Results 221 to 230 of about 18,230 (249)

Isocitrate lyase localisation in Saccharomyces cerevisiae cells

Gene, 1997
The 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 ...
Pilar Herrero, Fernando Moreno, Romina S Chaves, Isabel Ordiz, Marı́a de los Angeles del Brı́o   +4 more
openaire   +3 more sources

Bromophenols as Candida albicans isocitrate lyase inhibitors

Bioorganic & Medicinal Chemistry Letters, 2010
A 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,
Dongsik Yang, Yu-Ri Han, Ki-Bong Oh, Jiyoung Park, Yeon-Ju Lee, Jongheon Shin, Heung Bae Jeon, Hyi-Seung Lee, So-Hyoung Lee, Mihyun Kwon   +9 more
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Purification, Identification, and Characterization of Peanut Isocitrate Lyase

Journal of Agricultural and Food Chemistry, 2008
Isocitrate 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 ...
Ping-Lin Ong, Shing-Fei Lin, Robin Y.-Y. Chiou, Chun-Ru Jhou   +3 more
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Isolation and characterization of isocitrate lyase of castor endosperm

Archives of Biochemistry and Biophysics, 1982
Abstract 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 ...
Malhotra Op, Pramod K. Srivastava
openaire   +3 more sources

Escherichia coli isocitrate lyase: properties and comparisons

Biochimica et Biophysica Acta (BBA) - General Subjects, 1988
The 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.
Henry C. Reeves, Eugene F. Robertson, Jeffrey C. Hoyt, Kathleen A. Berlyn   +3 more
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A new continuous optical assay for isocitrate lyase

Experientia, 1984
A new continuous optical assay method for isocitrate lyase is reported. This is a coupled assay which requires lactate dehydrogenase as an ancillary enzyme. The method yields linear data up to 0.12 units/ml. The assay is also suitable for crude extracts.
GIACHETTI, EUGENIO, PINZAUTI, GIANCARLO, VANNI, PAOLO   +2 more
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Stereochemistry of the isocitrate lyase reaction

Biochemical and Biophysical Research Communications, 1964
David B. Sprinson, M. Sprecher, R. Berger   +2 more
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Isocitrate lyase from Neurospora crassa

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
M. Kobr, Gilbert Turian
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Development of a versatile and efficient C–N lyase platform for asymmetric hydroamination via computational enzyme redesign

Nature Catalysis, 2021
Ying-Lu Cui, Tong Zhu, Bian Wu
exaly  

The role of isocitrate lyase in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
H.L. Kornberg, J.M. Ashworth
openaire   +3 more sources