internal peptidyl-lysine acetylation

Definition

Target type: biologicalprocess

The addition of an acetyl group to a non-terminal lysine residue in a protein. [GOC:mah]

Internal peptidyl-lysine acetylation is a post-translational modification (PTM) that involves the addition of an acetyl group (CH3CO) to the ε-amino group of a lysine residue within a protein. This modification is catalyzed by a diverse group of enzymes known as lysine acetyltransferases (KATs), which are involved in various cellular processes.

Here's a detailed description of the process:

1. **Substrate Recognition and Binding:** KATs recognize and bind to specific lysine residues within their target proteins. This recognition is often mediated by the specific amino acid sequence surrounding the lysine residue, as well as by the overall protein structure.

2. **Acetyl Group Transfer:** Once bound to the target protein, KATs utilize acetyl-CoA as a donor molecule to transfer an acetyl group to the ε-amino group of the lysine residue. This reaction is typically driven by the release of CoA and the formation of a new N-ε-acetyllysine residue.

3. **Regulation of Protein Function:** Internal peptidyl-lysine acetylation can significantly impact protein function. It can influence protein-protein interactions, alter protein stability, and modulate enzymatic activity. This modification is frequently involved in:
- **Gene regulation:** Acetylation can affect the accessibility of DNA to transcription factors, thus modulating gene expression.
- **Signal transduction:** Acetylation can modify the activity of signaling proteins, leading to changes in cellular responses.
- **Metabolic pathways:** Acetylation can impact the activity of metabolic enzymes, influencing energy production and nutrient utilization.
- **Protein degradation:** Acetylation can affect the stability of proteins and influence their susceptibility to degradation.

4. **Dynamic and Reversible Process:** Internal peptidyl-lysine acetylation is a highly dynamic and reversible process. De-acetylation, the removal of the acetyl group, is catalyzed by a class of enzymes known as lysine deacetylases (KDACs). The balance between acetylation and de-acetylation plays a crucial role in regulating protein function and cellular signaling.

In summary, internal peptidyl-lysine acetylation is a fundamental PTM that exerts a profound impact on cellular function by modulating protein structure, activity, and interactions. This reversible process is intricately regulated by KATs and KDACs, which are central to the control of various cellular processes, including gene expression, signal transduction, and metabolism.'
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Proteins (3)

Compounds (29)