Caenorhabditis elegans and Ascaris suum: inhibition of isocitrate lyase by itaconate |
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Authors: | T R Patel B A McFadden |
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Affiliation: | Program in Biochemistry and Biophysics, Chemistry Department, Washington State University, Pullman, Washington 99164, U.S.A. |
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Abstract: | The largest forms of isocitrate lyase from Caenorhabditis elegans and Ascaris suum of 543,000 and 549,000 daltons, respectively, can be purified from three- to five-fold in excellent yield by pelleting from extracts at 160,000g for 4 hr. Isocitrate lyase in the pellet is much more stable toward proteolysis. Itaconate which both inhibits isocitrate lyase and suppresses the level of this enzyme in bacteria inhibits the partially purified isocitrate lyase from both C. elegans and A. suum. The inhibition is noncompetitive with respect to ds-isocitrate at one itaconate concentration. The Ki values at 30 C, pH 7.7, are 19 and 7.3 μM for the enzyme from C. elegans and A. suum, respectively. Itaconate inhibits the growth of C. elegans in random axenic as well as monoxenic cultures. At a concentration of 10 mM, itaconate is more effective in the inhibition of random axenic cultures than is oxalate, maleate, or succinate. At 60 mM itaconate, reproduction of C. elegans larvae is completely abolished. |
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Keywords: | Free-living nematode Parasitic nematode Isocitrate lyase (EC 4.1.3.1) Itaconate Isocitrate lyase purification Itaconate Inhibition of growth Itaconate Inhibition of isocitrate lyase |
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