Asparaginase

Asparaginase is a hydrolase enzyme that catalyzes the hydrolysis of the amino acid L-asparagine into L-aspartic acid and ammonia. It is commonly derived from bacterial sources such as Escherichia coli and Erwinia chrysanthemi.

Asparaginase functions by depleting extracellular L-asparagine, a vital amino acid that certain cells—particularly cancer cells—cannot synthesize due to low levels of asparagine synthetase. By eliminating L-asparagine, asparaginase starves these cells, leading to inhibited protein synthesis and cell death.

• Reaction: L-asparagine + H₂O → L-aspartic acid + NH₃
• Optimal pH: 8.0 (active in pH 7.0–8.6 range)
• Optimal temperature: 37°C (tends to lose activity above 45°C)
• Inhibitors: L-Aspartic acid, L-Glutamic acid, Cu²⁺, Hg²⁺, Zn²⁺

• Used to investigate amino acid dependency and metabolic vulnerabilities in tumor cells.
• Assists in studies of nitrogen metabolism and enzyme-substrate specificity.
• Induces apoptosis in leukemic cells by depriving them of asparagine.
• Used as part of multi-drug regimens (e.g., with vincristine, prednisone, and methotrexate).

• Available as white lyophilized powder.
• Store at 2-8°C (dry form); keep frozen at –20°C for long-term enzyme stability.