What is the Difference Between Acylation and Prenylation?
🆚 Go to Comparative Table 🆚Acylation and prenylation are two post-translational protein modifications that involve the covalent attachment of lipid groups to proteins. Both processes result in hydrophobic modifications of proteins, but there are differences in the type of lipid groups and their attachment sites.
Here are the key differences between acylation and prenylation:
- Type of Lipid Groups: Acylation involves the covalent attachment of fatty acids, such as myristate and palmitate, to proteins. In contrast, prenylation involves the addition of prenyl groups, such as farnesyl or geranylgeranyl, to proteins.
- Attachment Site: Acylation typically occurs on the N-terminal glycine residue or lysine residues within the protein sequence. Prenylation, on the other hand, involves the covalent attachment of prenyl groups to a cysteine residue at or near the C-terminus of the protein.
- Physical Interaction: Prenyl groups, unlike acyl chains, are less packed and contain double bonds, which may lead to different physical interactions with membranes. For example, prenyl groups may not be directly embedded in the lipid bilayer but instead interact with specific receptors.
In summary, acylation and prenylation are post-translational protein modifications that use different lipid groups and attachment sites to modify proteins. While both processes result in hydrophobic modifications, they may interact with membranes in different ways due to the distinct physical properties of the lipid groups involved.
Comparative Table: Acylation vs Prenylation
Here is a table comparing the differences between acylation and prenylation:
| Characteristic | Acylation | Prenylation |
|---|---|---|
| Definition | Covalent attachment of fatty acids to proteins | Covalent attachment of prenyl groups to proteins |
| Type of Modification | Post-translational modification | Post-translational modification |
| Hydrophobic Modification | Modifies proteins hydrophobically | Modifies proteins hydrophobically |
| Fatty Acids | Myristate and palmitate are the most common fatty acid modifying groups | Farnesyl or geranylgeranyl are the most common prenyl groups |
| Attachment Site | N-terminal glycine residue | Cysteine residue at or near the C-terminus |
| Prenyl Groups | - | Farnesyl and geranylgeranyl |
| Types | S-acylation (also called S-palmitoylation) | S-farnesylation and S-geranylgeranylation |
| Enzymes | - | Farnesyltransferase (FTase) and Geranylgeranyltransferase type I (GGTase-I) |
Both acylation and prenylation are post-translational modifications that hydrophobically modify proteins. Acylation involves the covalent attachment of fatty acids, such as myristate and palmitate, to the N-terminal glycine residue of proteins. In contrast, prenylation involves the covalent attachment of prenyl groups, such as farnesyl or geranylgeranyl, to a cysteine residue at or near the C-terminus of proteins.
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