peptidylamidoglycolate lyase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: peptidylamidoglycolate = peptidyl amide + glyoxylate. [EC:4.3.2.5]

Peptidylamidoglycolate lyase activity refers to the enzymatic cleavage of the amide bond within a peptidylamidoglycolate molecule. Peptidylamidoglycolates are structurally unique molecules consisting of a peptide chain linked to an amidoglycolate moiety. This activity is crucial in the breakdown of these molecules and is involved in various metabolic pathways. The enzyme responsible for this activity utilizes a mechanism involving nucleophilic attack on the carbonyl carbon of the amide bond, leading to the formation of a tetrahedral intermediate. This intermediate subsequently breaks down, releasing the carboxyl group of the amidoglycolate and the free amino group of the peptide chain. The precise mechanism and specific residues involved in the catalytic process can vary between different peptidylamidoglycolate lyases, depending on their structural and evolutionary relationships. This activity plays a vital role in the degradation of various natural products, including antibiotics and peptides, as well as in the biosynthesis of certain secondary metabolites. It is also implicated in the regulation of cellular processes, such as signal transduction and gene expression, through its involvement in the metabolism of signaling molecules.'
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Proteins (1)

Compounds (3)