Difference between “Apoenzyme” and “Holoenzyme”

Enzymes are biological catalysts. They are substrate-specific and play an essential role in various biochemical reactions. Most of the enzymes, except catalytic RNAs or ribozymes, are proteins and made up of amino acids. Some enzymes also require a non-protein part for their activity. Based on these, enzymes are categorised into two types:

  • Simple enzymes – They are only made up of proteins, e.g. trypsin, pepsin, etc.
  • Conjugate enzymes or holoenzymes – They consist of a protein as well as non-protein part essential for the activity. The protein part of the holoenzyme is known as apoenzyme, which is inactive. The non-protein part is called a cofactor and is necessary for the catalytic function of the enzymes. E.g. metal ions (Mg2+, Fe3+, Zn2+), organic molecules or coenzymes (NAD+, NADP+, FAD2+) and prosthetic groups. E.g. catalase, alcohol dehydrogenase, pyruvate kinase, DNA polymerase, etc.

So holoenzyme is an active enzyme-cofactor complex, i.e. an apoenzyme attached to a cofactor.

Apoenzyme (Inactive) + Cofactor ⇌ Holoenzyme (Active)

Difference between Apoenzyme and Holoenzyme

The table below shows the main differences between Apoenzyme and Holoenzyme:




The catalytically inactive protein part of an enzyme

The catalytically active apoenzyme-cofactor complex

Chemical Constituents

Contains only protein

Contains protein as well as cofactors such as metal ions or other organic complexes known as coenzymes


Inactive and becomes active only after attaching to a cofactor

Active and fully functional to catalyse a biochemical reaction


Does not contain cofactors

Contains cofactors like metal ions or coenzymes


The protein moiety of the holoenzymes, e.g. carbonic anhydrase without Zn2+ ions.

DNA polymerase, RNA polymerase, carbonic anhydrase, etc.

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