Asparagine is a non-essential protein amino acid that is present in many fruits and vegetables including asparagus, from which it gets its name.
Other dietary sources include meat, potatoes, eggs, nuts, and dairy. It can also be formed from aspartic acid and glutamine using the enzyme asparagine synthetase.
In addition to being a structural component of many proteins, asparagine is also useful to the urea cycle. It acts as a nontoxic carrier of residual ammonia to be eliminated from the body.
Asparagine is rapidly converted to aspartic acid by the enzyme asparaginase.
Interestingly, L-asparaginase has been successfully used as a chemotherapeutic agent for decades. It causes extracellular depletion of asparagine which seems to play a critical role in cellular adaptations to glutamine and apoptosis.
Overall low amino acids from poor dietary intake or GI malabsorption/maldigestion may result in low levels of arginine. Low levels of its precursors (aspartic acid and glutamine), or enzymatic dysfunction in arginine synthetase can also result in low asparagine levels. Upregulation of asparaginase may contribute to lower levels of asparagine and rarely can be associated with hyperammonemia.
Depleted levels of arginine due to genetic mutations in asparagine synthetase are associated with neurodevelopmental disorders.
High dietary protein intake can elevate asparagine levels. Asparagine may also be elevated in hyperammonemia to serve as a reservoir for waste nitrogen.
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