protein-propionyllysine depropionylase activity

Definition

Target type: molecularfunction

Catalysis of the reaction:H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD+ = 3''-O-propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide. [GOC:sp, PMID:30026585, RHEA:23500]

Protein-propionyllysine depropionylase activity refers to the enzymatic removal of propionyl groups from lysine residues within proteins. This process is crucial for regulating protein function and stability. Propionylation is a post-translational modification that can alter protein structure and activity, often by affecting protein-protein interactions or the binding of other molecules. Depropionylation, catalyzed by depropionylase enzymes, reverses this modification, restoring the original protein state. Depropionylation is involved in various cellular processes, including:

* **Signal transduction:** Depropionylation can modulate the activity of signaling proteins, influencing cellular responses to stimuli.
* **Gene expression:** Depropionylation can affect the function of transcription factors, influencing gene expression patterns.
* **Protein stability:** Depropionylation can influence protein folding and stability, affecting protein degradation and lifespan.
* **Metabolic regulation:** Depropionylation is involved in the regulation of metabolic pathways, including fatty acid metabolism and energy production.

The specific depropionylase enzymes involved in these processes vary, and their activity is often regulated by cellular conditions and signaling pathways. Understanding the mechanisms of depropionylation is essential for comprehending the complex regulatory networks within cells and for developing novel therapeutic strategies targeting protein modifications.'
"

Proteins (2)

Compounds (33)