What enzyme removes the amino group from an amino acid?

The enzyme that removes the amino group from an amino acid is deaminase. This process is known as deamination, and it plays a crucial role in nitrogen metabolism. Deaminases facilitate the conversion of amino acids into corresponding keto acids by removing the amino group (–NH2). This reaction is essential in various biological processes, including energy production and the synthesis of other biomolecules.

In contrast, decarboxylases are enzymes that remove a carboxyl group (–COOH) from amino acids and other compounds rather than an amino group. Gelatinases are specific enzymes that break down gelatin, a protein derived from collagen, but do not remove amino groups. Ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide, which is unrelated to the removal of amino groups from amino acids. Therefore, deaminase is the appropriate choice for the removal of the amino group.