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Enzyme Chemistry: Apo and Holoenzymes Explained

There are two types of enzymes - apo enzymes and holoenzymes. Apo enzymes require cofactors like metals or vitamins to become active, forming holoenzymes. Cofactors attach to the apo enzyme protein to create the catalytically active holoenzyme. DNA polymerase is an example of a holoenzyme, containing protein subunits and a magnesium ion cofactor to catalyze DNA replication. An apo enzyme forms when its cofactor is removed, leaving an inactive protein that can later re-bind its cofactor to regain function.

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127 views2 pages

Enzyme Chemistry: Apo and Holoenzymes Explained

There are two types of enzymes - apo enzymes and holoenzymes. Apo enzymes require cofactors like metals or vitamins to become active, forming holoenzymes. Cofactors attach to the apo enzyme protein to create the catalytically active holoenzyme. DNA polymerase is an example of a holoenzyme, containing protein subunits and a magnesium ion cofactor to catalyze DNA replication. An apo enzyme forms when its cofactor is removed, leaving an inactive protein that can later re-bind its cofactor to regain function.

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manahil siddiqui
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© © All Rights Reserved
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Describe the chemistry of two types of enzymes and explain how the Apo enzyme forms

Numerous enzymes require a small molecule called a cofactor to aid in catalytic

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.

Apo enzyme- A cofactor-required enzyme that is not bound. An Apo enzyme is a

dormant enzyme that is activated by the binding of an organic or inorganic cofactor.

A holoenzyme is a proenzyme in the presence of its cofactor. A holoenzyme is a

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

their entirety comprise all of the subunits needed for activity.

Example of Holoenzyme

DNA polymerase is a holoenzyme that catalyses deoxyribose nucleotide

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

polymerase is catalytically active due to the presence of a magnesium ion.


Formation of Apo enzyme

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

reconstitution as a chemical tool for structural enzymology and biotechnology. Angewandte

Chemie International Edition, 48(9), 1550-1574.

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