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Targeting isocitrate lyase for the treatment of latent tuberculosis
Drug Discovery Today, 2017Tuberculosis (TB) is an infectious disease caused by Mycobacterium tuberculosis that can remain dormant for many years before becoming active. One way to control and eliminate TB is the identification and treatment of latent TB, preventing infected individuals from developing active TB and thus eliminating the subsequent spread of the disease ...
Ram Prasad Bhusal +4 more
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Determination of isocitrate lyase activity in polyacrylamide gels
Analytical Biochemistry, 1972Abstract Isocitrate lyase (EC 4.1.3.1), the first enzyme of the glyoxylate cycle, catalyzes the aldol cleavage of threo- d s(+)-isocitric acid to succinic and glyoxylic acids. The enzyme plays a key role in the metabolism of short-chain fatty acids and has been found to be essential both in microbial growth on C2-compounds and in gluconeogenesis in ...
H C, Reeves, M J, Volk
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1969
Publisher Summary The anaplerotie function of isocitrate lyase and malate synthase during microbial growth on acetate is well documented. Catalysis by these enzymes is also vital in the conversion of lipid reserves to carbohydrates, as found, for example, early in the germination of fatty plant seedlings.
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Publisher Summary The anaplerotie function of isocitrate lyase and malate synthase during microbial growth on acetate is well documented. Catalysis by these enzymes is also vital in the conversion of lipid reserves to carbohydrates, as found, for example, early in the germination of fatty plant seedlings.
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Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine
Molecular and Cellular Biochemistry, 1977Recently it has been demonstrated that hydroxylamine is an activator of triglyceride catabolism. We have studied the effect of hydroxylamine on isocitrate lyase activity and lipid catabolism and have noted a stimulation of isocitrate lyase biosynthesis by 5 mM hydroxylamine.
VANNI, PAOLO +3 more
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Advances in Mycobacterial Isocitrate Lyase Targeting and Inhibitors
Current Medicinal Chemistry, 2012Isocitrate lyase plays a key role for survival of Mycobacterium tuberculosis in the latent form during a chronic stage of infection. This enzyme is important for M. tuberculosis during steady stage growth when it converts isocitrate to succinate and glyoxylate. Then, the glyoxylate is condensed with acetyl-CoA to form malate by malate synthase.
M, Krátký, J, Vinšová
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Purification, Identification, and Characterization of Peanut Isocitrate Lyase
Journal of Agricultural and Food Chemistry, 2008Isocitrate lyase (ICL, EC 4.1.3.1) is commonly present in oil-rich seeds in catalyzing the cleavage of isocitrate to glyoxylate and succinate and plays an essential role in lipid metabolism and gluconeogenesis. When peanut kernels (Tainan 14) were germinated at 30 degrees C, the cotyledon ICL activities increased substantially in the initial 4 days ...
Shing-Fei, Lin +3 more
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Bromophenols as Candida albicans isocitrate lyase inhibitors
Bioorganic & Medicinal Chemistry Letters, 2010A new series of bromophenols was synthesized by reactions of corresponding phenol analogs with bromine. The synthesized compounds were tested for inhibitory activity against isocitrate lyase (ICL) of Candida albicans and antimicrobial activity against gram-positive and, gram-negative bacteria and fungi. Among the synthesized bromophenols, bis(3-bromo-4,
Ki-Bong, Oh +9 more
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Isocitrate lyase localisation in Saccharomyces cerevisiae cells
Gene, 1997The isocitrate lyase from Saccharomyces cerevisiae was only located in the cell cytoplasm. This protein was found not to be associated with cell organelles, even under growth conditions that induce peroxisome proliferation. This conclusion is supported by experiments carried out by damaging the protoplast plasma membrane with DEAE-dextran, by ...
R S, Chaves +4 more
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Isolation and characterization of isocitrate lyase of castor endosperm
Archives of Biochemistry and Biophysics, 1982Abstract Isocitrate lyase (threo-DS-isocitrate glyoxylate-lyase, EC 4.1.3.1) has been purified to homogeneity from castor endosperm. The enzyme is a tetrameric protein (molecular weight about 140,000; gel filtration) made up of apparently identical monomers (subunit molecular weight about 35,000; gel electrophoresis in the presence of sodium dodecyl ...
O P, Malhotra, P K, Srivastava
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Escherichia coli isocitrate lyase: properties and comparisons
Biochimica et Biophysica Acta (BBA) - General Subjects, 1988The 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.
J C, Hoyt +3 more
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