PMID: 8955411Dec 1, 1996Paper

N-acetyl-heparosan lyase of Escherichia coli K5: gene cloning and expression

Journal of Bacteriology
R LegouxM Salomé

Abstract

The structure of the capsular polysaccharide of Escherichia coli K5 is identical to that of N-acetyl-heparosan, a nonsulfated precursor of heparin, which makes this E. coli antigen an attractive starting point for the chemical synthesis of analogs of low-molecular-weight heparin. This polysaccharide is synthesized as a high-molecular-weight molecule that can be depolymerized by an enzyme displaying endo-beta-eliminase activity. The eliminase-encoding gene, designated elmA, has been cloned from E. coli K5 by expression in E. coli K-12. The K-12 genome is devoid of the elmA sequence. The elmA gene product is 820 amino acids long. Active recombinant eliminase is produced by K-12 cells in both cell-bound and secreted forms. Deletion analyses have shown that the C terminus and the N terminus are required for activity and secretion, respectively.

References

Dec 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·F SangerA R Coulson

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Citations

Jan 31, 2003·The Journal of Biological Chemistry·Martina MühlenhoffRita Gerardy-Schahn
Aug 19, 2010·Biotechnology and Bioengineering·Zhenyu WangRobert J Linhardt
Jun 4, 2010·The Journal of Biological Chemistry·James E ThompsonIan S Roberts
Oct 17, 2014·Applied Microbiology and Biotechnology·Florian LelchatClaire Boisset
Jul 1, 2004·Critical Reviews in Biotechnology·P MichaudJ Courtois
Mar 30, 2004·The Journal of Biological Chemistry·Kevin J MurphyJohn T Gallagher
Jan 1, 2014·FEMS Microbiology Reviews·Brady F CressMattheos A G Koffas
Dec 7, 2005·Carbohydrate Research·Toshikazu MinamisawaJun Hirabayashi

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