lasparagine

Lasparagine is not a standard term in biochemistry and is commonly a misspelling of asparagine (Asn). The following overview summarizes asparagine, the polar amino acid typically found in proteins and cellular metabolism.

Asparagine is a neutral, polar amino acid with a side chain that ends in a carboxamide group. It is one of the 20 standard amino acids incorporated into proteins during translation. In humans, asparagine can be synthesized from aspartate by the enzyme asparagine synthetase, using glutamine as the nitrogen donor and ATP, and it can also be obtained through the diet.

Within proteins, asparagine residues are notable as sites of N-linked glycosylation, a common post-translational modification that influences protein folding, stability, and signaling. Asparagine is degraded by the enzyme asparaginase to aspartate and ammonia; this pathway is exploited in medicine, where L-asparaginase is used to treat certain leukemias by depleting circulating asparagine.

In metabolic terms, asparagine participates in nitrogen transport and amino acid interconversion in various tissues. While humans can synthesize it, dietary intake contributes to pool size. In plants and microorganisms, asparagine often serves as a reservoir of organic nitrogen and plays roles in stress responses and metabolism.