Results 181 to 190 of about 57,138 (236)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
ISOCITRATE LYASE IN AN ALGINOLYTIC BACTERIUM
Canadian Journal of Microbiology, 1963Glyoxylate has been discerned as an apparent intermediate in mannuronate dissimilation by A. alginicum. Isocitrate lyase was demonstrated in extracts of the bacterium, even after prolonged culture on seawater nutrient broth. Resting cells were able to oxidize glyoxylate slowly, but none of the enzymes usually accounting for glyoxylate catabolism were ...
Joy Williams, R. L. Todd, W. J. Payne
openaire +1 more source
On the Mechanism of Action of Isocitrate Lyase
European Journal of Biochemistry, 1975The enzymes citrate lyase and isocitrate lyase catalyse similar reactions in the cleavage of citrate to acetate plus oxaloacetate and of isocitrate to succinate plus glyoxylate, respectively. Nevertheless, the mechanism of action of each enzyme appears to be different from each other. Citrate lyase is an acyl carrier protein‐containing enzyme complex
P, Dimroth, K, Mayer, H, Eggerer
openaire +2 more sources
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.
openaire +1 more source
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.
openaire +1 more source
Isocitrate lyase in Coprinus lagopus (sensu Buller)
Canadian Journal of Microbiology, 1969Isocitrate lyase activity was detected in cell-free extracts of both a monokaryon and a dikaryon of Coprinus lagopus sensu Buller grown in media containing either acetate or glucose as carbon source. The activity in extracts of mycelium grown in an acetate medium was greater than that in extracts of mycelium grown in a glucose medium but marked ...
P J, Casselton +2 more
openaire +2 more sources
Genetics and function of isocitrate lyase in Coprinus
Molecular and General Genetics MGG, 1977Thirteen chromosomal loci have been identified which affect acetate metabolism in Coprinus. Mutants at only two loci, acu-l and acu-7, are deficient in isocitrate lyase (ICL) (EC 4.1.3.1) activity. acu-1 mutants are unable to induce ICL because they lack acetyl-CoA synthetase which is required to convert acetate to the metabolic inducer of ICL.
H B, King, L A, Casselton
openaire +2 more sources
Isocitrate lyase from parasitic and free-living nematodes
Archives of Biochemistry and Biophysics, 1975Abstract Isocitrate lyase and malate synthase were demonstrated in the soil nematode Caenorhabditis elegans and the isocitrate lyase partially characterized and compared with that from embryos of the hog roundworm Ascaris lumbricoides . Both enzymes have similar pH optima, molecular weights and K m s for isocitrate.
W J, Colonna, B A, McFadden
openaire +2 more sources
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
openaire +2 more sources
Studies on isocitrate lyase isolated from Lupinus cotyledons
Canadian Journal of Biochemistry, 1979Isocitrate lyase (threo-Ds-isocitrate glyoxylate-lyase, EC 4.1.3.1) was isolated from cotyledons of Lupinus seedlings, purified 100-fold with respect to its initial specific activity and characterized (Km, pH optimum, Mg2+ requirement, sulfhydryl inhibitors, and synthase activity).
VANNI, PAOLO +3 more
openaire +3 more sources
Catabolite inactivation of isocitrate lyase from Saccharomyces cerevisiae
Archives of Microbiology, 1987A reversible carbon catabolite inactivation step is described for isocitrate lyase from Saccharomyces cerevisiae. This reversible inactivation step of isocitrate lyase is similar to that described for fructose 1,6-bisphosphatase. Addition of 2,4-dinitrophenol, nystatin or glucose to cultures, grown in ethanol as carbon source, caused a rapid loss of ...
Y S, López-Boado +3 more
openaire +2 more sources