Amidhydrolyse

Amidhydrolyse, commonly referred to as amide hydrolysis, is the chemical process by which an amide bond is cleaved by the addition of water. The reaction converts an amide into a carboxylic acid (or its salt) and an amine (or ammonium) depending on the reaction conditions and pH. Amide hydrolysis can proceed through different pathways, most notably acid-catalyzed, base-catalyzed, or enzymatic routes.

In acid hydrolysis, heating an amide with a strong mineral acid yields a carboxylic acid and an ammonium ion after proton transfers. In base hydrolysis, aqueous base converts the amide to a carboxylate and an amine. Enzymatic hydrolysis is carried out by specialized enzymes such as amidases, which convert amides to carboxylic acids and ammonia, and is a central step in nitrogen and carbon metabolism in living organisms. Proteases, which hydrolyze peptide bonds, are a broader and biologically important class of amide-hydrolyzing enzymes.

Biological and environmental relevance is wide. Amidhydrolyse participates in protein turnover and nitrogen cycling, as well as in the breakdown of synthetic and natural amide-containing compounds. In biotechnology, enzymes that perform amide hydrolysis are used to produce amino acids and to modify peptides and proteins. Industrially, controlled amide hydrolysis is applied in the processing of polymers and in the production of intermediates for pharmaceuticals.

Representative examples include the hydrolysis of acetamide to acetic acid and ammonia, benzamide to benzoic acid and ammonia, and the enzymatic hydrolysis of certain penicillin derivatives by penicillin amidases to yield 6-aminopenicillanic acid. The specific pathway and products depend on the substrate, catalyst, and reaction conditions. See also amide bond, amidase, and hydrolysis.