amidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3. [EC:3.5.1.4]

Amidase activity refers to the catalytic hydrolysis of an amide bond, a key chemical linkage in proteins and other molecules. This enzymatic function plays a crucial role in various biological processes, including:

- **Protein degradation:** Amidases break down proteins by cleaving peptide bonds, contributing to protein turnover and the recycling of amino acids.
- **Metabolic pathways:** They participate in the breakdown and synthesis of various metabolites, including amino acids, fatty acids, and neurotransmitters.
- **Drug detoxification:** Amidases can hydrolyze amide-containing toxins and drugs, facilitating their elimination from the body.
- **Signal transduction:** Some amidases are involved in signaling pathways by cleaving amide bonds in signaling molecules, influencing cellular responses.

The mechanism of amidase activity typically involves the following steps:

1. **Substrate binding:** The enzyme binds to the amide substrate, positioning the amide bond within the active site.
2. **Nucleophilic attack:** A nucleophilic group within the enzyme's active site attacks the carbonyl carbon of the amide bond.
3. **Proton transfer:** A proton is transferred to the nitrogen atom of the amide bond.
4. **Bond cleavage:** The amide bond is cleaved, releasing the amine and carboxylic acid products.

Amidases exhibit diverse substrate specificity, with some enzymes acting on specific amide substrates while others have broader substrate ranges. This variety reflects their involvement in a wide array of biological processes.'
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Proteins (2)

Compounds (60)