Professional Documents
Culture Documents
Describe The Chemistry of Two Types of Enzymes and Explain How The Apo Enzyme Forms
Describe The Chemistry of Two Types of Enzymes and Explain How The Apo Enzyme Forms
Describe The Chemistry of Two Types of Enzymes and Explain How The Apo Enzyme Forms
activity. A cofactor is a non-protein molecule that performs chemical reactions that the
regular 20 amino acids cannot. Cofactors may be inorganic (metals) or organic (small organic
molecules) (coenzymes).
Cofactors, which are primarily metal ions or coenzyme, are inorganic and organic
chemicals that participate in enzyme reactions. Coenzymes are non-protein organic molecules
that are primarily vitamin derivatives that are soluble in water through phosphorylation; they
attach to the Apo enzyme protein molecule to form the active holoenzyme.
polypeptide that is complete and catalytically active. The majority of cofactors are not
covalently linked but are closely bound. However, covalently binding organic prosthetic
groups such as an iron ion or a vitamin are possible. DNA polymerase and RNA polymerase
are examples of holoenzymes because they contain many protein subunits. Complexes in
Example of Holoenzyme
polymerization into a DNA chain. DNA polymerase is a key component of DNA replication.
It uses the intact DNA strand as a basis for the new strand's synthesis. The newly
polymerized DNA strand is complementary to and similar to the template strand. DNA
A protein that, when combined with a coenzyme, forms an active enzyme system and
controls the system's substrate specificity. Enzymes can accelerate biochemical reactions.
Certain enzymes use cofactors (non-protein molecules) to catalyse, while others do not.
Simple enzymes are those that do not need cofactors. Pepsin, trypsin, and urease are both
examples.
References
Fruk, L., Kuo, C. H., Torres, E., & Niemeyer, C. M. (2009). Apoenzyme