Results 201 to 210 of about 29,848 (251)
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2009
Some organisms possess enzymes that allow the net conversion of acetyl-CoA to succinate. This is accomplished by the glyoxylate cycle. The overall reaction of this cycle is: 2 acetyl-CoA + NAD + 2 H2O -> succinate + 2 CoA-SH + NADH + H+ As becomes clear from case studies presented, except from prokaryotes, this pathway does not operate as a real ...
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Some organisms possess enzymes that allow the net conversion of acetyl-CoA to succinate. This is accomplished by the glyoxylate cycle. The overall reaction of this cycle is: 2 acetyl-CoA + NAD + 2 H2O -> succinate + 2 CoA-SH + NADH + H+ As becomes clear from case studies presented, except from prokaryotes, this pathway does not operate as a real ...
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Effect of Leaf Senescence on Glyoxylate Cycle Enzyme Activities
Australian Journal of Plant Physiology, 1992In order to elucidate the metabolism of the peroxisomes during foliar senescence of leaf beet (Beta vulgaris L., var. cicla), peroxisomal activities have been determined at various stages of senescence. Catalase and hydroxypyruvate reductase activities decreased whereas those of the β-oxidation pathway and glyoxylate cycle enzymes increased at the same
PISTELLI, LAURA, Perata P., ALPI, AMEDEO
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Thermodynamics and Kinetics of the Glyoxylate Cycle
Biochemistry, 2006Because the standard Gibbs energies of formation of all the species of reactants in the glyoxylate cycle are known at 298.15 K, it is possible to calculate the apparent equilibrium constants of the five reactions in the cycle in the pH range 5-9 and ionic strengths from 0 to approximately 0.35 M.
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Microbodies and glyoxylate-cycle enzyme activities in filamentous fungi
Planta, 1975Microbodies were observed in the hyphal tips of all 14 fungi investigated. Their morphology varied among the fungi and their numbers were influenced by the growth medium. Microbodies were closely associated with mitochondria in one fungus and with the endoplasmic reticulum in several fungi.
D P, Maxwell +5 more
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Particulate enzymes of the glyoxylate cycle in Neurospora crassa
Biochemical and Biophysical Research Communications, 1969Abstract A particle carrying at least some of the enzymes of the glyoxylate cycle was found in Neurospora crassa . This particle has a density different from that of the mitochondrion. The proportion of the isocitrate lyase bound to this particle varies with the composition of the carbon source.
M J, Kobr +2 more
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Tricarboxylic acid and glyoxylate cycles in the "Leishmaniae"
Acta tropica, 1977Cell-free extacts of four species of Leishmania (L. brasiliensis, L. donovani, L. mexicana and L. tropica) have been shown to contain all enzymes of the tricarboxylic acid cycle. However, the activity of citrate synthase is so low that it is doubtful whether this pathway is of significance in the metabolism of carbohydrate substrates.
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Evidences of glyoxylate cycle in peroxisomes of senescent cotyledons
Plant Science, 1995Abstract The metabolic pathway of the glyoxylate cycle has been investigated in peroxisomes isolated from senescent pumpkin ( Cucurbita sp.) cotyledons. β-oxidation activity, as well as activities of glyoxylate cycle enzymes isocitrate lyase (EC 4.1.3.1), malate synthase (EC 4.1.3.2), malate dehydrogenase (EC 1.1.1.37) and citrate synthase (EC 4.1.3.
PISTELLI, LAURA +2 more
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TCA cycle‐independent acetate metabolism via the glyoxylate cycle in Saccharomyces cerevisiae
Yeast, 2010AbstractIn Saccharomyces cerevisiae, the accepted theory is that due to TCA cycle dysfunction, the Δcit1 mutant lacking the mitochondrial enzyme citrate synthase (Cit1) cannot grow on acetate, regardless of the presence of the peroxisomal isoenzyme (Cit2). In this study, we re‐evaluated the roles of Cit1 and Cit2 in acetate utilization and examined the
Yong Joo, Lee +3 more
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Synthesis and Function of Glyoxylate Cycle Enzymes
2002The glyoxylate cycle in plants has been the subject of much research for several decades, and many hundreds of primary research papers have been published. There have been numerous reviews covering different aspects of the synthesis and function of glyoxylate cycle enzymes (Beevers, 1979; Trelease, 1984; Escher and Widmer 1997; Eastmond and Graham ...
Johanna E. Cornah, Steven M. Smith
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The glyoxylate cycle in Candida albicans infection
Trends in Biotechnology, 2001Candida albicans, a normal component of the mammalian gastrointestinal flora, causes most fungal infections in immunosuppressed patients. Candida is normally phagocytosed by macrophages and neutrophils. Neutropenic patients, deficient in these immune cells, are particularly susceptible to systemic candidiasis.
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