Regulation of isocitrate metabolism in Chlamydomonas segnis

1977 ◽  
Vol 55 (16) ◽  
pp. 2178-2185 ◽  
Author(s):  
Samuel S. K. Foo ◽  
Samir S. Badour
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Nitrogen Deficiency ◽  
Competitive Inhibitor ◽  
Enzyme Preparations ◽  
Batch Cultures ◽  
Keto Acids ◽  
Effective Inhibition ◽  
Lyase Activity

Isocitrate lyase (EC 4.1.3.1) and isocitrate dehydrogenase (NADP+) (EC 1.1.1.42) activities were detected in cell-free extracts of Chlamydomonas segnis Ettl when the alga was grown photoautotrophically with 5% CO2 in air (v/v) at 11 klx. When the cultures were either bubbled with air (0.03% CO2), exposed to low light intensity (3 klx), or subjected to manganese or nitrogen deficiency, isocitrate lyase activity was undetectable. During growth in batch cultures provided with 5% CO2, the activity of the dehydrogenase was about 5–12 times greater than the lyase.Using partially purified (about 50-fold) enzyme preparations, isocitrate dehydrogenase (NADP+) showed greater affinity for isocitrate (Km = 0.008 mM) than did isocitrate lyase (Km = 0.1 mM). The dehydrogenase had Km values of 0.011 mM and 0.006 mM for NADP and Mn2+, respectively. Both enzymes were inhibited by α-ketoglutarate and oxalacetate at 1 mM, but the dehydrogenase was more sensitive to these two keto acids (68–79%) than the lyase (36%). Glycolate at 1 mM inhibited (36%) only the lyase, while glyoxylate had little effect. The dehydrogenase was subject to concerted inhibition by oxalacetate plus glyoxylate (Ki = 0.01 mM). This inhibition was competitive with respect to isocitrate, and preincubation of the enzyme with NADP in absence of isocitrate was necessary for effective inhibition. Each of NADPH (Ki = 0.06 mM) and ATP (Ki = 0.65 mM) was a non-competitive inhibitor (with respect to isocitrate) of isocitrate dehydrogenase (NADP+), and both nucleotides are suggested to be active in the in vivo regulation of isocitrate metabolism in C. segnis during photoautotrophy.

Photo-induction sexuée du pyrénomycète Nectria galligena: influence de la mycosporine sur le rapport des activités NADPM+-socitrate déshydrogénase/isocitrate lyase

1989 ◽  
Vol 67 (2) ◽  
pp. 447-450 ◽  
Author(s):  
B. Dehorter ◽  
L. Lacoste
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Nectria Galligena ◽  
Lyase Activity ◽  
Growth Of Fungi ◽  
The Glyoxylate Cycle

The activity of two enzymes of the tricarboxylic acid cycle (NADP+-isocitrate dehydrogenase, EC 1.1.1.42) and the glyoxylate cycle (isocitrate lyase, EC 4.1.3.1) were assayed in vitro to determine the effects of darkness, light, and mycosporin (P310) on sexual morphogenesis in Nectria galligena Bres. In the absence of mycosporin, high isocitrate lyase activity was associated with vegetative growth of fungi kept in the dark. In contrast, light-induced perithecial development and mycosporin biosynthesis could be correlated with high ratios of isocitrate dehydrogenase to isocitrate lyase activity. This was confirmed by the fact that when mycosporin was added to the nutrient medium with incubation in darkness, the fertility of the fungus was partially expressed and the activity of isocitrate lyase was significantly reduced. Thus this enzyme would be repressed in vivo by mycosporin. Because of its photomimetic role in sexual differentiation and regulation of intermediate metabolism, mycosporin appears to be a biochemical transmitter of light energy required for the formation of ascocarps.

Acetate metabolism in Escherichia coli

1978 ◽  
Vol 24 (2) ◽  
pp. 149-153 ◽  
Author(s):  
T. M. Lakshmi ◽  
Robert B. Helling
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Citrate Synthase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Acetate Metabolism ◽  
Wild Type ◽  
Intermediary Metabolites ◽  
Lyase Activity ◽  
Acetate Medium ◽  
The Glyoxylate Cycle

Levels of several intermediary metabolites were measured in cells grown in acetate medium in order to test the hypothesis that the glyoxylate cycle is repressed by phosphoenolpyruvate (PEP). Wild-type cells had less PEP than either isocitrate dehydrogenase – deficient cells (which had greater isocitrate lyase activity than the wild type) or isocitrate dehydrogenase – deficient, citrate synthase – deficient cells (which are poorly inducible). Thus induction of the glyoxylate cycle is more complicated than a simple function of PEP concentration. No correlation between enzyme activity and the level of oxaloacetate, pyruvate, or citrate was found either. Citrate was synthesized in citrate synthase – deficient mutants, possibly via citrate lyase.

scholarly journals RegA Plays a Key Role in Oxygen-Dependent Establishment of Persistence and in Isocitrate Lyase Activity, a Critical Determinant of In vivo Brucella suis Pathogenicity

2017 ◽  
Vol 7 ◽  
Author(s):  
Elias Abdou ◽  
María P. Jiménez de Bagüés ◽  
Ignacio Martínez-Abadía ◽  
Safia Ouahrani-Bettache ◽  
Véronique Pantesco ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Critical Determinant ◽  
Brucella Suis ◽  
Lyase Activity

AN ASSESSMENT OF THE POSSIBLE ROLE OF 17α,20α-DIHYDROXY-4-PREGNEN-3-ONE IN THE REGULATION OF TESTOSTERONE SYNTHESIS BY RAT AND RABBIT TESTIS

1974 ◽  
Vol 61 (3) ◽  
pp. 401-410 ◽  
Author(s):  
H. W. A. de BRUIJN ◽  
H. J. van der MOLEN
Keyword(s):  
Venous Blood ◽  
Competitive Inhibitor ◽  
Testicular Tissue ◽  
Seminiferous Tubules ◽  
Interstitial Tissue ◽  
Lyase Activity ◽  
Testosterone Biosynthesis

SUMMARY 17α,20α-Dihydroxy-4-pregnen-3-one is a competitive inhibitor of C17,20-lyase activity in rat testicular tissue in vitro and the significance of this inhibition in vitro was evaluated for testosterone biosynthesis in rat and rabbit testis in vivo. It is concluded that 17α,20α-dihydroxy-4-pregnen-3-one is not involved in the regulation of C17,20-activity in vivo, because it was not possible to detect any 17α,20α-dihydroxy-4-pregnen-3-one in rat and rabbit testicular tissue or in testicular venous blood. If present, the levels are lower than 10 pmol/g testis. Levels of 17α-hydroxyprogester-one are in the order of 50 pmol/g testis. The C17,20-lyase has a higher affinity for 17α-hydroxyprogesterone than for 17α,20α-dihydroxy-4-pregnen-3-one and hence inhibition under in-vivo conditions is not favoured. In rat testes the 20α-hydroxysteroid dehydrogenase activity, which can convert 17α-hydroxyprogesterone to 17α,20α-dihydroxy-4-pregnen-3-one, was found to be mainly (97%) localized in the seminiferous tubules and not at the site of testosterone formation in the interstitial tissue.

scholarly journals Tin-protoporphyrin suppression of hyperbilirubinemia in mutant mice with severe hemolytic anemia

Blood ◽  
1983 ◽  
Vol 61 (5) ◽  
pp. 1011-1013 ◽  
Author(s):  
S Sassa ◽  
GS Drummond ◽  
SE Bernstein ◽  
A Kappas
Keyword(s):  
Heme Oxygenase ◽  
Competitive Inhibitor ◽  
Mutant Mice ◽  
Hemolytic Disease ◽  
Enzyme Preparations ◽  
Substantial Inhibition ◽  
Plasma Bilirubin ◽  
Tin Protoporphyrin

Abstract Tin-protoporphyrin is a potent competitive inhibitor of heme oxygenase both in vivo in animals and in vitro in isolated enzyme preparations, and when administered to neonatal rats, prevents the development of postnatal hyperbilirubinemia. In this study we examined the effect of the metalloporphyrin on the activity of heme oxygenase in liver, kidney, and spleen, and on the level of bilirubin in plasma in three types of anemic mutant mice with severe hemolytic diseases. We report that the administration of tin-protoporphyrin to anemic mutants homozygous for severe hemolytic disease results in substantial inhibition of heme oxidation in liver, spleen, and kidney and in significant reduction of plasma bilirubin levels. Tin-protoporphyrin thus has the capacity to significantly inhibit in vivo heme degradation and to concurrently diminish plasma bilirubin levels in severe chronic hemolytic disorders.

scholarly journals DEVELOPMENTAL STUDIES ON GLYOXYSOMES IN RICINUS ENDOSPERM

1970 ◽  
Vol 44 (1) ◽  
pp. 94-102 ◽  
Author(s):  
B. P. Gerhardt ◽  
Harry Beevers
Keyword(s):  
Enzyme Activities ◽  
Isocitrate Lyase ◽  
Total Activity ◽  
Early Growth ◽  
Soluble Form ◽  
Synthetase Activity ◽  
Developmental Studies ◽  
Lyase Activity ◽  
Specific Activities

The development of glyoxysomes and their associated enzymes, isocitrate lyase and malate synthetase, was studied in the endosperm of castor bean seeds during germination and early growth in darkness. The protein content of the glyoxysome fraction, separated by sucrose density centrifugation, increased linearly from day 2 to day 4 and declined subsequently, while maximum enzyme activities were reached at day 5. The specific activities of the enzymes in the glyoxysomes increased until day 5 and remained constant thereafter. At all stages of germination the only organelle with isocitrate lyase activity was the glyoxysome, but at the earlier stages a greater portion of the total activity was recovered in the soluble form. Malate synthetase was found primarily in the glyoxysomes after day 4, but at earlier stages part of the activity appeared at regions of lower density on the sucrose gradient. It was shown that this particulate malate synthetase activity was due to glyoxysomes broken during preparation, and that, as a result of this breakage, isocitrate lyase was solubilized. We conclude that both enzymes are housed in the glyoxysome in vivo throughout the germination period, and that the rise and fall in enzyme activities in phase with fat breakdown correspond to the net production and destruction of this organelle.

scholarly journals Tin-protoporphyrin suppression of hyperbilirubinemia in mutant mice with severe hemolytic anemia

Blood ◽  
1983 ◽  
Vol 61 (5) ◽  
pp. 1011-1013
Author(s):  
S Sassa ◽  
GS Drummond ◽  
SE Bernstein ◽  
A Kappas
Keyword(s):  
Heme Oxygenase ◽  
Competitive Inhibitor ◽  
Mutant Mice ◽  
Hemolytic Disease ◽  
Enzyme Preparations ◽  
Substantial Inhibition ◽  
Plasma Bilirubin ◽  
Tin Protoporphyrin

Tin-protoporphyrin is a potent competitive inhibitor of heme oxygenase both in vivo in animals and in vitro in isolated enzyme preparations, and when administered to neonatal rats, prevents the development of postnatal hyperbilirubinemia. In this study we examined the effect of the metalloporphyrin on the activity of heme oxygenase in liver, kidney, and spleen, and on the level of bilirubin in plasma in three types of anemic mutant mice with severe hemolytic diseases. We report that the administration of tin-protoporphyrin to anemic mutants homozygous for severe hemolytic disease results in substantial inhibition of heme oxidation in liver, spleen, and kidney and in significant reduction of plasma bilirubin levels. Tin-protoporphyrin thus has the capacity to significantly inhibit in vivo heme degradation and to concurrently diminish plasma bilirubin levels in severe chronic hemolytic disorders.

Metabolic activity of acetate-grown Bacillus megaterium KM

1970 ◽  
Vol 16 (12) ◽  
pp. 1199-1203 ◽  
Author(s):  
A. Donawa ◽  
W. E. Inniss
Keyword(s):  
Bacillus Megaterium ◽  
Isocitrate Dehydrogenase ◽  
De Novo ◽  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Malate Synthase ◽  
Concerted Action ◽  
Lyase Activity ◽  
Glyoxylate Pathway

Acetate-grown Bacillus megaterium KM possessed high isocitrate lyase and malate synthase activity as compared to glucose-grown cells. Chloramphenicol prevented the increase in isocitrate lyase activity when cells were transferred from glucose to acetate media, indicating that such an increase in activity was probably due to de novo protein synthesis.The affinity of the substrate, isocitrate, was greater for isocitrate dehydrogenase than for isocitrate lyase. Phosphoenolpyruvate was found to inhibit isocitrate lyase non-competitively. The concerted action of glyoxylate and oxaloacetate was capable of inhibiting isocitrate dehydrogenase. The role such factors play in the balancing of the tricarboxylic acid cycle and the glyoxylate pathway in the microorganism is considered.

Effective inhibition of irradiation on human gliomas growth in vitro and in vivo after epidermal growth factor receptor silencing with RNA interference

Neuroreport ◽  
2011 ◽  
Vol 22 (15) ◽  
pp. 773-777
Author(s):  
Guangbin Cui ◽  
Tao Zhang ◽  
Longxiao Wei ◽  
Pang Du ◽  
Feng Zhang ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Rna Interference ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Human Gliomas ◽  
Effective Inhibition ◽  
Epidermal Growth

scholarly journals Isocitrate Lyase Activity in Lactobacillus murinus CNRZ 313

1983 ◽  
Vol 66 (6) ◽  
pp. 1232-1236 ◽  
Author(s):  
M.C. Albizzatti de Rivadeneira ◽  
M.C. Manca de Nadra ◽  
A.A. Pesce de Ruiz Holgado ◽  
G. Oliver
Keyword(s):  
Isocitrate Lyase ◽  
Lyase Activity ◽  
Lactobacillus Murinus
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