Commercial (BY-NC)
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
0% found this document useful (0 votes)
197 views3 pages

Introduction To Enzymes

Enzyme inhibitors alter the catalytic action of enzymes and slow down or stop catalysis. There are three main types of inhibition: competitive, non-competitive, and substrate inhibition. Competitive inhibition occurs when a substrate and inhibitor resembling the substrate compete for the enzyme's active site. The lock and key theory explains this as the inhibitor occupies the active site but cannot open the lock to start the reaction. Non-competitive inhibitors alter the enzyme so it cannot accept the substrate. Substrate inhibition can occur with excessive substrate, which blocks active sites and prevents reaction.

Uploaded by

Yohan_N
Copyright
© Attribution Non-Commercial (BY-NC)
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
You are on page 1/ 3

Introduction to Enzymes

The following has been excerpted from a very popular Worthington publication which was originally published in 1972 as the Manual of Clinical Enzyme Measurements. While some of the presentation may seem somewhat dated, the basic concepts are still helpful for researchers who must use enzymes but who have little background in enzymology. Effects of Inhibitors on Enzyme Activity
Enzyme inhibitors are substances which alter the catalytic action of the enzyme and consequently slow down, or in some cases, stop catalysis. There are three common types of enzyme inhibition - competitive, non-competitive and substrate inhibition. Most theories concerning inhibition mechanisms are based on the existence of the enzymesubstrate complex ES. As mentioned earlier, the existence of temporary ES structures has been verified in the laboratory. Competitive inhibition occurs when the substrate and a substance resembling the substrate are both added to the enzyme. A theory called the "lock-key theory" of enzyme catalysts can be used to explain why inhibition occurs.

The lock and key theory utilizes the concept of an "active site." The concept holds that one particular portion of the enzyme surface has a strong affinity for the substrate. The substrate is held in such a way that its conversion to the reaction products is more favorable. If we consider the enzyme as the lock and the substrate the key (Figure 9) - the key is inserted in the lock, is turned, and the door is opened and the reaction proceeds. However, when an inhibitor which resembles the substrate is present, it will compete with the substrate for the position in the enzyme lock. When the inhibitor wins, it gains the lock position but is unable to open the lock. Hence, the observed reaction is slowed down because some of the available enzyme sites are occupied by the inhibitor. If a dissimilar substance which does not fit the site is present, the enzyme rejects it, accepts the substrate, and the reaction proceeds normally.

Non-competitive inhibitors are considered to be substances which when added to the enzyme alter the enzyme in a way that it cannot accept the substrate. Figure 10.

Substrate inhibition will sometimes occur when excessive amounts of substrate are present. Figure 11 shows the reaction velocity decreasing after the maximum velocity has been reached.

Additional amounts of substrate added to the reaction mixture after this point actually decrease the reaction rate. This is thought to be due to the fact that there are so many substrate molecules competing for the active sites on the enzyme surfaces that they block the sites (Figure 12) and prevent any other substrate molecules from occupying them.

This causes the reaction rate to drop since all of the enzyme present is not being used. Next: Effects of Temperature PDF version of Introduction to Enzymes

You might also like