To aid in catalytic activity, many enzymes require the inclusion of a tiny molecule known as a cofactor. A cofactor is a non-protein molecule that performs chemical reactions that the usual 20 amino acids cannot. Cofactors can be inorganic (metals) or organic (small organic compounds) (coenzymes). Cofactors, which are typically coenzymes or metal ions , are inorganic and organic molecules that help enzymes perform their functions. Coenzymes are nonprotein organic molecules that bind to apoenzyme protein molecules to produce active holoenzymes. They are mostly vitamin derivatives that are soluble in water due to phosphorylation. Holoenzyme refers to apoenzyme in the presence of its cofactor. A holoenzyme is an enzyme that is both full and catalytically active. The majority of cofactors are firmly bonded rather than covalently bound. Organic prosthetic groups, such as iron ions or vitamins, can, however, be covalently bound. DNA polymerase and RNA polymerase are examples of holoenzymes, which comprise several protein components. All of the subunits required for activity are found in the full complexes.
Holoenzyme
The term holoenzyme refers to an apoenzyme that is complete and catalytically active, as well as the cofactor. A cofactor might be a tiny organic molecule or a metal ion. The majority of metal ions are covalently or noncovalently linked to the enzyme. Prosthetic groupings are what they’re called. Coenzymes are a type of small chemical molecule.
Coenzymes can bind to enzymes either tightly or loosely. Cu, Co, Mg, Mn, Ni, Fe and other ions can be used as prosthetic groups. NADP, NAD, FAD, folic acid, biotin, and other coenzymes are examples. Cofactors bind to the enzyme succinate dehydrogenase. DNA polymerase and RNA polymerase are two examples of holoenzymes. Multi-protein subunits make up these enzymes. As a result, they are both complete and complex. A biological reaction can only be catalysed by holoenzymes.