Erwinia carotovora, asparaginase

L-Asparaginase, an enzyme derived from E. coli or Erwinia carotovora, has been employed in cancer chemotherapy where its selectivity depends upon the essential requirement of some tumours for the amino acid L-asparagine. Normal tissues do not require this amino acid and thus the enzyme is administered with the intention of depleting tumour cells of asparagine by converting it to aspartic acid and ammonia. Whilst L-asparaginase showed promise in a variety of experimentally induced tumours, it is only useful in humans for the treatment of acute lymphoblastic leukaemia, although it is sometimes used for myeloid leukaemia. 

Asparaginases with antilymphoma activity have also been found in extracts of Serratia marcescens (35-37), Erwinia carotovora (38), and Proteus vulgaris (36). Escherichia coli extracts contain a second asparaginase that is devoid of antilymphoma activity (39), and a similarly inactive enzyme has been found in a fungus, Fusarium tricinctum (40). An enzyme from Streptomyces griseus has L-asparaginase activity when assayed in tris-Cl (pH 8.6) but little or no activity in sodium borate (pH... 

Howard, J. B. and Carpenter, F. H. (1972). L-asparaginase from Erwinia carotovora. Substrate specificity and enzymatic properties. J. Biol. Chem. 247, 1020-1030. 

Kotzia, G. A. and Labrou, N. E. (2005). Cloning, expression and characterisation of Erwinia carotovora L-asparaginase. J. Biotechnol. 119,309-323. 

Krasotkina, J., Borisova, A., Gervaziev, Y. and Sokolov, N. (2004). One-step purification and kinetic properties of the recombinant L-asparaginase from Erwinia carotovora. Biotechnol. Appl. Biochem. 39, 215-221. 

Lee, S. M., Wroble, M. H. and Ross, J. T. (1989). L-Asparaginase from Erwinia carotovora an improved recovery and purification process using affinity chromatography. Appl. Biochem. Biotechnol. 22, 1-11. 

Papageorgiou, A. C., Posypanova, G. A., Andersson, C. S., Sokolov, N. N. and Krasotkina, J. (2008). Structural and Functional Insights into Erwinia carotovora L-Asparaginase. FEBSJ. 275, 4306-4316. 

K. Heilman, D. S. Miller, and R. A. Cammack, The effect of freeze-drying on the quaternary structure of L-asparaginase from Erwinia carotovora, Biochim. Biophys. Acta 749.-133-142 (1983). 

Colaspase and crisantaspase are the British Approved Names of asparaginase obtained from cultures of Escherichia coli and Erwinia carotovora respectively. 

J. R. Uren and R. C. Ragin. Improvement in the therapeutic, immunological, and clearance properties of Escherichia coli and Erwinia carotovora 1-asparaginases by attachment of poly-DL-alanyl peptides. Cancer Res. 39 1927 (1979). 

T. Han and T. Ohnuma. The in vitro blastogenesis inhibited by Erwinia carotovora 1-asparaginase. Nature New Biol. 239 50 (1972). 

D. Ridgway, R. C. Neerhout, and A. Bleyer. Attenuation of asparaginase-induced hyperglycemia after substitution of the Erwinia carotovora for the Escherichia coli enzyme preparation. Cancer 63 561 (1989). 

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