Asparaginase Escherichia coli

L-Asparaginase is an enzyme that may be produced by Escherichia coli. Asparaginase hydrolyzes the reaction of asparagines to aspartic acid and ammonia to deplete lymphoid cells of asparagine, which inhibits protein synthesis. The... 

Pegylated-L-asparaginase, PEG-conjugated L-asparaginase (of Escherichia coli) Erwinia L-asparginase is extracted from Erwinia chrysanthemi. 

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... 

Aung, H. P., Bocola, M., Schleper, S. and Rohm, K. H. (2000). Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochim. Biophys. Acta 1481, 349-359. 

Duval, M., Suciu, S., Ferster, A., Rialland, X., Nelken, B., Lutz, P., Benoit, Y., Robert, A., Manel, A. M., Vilmer, E., Otten, J. and Philippe, N. (2002). Comparison of Escherichia coli-asparaginase with Erwin V/-asparaginasc in the treatment of childhood lymphoid malignancies results of a randomized European Organization for Research and Treatment of Cancer-Children s Leukemia Group phase 3 trial. Blood 99, 2734-2739. 

Kozak, M., Borek, D., Janowski, R. and Jaskolski, M. (2002). Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli L-asparaginase II (AspOOGlu mutant). Ada Crystallogr. Sect. D Biol. Crystallogr. 58, 130-132. 

Palm, G. J., Lubkowski, J., Derst, C., Schleper, S., Rohm, K. H. and Wlodawer, A. (1996). A covalently bound catalytic intermediate in Escherichia coli asparaginase crystal structure of a Thr-89-Val mutant. FEBS Lett. 390 (2), 211-216. 

A. L Swain, M. Jaskolski, D. Hoioaet, et al. Crystal structure of Escherichia coli 1-asparaginase, an enzyme used in cancer therapy. P oc. NatL Acad. Sci. USA 90.1474 (1993). 

D. T. Bonthron. 1-Asparaginase tl of Escherichia coli K-12 cloning, mapping and... 

T. Yosiumoto, H. Nishimun, Y.Saito.etal. Characterization of polyethylene glycol-modified 1-asparaginase from Escherichia coli and its application to therapy of lEUksnhJpn. J. Cancer Ret. 77 1264 (1986). 

W. E. Evans, A. Tsiatis, G. Riven, etal. Anaphylactoid reactions to Escherichia coli and Erwinia asparaginase in childien with leukemia and lymphoma. Cancer 49 1378 (1982). 

E. Eden, M. P. Shaw, J. S. Lilleyman, et al. Non-randomised study comparing toxicity of Escherichia coli and Erwinia asparaginase in children with leukemia. Mad... 

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

L-Asparaginase is unique among cytotoxic drugs in its unusual mechanism of action, patterns of toxicity, and source (see Table 124—15). It is an enzyme produced by Escherichia coli and other bacteria. 

L. T. Mashbum and J. C. Wriston. Tumor inhibitory effect of 1-asparaginase from Escherichia coli. Arch. Biochem. 705 450 (1964). 

M. P. Jennings and I. R. Beacham. Analysis of the Escherichia coli gene encoding 1-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J. BacterioL 772 1491 (1990). 

T. Maita and G. Matsuda. The primary structure of 1-asparaginase from Escherichia coli. Hoppe Seyler s Z Physiol. Chem. 367 105 (1980). 

E. Harms, A. Wehner, M. P. Jennings, et al. Construction and expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts. Protein Exp. Purif. 2 144 (1991). 

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). 

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). 

Kamisaki, Y., Wada, H., Yagura, H., Matsushima, A. and Inada, Y. (1981) Reduction in immunogenicity and clearance rate of Escherichia coli L-asparaginase by modification with monomethoxypoly(ethylene glycol). J. Pharmacol. Exp. Ther. 216 410-414. 

It is a preparation from Escherichia coli containing the enzyme L-asparaginase amidohydrolase. 

The influence of glycosylation on tissue uptake of enzymes has been investigated. Lactose and A-acetylneuraminyl-Iactose have been coupled to Escherichia coli L-asparaginase by reductive amination with sodium cyanoborohydride (see Scheme 2, Vol. 10, Part II, Chapter 8, p. 428). Oligosaccharides obtained from... 

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