Asparagine synthetase (or aspartate-ammonia ligase) is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. This amidation reaction is similar to that promoted by glutamine synthetase. The enzyme is ubiquitous in its distribution in mammalian organs, but basal expression is relatively low in tissues other than the exocrine pancreas. Cancerous cells exhibit rapid growth and cell division and subsequently have an increased nutritional need. The particularly low-level expression of asparagine synthetase in primary acute lymphoblastic leukemia (ALL) and numerous ALL cell lines, as compared to that of normal cells, makes asparagine depletion an effective method of treatment due to the cells' unusual dependency on circulating serum asparagine as a necessary nutrition for growth. A correlation between L-asparaginase efficacy and asparagine synthetase protein levels in a number of human ovarian cell lines has been observed. As mentioned above, this result confirmed similar observations in human leukemia cell lines. Hence asparagine synthetase might be used as a biomarker in ovarian cancer screening and potential treatment.