PMID:2673042
| Citation |
Ko, YH, Vanni, P and McFadden, BA (1989) The interaction of 3-phosphoglycerate and other substrate analogs with the glyoxylate- and succinate-binding sites of isocitrate lyase. Arch. Biochem. Biophys. 274:155-60 |
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| Abstract |
The gene for isocitrate lyase from Escherichia coli has recently been cloned and sequenced. However, knowledge of this enzyme from E. coli is limited. Because of the possible role of 3-phosphoglycerate as a metabolic inhibitor of isocitrate lyase in E. coli, a detailed analysis of this compound as an inhibitor is reported in this paper. Kinetic data suggest that 3-phosphoglycerate is an analog of isocitrate (or glyoxylate) and also that it competes with succinate, or succinate analogs, by interfering with their binding to the enzyme. This could be due to the steric bulk of the phosphate moiety of 3-phosphoglycerate extending in the direction of and over the succinate-binding site. The interaction of other substrate analogs, including glycolate, oxalate, phosphoenolpyruvate, and cis-aconitate, with isocitrate lyase from E. coli is also characterized. |
| Links | |
| Keywords |
Binding Sites; Binding, Competitive; Escherichia coli/enzymology; Glyceric Acids/metabolism; Glyoxylates/metabolism; Isocitrate Lyase/isolation & purification; Isocitrate Lyase/metabolism; Kinetics; Models, Theoretical; Oxo-Acid-Lyases/metabolism; Substrate Specificity; Succinates/metabolism |
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