ATP-dependent peptidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. [GOC:mah]

ATP-dependent peptidase activity is a fundamental molecular process involved in the hydrolysis of peptide bonds within proteins, utilizing the energy derived from ATP. This activity is crucial for a wide range of cellular processes, including protein degradation, processing, and regulation.

ATP-dependent peptidases employ a conserved catalytic mechanism that involves the hydrolysis of ATP to ADP and inorganic phosphate, providing the energy required to break the peptide bond. The mechanism often involves a two-step process:

1. **ATP binding and hydrolysis:** ATP binds to the peptidase, inducing a conformational change in the enzyme, facilitating the binding of the target protein substrate. ATP hydrolysis then occurs, releasing energy that is used to activate the peptidase.
2. **Peptide bond cleavage:** The activated peptidase cleaves the peptide bond within the protein substrate, releasing a smaller peptide fragment.

The specific activity and substrate specificity of ATP-dependent peptidases vary depending on the enzyme. Some peptidases are highly specific for particular amino acid sequences, while others exhibit broader substrate preferences.

Notable examples of ATP-dependent peptidases include:

* **Clp proteases:** Involved in the degradation of misfolded or damaged proteins, contributing to protein quality control.
* **Lon proteases:** Play a role in the regulation of protein turnover and stress response.
* **HslUV protease:** Participate in the degradation of misfolded proteins and the removal of short-lived regulatory proteins.

The intricate molecular function of ATP-dependent peptidases is essential for maintaining cellular homeostasis, regulating protein activity, and responding to stress. These enzymes are critical players in diverse biological processes, from protein synthesis and degradation to signal transduction and immunity.'
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Proteins (5)

Compounds (4)