Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of key enzymes of the citrate (CC), glyoxylate (GC), and pentose phosphate cycles (PPC) was determined in the cells of Candida lipolytica and Candida tropicalis growing on hexadecane and glucose. The activity of isocitrate lyase and malate synthase (enzymes of GC) was very high in hexadecane grown cells but was almost absent in "glucose" grown. The activity of citrate synthase and aconitase was 2-4 times and 1.5-2 times, respectively, higher in the cells, grown on n-alkane. The activity of citrate synthase of "hexadecane" and "glucose" yeasts was higher than the activity of other enzymes of CC (aconitase and isocitrate dehydrogenase), especially in the "hexadecane" cells. The activity of the key enzymes of PPC was almost the same in the yeast cells, grown on "hexadecane" and "glucose". Possible factors causing differences in the activities of the enzymes of GC and CC are discussed. Yeast organisms incapable to grow on n-alkanes were found to be able to grow on acetate (43 strains belonging to 35 yeast species have been studied) and to have a high activity of isocitrate lyase. Therefore, the absence of growth of many yeast strains on n-alkanes is not caused by the absence of the activity of enzymes of GC in these strains.
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PMID:[The activity of citrate glyoxylate and pentosephosphate cycle enzymes during yeast growth on hexadecane and glucose]. 94 Apr 96

The activity of key enzymes of the citrate and glyoxylate cycles was compared in yeast cells during intensive synthesis of citric acids and in its absence in the course of growth of Candida lipolytica on glucose ("glucose" yeast cells) and on hexadecane ("hexadecane" yeast cells). Citrate and isocitrate were found to be formed by the yeast in the tricarboxylic acid cycle. The ability of the yeast for "overproduction" of citrate and isocitrate during its growth on glucose and hexadecane depends on the high activity of the key enzyme of cycle, citrate synthase, as compared with the activity of other enzymes of the tricarboxylic acid cycle. Citrate predominated among excreted acids during growth on glucose in conditions of nitrogen deficiency while isocitrate prevailed during growth on hexadecane. The predominating synthesis of citrate in the first case seems to be related to a lower activity of aconitase in the "glucose" cells as compared with the "hexadecane" cells.
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PMID:[Enzyme activity of citrate, glyoxylate and pentosephosphate cycles during synthesis of citric acids by Candida lipolytica]. 100 46

The activity of enzymes of the citrate and glyoxylate cycles was comparatively assayed in the parent strain of Candida lipolytica producing citric and isocitric acids in a medium with hexadecane and in its two mutants one of which produced citrate and the other synthesized isocitrate. The enzyme activities were determined in the dynamics of the yeast growth: (a) in the exponential growth phase (no production of the acids); (b) in the lag phase (the beginning of the acid production); and (c) in the stationary phase (active production of the acids). All of the strains had a high activity of citrate synthase. The mutant producing citrate exhibited a high activity of isocitrate lyase and a low activity of aconitate hydratase, whereas the mutant producing isocitrate manifested a high activity of aconitate hydrase and a low activity of isocitrate dehydrogenase and isocitrate lyase. The data pertinent to a change in the enzyme activities due to the growth limitation with a nitrogen source and the production of the acids are considered for explaining the mechanism of overproduction of citric and isocitric acids from n-alkanes by yeast organisms.
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PMID:[Citrate and glyoxylate cycle enzyme activity in citric and isocitric acid synthesis by different strains of Candida lipolytica]. 707 Mar 6