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Escherichia coli isocitrate lyase: properties and comparisons

1988; Elsevier BV; Volume: 966; Issue: 1 Linguagem: Inglês

10.1016/0304-4165(88)90125-0

1872-8006

Jeffrey C. Hoyt, Eugene F. Robertson, Kathleen A. Berlyn, Henry C. Reeves,

Enzyme Catalysis and Immobilization

The glyoxylate cycle was first discovered during studies on bacteria and fungi with the ability to grow on acetate or ethanol as the sole carbon source. Isocitrate lyase, the first enzyme unique to the glyoxylate cycle, has been studied in numerous prokaryotic and eukaryotic organisms. However, information on this enzyme from Escherichia coli is limited. We have recently reported the purification and in vitro phosphorylation of this enzyme. In this present study we have examined and characterized a variety of inhibitors, the divalent cation requirement and the amino acid composition of E. coli isocitrate lyase and compared these results to those obtained with other organisms.