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

@article{Srikhanta2013DistinctPR,
  title={Distinct physiological roles for the two L-asparaginase isozymes of Escherichia coli.},
  author={Yogitha N. Srikhanta and John M. Atack and Ifor R. Beacham and Michael P Jennings},
  journal={Biochemical and biophysical research communications},
  year={2013},
  volume={436 3},
  pages={362-5}
}
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… CONTINUE READING

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Beacham, Co-dependent positive regulation of the ansB promoter of Escherichia coli by CRP and the FNR protein: a molecular analysis

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