isocitrate lyase

i·so·cit·rate ly·ase

an enzyme that catalyzes the reversible aldol condensation of glyoxylate and succinate, forming threo-ds-isocitrate; participates in the glyoxylate cycle.
References in periodicals archive ?
Isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 2.3.3.9) are the sole enzymes for this metabolic pathway.
The latter produces glyoxylate and succinate in the reaction catalyzed by isocitrate lyase. Further, glyoxylate condenses with a second acetyl-CoA molecule in a reaction catalyzed by malate synthase, after the malate produced is oxidized to oxaloacetate and thus regenerating the intermediate (steps B-1 to B-5, Figure 1).
Previously, some salicylanilide-based derivatives were reported as mild inhibitors of mycobacterial isocitrate lyase (ICL) and methionine aminopeptidase [3].
Isocitrate lyase (ICL; EC 4.1.3.1) is one of two enzymes comprising the glyoxylate shunt and splits isocitrate into succinate and glyoxylate; this metabolic pathway is absent in vertebrates.
When this 'switch' is turned on an enzyme called isocitrate lyase (ICL) is expressed, leading to activation of the T3SS.
Compounds that have potential activity versus nonmultiplying bacilli include congeners of metronidazole and isocitrate lyase inhibitors.
Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 2000; 406: 735-738.
The research program includes the pleuromutilins, a novel class of antibiotics, and two target-based projects, isocitrate lyase (Icl) and InhA.
tuberculosis that lack the gene for this enzyme, known as isocitrate lyase, had concentrations of the disease-causing bacteria in their lungs similar to those in mice infected with normal M.
Surprisingly large portions of the genome encode either enzymes of fatty acid metabolism, such as isocitrate lyase, or acidic, glycine-rich polypeptides of unknown function.
Also it was found that benzoxazoles inhibit essential bacterial enzymes, such as hyaluronan lyase [11] and isocitrate lyase [12], as well as bacterial two-component systems [29-31].
Bugg says the researchers have harvested plenty of new data from the remaining three: porcine pancreatic elastase (a pig enzyme similar to one that damages lung tissue in leukemia patients); isocitrate lyase (an enzyme in nematodes); and gamma interferon (a protein that stimulates the immune system).