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Structural Biochemistry/Enzyme/Apoenzyme and Holoenzyme: Cofactor: A Definition

Many enzymes require additional small molecules called cofactors to aid in their catalytic activity. Cofactors can be inorganic ions or organic coenzymes derived from vitamins. An apoenzyme is an inactive enzyme that requires a cofactor, while a holoenzyme is the active form containing both the apoenzyme and bound cofactor. DNA polymerase and RNA polymerase are examples of holoenzymes - they are multi-subunit protein complexes that use magnesium ions and ribonucleotides, respectively, to catalyze DNA and RNA polymerization.

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164 views2 pages

Structural Biochemistry/Enzyme/Apoenzyme and Holoenzyme: Cofactor: A Definition

Many enzymes require additional small molecules called cofactors to aid in their catalytic activity. Cofactors can be inorganic ions or organic coenzymes derived from vitamins. An apoenzyme is an inactive enzyme that requires a cofactor, while a holoenzyme is the active form containing both the apoenzyme and bound cofactor. DNA polymerase and RNA polymerase are examples of holoenzymes - they are multi-subunit protein complexes that use magnesium ions and ribonucleotides, respectively, to catalyze DNA and RNA polymerization.

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Ahmed Omaar
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© © All Rights Reserved
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Structural Biochemistry/Enzyme/Apoenzyme

and Holoenzyme
< Structural Biochemistry | Enzyme

Cofactor: A Definition[edit]
Many enzymes require an additional small molecule, known as a cofactor to aid with catalytic
activity. A cofactor is a non-protein molecule that carries out chemical reactions that cannot be
performed by the standard 20 amino acids. Cofactors can be either inorganic molecules (metals) or
small organic molecules (coenzymes).
Cofactors, mostly metal ions or coenzyme, are inorganic and organic chemicals that function in
reactions of enzymes. Coenzymes are organic molecules that are nonproteins and mostly
derivatives of vitamins soluble in water by phosphorylation; they bind apoenzyme protein molecule to
produce active holoenzyme.

Figure 1-1: A flow chart of the two types of cofactors.


Apoenzyme- An enzyme that requires a cofactor but does not have one bound. An apoenzyme is an
inactive enzyme, activation of the enzyme occurs upon binding of an organic or inorganic cofactor.
Holoenzyme- An apoenzyme together with its cofactor. A holoenzyme is complete and catalytically
active. Most cofactors are not covalently bound but instead are tightly bound. However,
organic prosthetic groups such as an iron ion or a vitamin can be covalently bound. Examples of
holoenzymes include DNA polymerase and RNA polymerase which contain multiple protein subunits.
The complete complexes contain all the subunits necessary for activity.

Figure 1-2: Illustrates that


an Apoenzyme + Cofactor = Holoenzyme.

Examples of Holoenzymes[edit]
DNA polymerase is a holoenzyme that catalyzes the polymerization of deoxyribonucleotides into a
DNA strand. DNA polymerase is an active participant in DNA replication. It reads the intact DNA
strand as a template and uses it to synthesize the new strand. The newly polymerized DNA strand is
complementary to the template strand and identical to template's original partner strand. DNA
polymerase uses a magnesium ion for catalytic activity.

Figure 1-3: Illustrates the holoenzyme


DNA polymerase a multi-subunit complex.
RNA polymerase is also a holoenzyme that catalyzes RNA. RNA polymerase is needed for
constructing RNA chains from DNA genes as templates, a process known as transcription. It
polymerizes ribonucleotides at the 3' end of an RNA transcript.

Figure 1-4: Illustrates the holoenzyme RNA


polymerase a subunit complex.

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