Distinct physiological roles for the two L-asparaginase isozymes of Escherichia coli

Abstract

Escherichia coli expresses two l-asparaginase (EC 3.5.1.1) isozymes: l-asparaginse I, which is a low affinity, cytoplasmic enzyme that is expressed constitutively, and l-asparaginase II, a high affinity periplasmic enzyme that is under complex co-transcriptional regulation by both Fnr and Crp. The distinct localisation and regulation of these enzymes suggest different roles. To define these roles, a set of isogenic mutants was constructed that lacked either or both enzymes. Evidence is provided that l-asparaginase II, in contrast to l-asparaginase I, can be used in the provision of an anaerobic electron acceptor when using a non-fermentable carbon source in the presence of excess nitrogen.