So far in this series we have looked at how enzymes work, what can affect the rate at which they work, and how their action can be inhibited. Today we are looking at coenzymes and cofactors: non-proteins that are needed in order for some enzymes to be able to catalyse their reaction.
Coenzymes are a specific type of cofactor. They are organic molecules, which just means that they contain carbon. The majority are carrier molecules, transferring things (often electrons) from one enzyme to another. They bind to the active site with the substrate and get changed during the reaction, but they are continually recycled. A great example of this is the coenzyme called NAD used in respiration. It is reduced to NADH during glycolysis, the link reaction, and the Krebs cycle. Then it is oxidised back to NAD during oxidative phosphorylation. Many coenzymes are derived from vitamins – see, vitamins are important!
Whilst coenzymes are a specific type of cofactor, there are other types of cofactor which have different ways of working. However they are all non-proteins. Many cofactors are ions which help the substrate to bind to the active site. Remember that chloride ions are cofactors for the enzyme amylase. Sometimes the ions can be an integral part of the enzyme and are tightly bound to it. If this is the case, they are referred to as prosthetic groups. Zinc ions are a prosthetic group of the enzyme carbonic anhydrase, which you may have come across in red blood cells. These ions are essential for the reaction to occur, but are not actually changed during the reaction.
- Coenzymes and cofactors are non-proteins which are necessary for some enzymes to catalyse a reaction.
- Coenzymes are organic molecules which often transfer electrons. They are changed and recycled.
- Cofactors are often ions. They are not changed in the reaction. Specific examples are chloride ions and zinc ions.