Many enzymes require the presence of a nonprotein substance called a cofactor. An inactive protein molecule is known as an apoenzyme. An active enzyme, it is called a holoenzyme. Cofactors may be organic or inorganic.
Many enzymes require the presence of a nonprotein substance called a cofactor. An inactive protein molecule is known as an apoenzyme. An active enzyme, it is called a holoenzyme. Cofactors may be organic or inorganic.
Many enzymes require the presence of a nonprotein substance called a cofactor. An inactive protein molecule is known as an apoenzyme. An active enzyme, it is called a holoenzyme. Cofactors may be organic or inorganic.
nonprotein substance called a cofactor. Cofactors may be organic or inorganic. There are three types of cofactors. the inactive protein molecule is known as an apoenzyme. an active enzyme, it is called a holoenzyme.
Type of cofactor Prosthetic groups Coenzymes Enzyme activators
Coenzymes small, non-protein organic molecules. they bind loosely and temporarily to the active site of the enzyme. play an accessory role in enzyme-catalyzed processes, acting as a donor or acceptor of a substance involved in the reaction. When combined with an inactive apoenzyme, coenzymes form a complete, active enzyme called the holoenzyme
The coenzymes readily detach and help to transfer chemical group, atoms or electrons from one enzyme to another Many coenzymes are derivatives of vitamins especially group B vitamins. NAD (nicotinamide adenine dinucleotide) for example is formed from niacin. It is a coenzyme for a number of dehydrogenase enzymes and acts as a hydrogen acceptor. Prosthetic group is a non-protein organic molecule tightly (often covalently) bound to a particular enzyme molecule. involved in the catalytic function of the enzyme. Haem is an example of a prosthetic group found in cytochromes and haemoglobin, which carries electrons and/or oxygen.
Ion activator Activators are inorganic ions such as Ca 2+ Zn 2+ , Mg 2+ , Fe 2+ and CF. They may attach temporarily to the enzyme and change its active site t make the shape more suitable for a reaction to take place. The ion may also bind the enzyme and substrate together.
Help draw electron away from the substrate molecule-making bond less stable-eisier to break Example-refer your book Calcium ions are needed to activate thrombokinase which converts prothrombin to thrombin in blood clotting. Chloride ions increase salivary amylase activity.
The largest number of vitamins (e.g., B complex vitamins) function as precursors for enzyme cofactors, that help enzymes in their work as catalysts in metabolism. In this role, vitamins may be tightly bound to enzymes as part of prosthetic groups: For example, biotin is part of enzymes involved in making fatty acids. Vitamins may also be less tightly bound to enzyme catalysts as coenzymes, detachable molecules that function to carry chemical groups or electrons between molecules. For example, folic acid carries various forms of carbon group methyl, formyl, and methylene in the cell. Although these roles in assisting enzyme-substrate reactions are vitamins' best-known function, the other vitamin functions are equally important.