aldehyde-lyase activity

Definition

Target type: molecularfunction

Catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone. [GOC:curators]

Aldehyde-lyase activity refers to the enzymatic ability to cleave a carbon-carbon bond adjacent to a carbonyl group, specifically an aldehyde, leading to the formation of two products: an aldehyde and a new carbon-carbon double bond. This reaction is crucial in various metabolic pathways, including the breakdown of carbohydrates, amino acids, and lipids. Aldehyde lyases are known to participate in diverse biological processes, such as:

- **Carbohydrate metabolism:** Cleavage of sugars, like fructose-1,6-bisphosphate, during glycolysis.
- **Amino acid metabolism:** Degradation of branched-chain amino acids, such as valine, leucine, and isoleucine.
- **Lipid metabolism:** Breakdown of fatty acids, including the removal of the terminal carboxyl group.
- **Detoxification:** Removal of harmful aldehydes from the body, preventing their accumulation.

The reaction mechanism often involves a nucleophilic attack on the carbonyl carbon by an active site residue, followed by elimination of a leaving group to form the new double bond. The specific residues involved in catalysis and the overall reaction mechanism can vary depending on the particular aldehyde lyase. However, the fundamental principle of cleaving the carbon-carbon bond adjacent to an aldehyde remains consistent.'
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Proteins (1)

Compounds (1)