L-lysine-lactamase

L-lysine-lactamase is an enzyme that catalyzes the hydrolysis of the amino acid L-lysine. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is L-lysine amidehydrolase.

Function

L-lysine-lactamase is involved in the metabolism of L-lysine, an essential amino acid in humans. It catalyzes the hydrolysis of L-lysine, resulting in the formation of ammonia and a carboxylic acid. This reaction is important in the breakdown and utilization of L-lysine in the body.

Structure

Like other enzymes, L-lysine-lactamase is a protein composed of amino acids. The exact structure of this enzyme can vary depending on the species in which it is found. However, all enzymes have a specific shape that allows them to bind to their substrate (in this case, L-lysine) and catalyze a specific reaction.

Clinical Significance

Abnormalities in the function or levels of L-lysine-lactamase can lead to health problems. For example, a deficiency in this enzyme can result in an inability to properly metabolize L-lysine, leading to a buildup of this amino acid in the body. This can cause a variety of symptoms, including neurological problems, growth retardation, and muscle weakness.

See Also

• Enzyme
• Hydrolase
• Amino acid
• Metabolism
• Protein