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Journal articles on the topic 'Glyoxylate cycle'

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Published: 4 June 2021

Last updated: 3 February 2022

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1

Bruce, David. "Glyoxylate cycle as drug target?" Genome Biology 2 (2001): spotlight—20010710–01. http://dx.doi.org/10.1186/gb-spotlight-20010710-01.

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2

Yokota, A., S. Haga, and S. Kitaoka. "Purification and some properties of glyoxylate reductase (NADP+) and its functional location in mitochondria in Euglena gracilis z." Biochemical Journal 227, no. 1 (1985): 211–16. http://dx.doi.org/10.1042/bj2270211.

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Euglena mitochondria contain both glyoxylate reductase (NADP+) and glycollate dehydrogenase to constitute the glycollate-glyoxylate cycle [Yokota & Kitaoka (1979) Biochem. J. 184, 189-192]. Euglena glyoxylate reductase (NADP+) was purified and its submitochondrial location was determined in order to elucidate the cycle. The purified glyoxylate reductase was homogeneous on polyacrylamide-gel electrophoresis. Difference spectra of the purified enzyme revealed that the enzyme was a flavin enzyme. The Mr of the enzyme was 82 000. The enzyme was specific for NADPH, with an apparent Km of 3.9 mi

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3

Dunn, M. F., J. A. Ramírez-Trujillo, and I. Hernández-Lucas. "Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis." Microbiology 155, no. 10 (2009): 3166–75. http://dx.doi.org/10.1099/mic.0.030858-0.

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The glyoxylate cycle is an anaplerotic pathway of the tricarboxylic acid (TCA) cycle that allows growth on C2 compounds by bypassing the CO2-generating steps of the TCA cycle. The unique enzymes of this route are isocitrate lyase (ICL) and malate synthase (MS). ICL cleaves isocitrate to glyoxylate and succinate, and MS converts glyoxylate and acetyl-CoA to malate. The end products of the bypass can be used for gluconeogenesis and other biosynthetic processes. The glyoxylate cycle occurs in Eukarya, Bacteria and Archaea. Recent studies of ICL- and MS-deficient strains as well as proteomic and t

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4

Gonçalves, Itamar Luís, Albanin Aparecida Mielniczki-Pereira, Ana Claudia Piovezan Borges, and Alice Teresa Valduga. "Metabolic modeling and comparative biochemistry in glyoxylate cycle." Acta Scientiarum. Biological Sciences 38, no. 1 (2016): 1. http://dx.doi.org/10.4025/actascibiolsci.v38i1.24597.

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Glyoxylate cycle in fatty acid catabolism enhances net production of oxaloacetate, a substrate for gluconeogenesis, in certain bacteria, invertebrates and oilseed in the growth stage. A theoretical model was developed to calculate ATP amount produced in each step of the catabolic pathway, taking into account the fatty acid’s hydrocarbon chain size. Results showed a decrease in energy efficiency in glyoxylate cycle when compared to animal metabolism. Although the glyoxylate cycle provides evolutionary adaptations, it determines a smaller amount of energy produced per carbon atom when compared t

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5

Korotkova, Natalia, Mary E. Lidstrom, and Ludmila Chistoserdova. "Identification of Genes Involved in the Glyoxylate Regeneration Cycle in Methylobacterium extorquens AM1, Including Two New Genes, meaC and meaD." Journal of Bacteriology 187, no. 4 (2005): 1523–26. http://dx.doi.org/10.1128/jb.187.4.1523-1526.2005.

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ABSTRACT The glyoxylate regeneration cycle (GRC) operates in serine cycle methylotrophs to effect the net conversion of acetyl coenzyme A to glyoxylate. Mutants have been generated in several genes involved in the GRC, and phenotypic analysis has been carried out to clarify their role in this cycle.

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6

Lu, Ying, Yong-Rui Wu, and Bin Han. "Anaerobic Induction of Isocitrate Lyase and Malate Synthase in Submerged Rice Seedlings Indicates the Important Metabolic Role of the Glyoxylate Cycle." Acta Biochimica et Biophysica Sinica 37, no. 6 (2005): 406–14. http://dx.doi.org/10.1111/j.1745-7270.2005.00060.x.

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Abstract The glyoxylate cycle is a modified form of the tricarboxylic acid cycle that converts C2 compounds into C4 dicarboxylic acids at plant developmental stages. By studying submerged rice seedlings, we revealed the activation of the glyoxylate cycle by identifying the increased transcripts of mRNAs of the genes of isocitrate lyase (ICL) and malate synthase (MS), two characteristic enzymes of the glyoxylate cycle. Northern blot analysis showed that ICL and MS were activated in the prolonged anaerobic environment. The activity assay of pyruvate decarboxylase and ICL in the submerged seedlin

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7

Dolan, Stephen K., and Martin Welch. "The Glyoxylate Shunt, 60 Years On." Annual Review of Microbiology 72, no. 1 (2018): 309–30. http://dx.doi.org/10.1146/annurev-micro-090817-062257.

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2017 marks the 60th anniversary of Krebs’ seminal paper on the glyoxylate shunt (and coincidentally, also the 80th anniversary of his discovery of the citric acid cycle). Sixty years on, we have witnessed substantial developments in our understanding of how flux is partitioned between the glyoxylate shunt and the oxidative decarboxylation steps of the citric acid cycle. The last decade has shown us that the beautifully elegant textbook mechanism that regulates carbon flux through the shunt in E. coli is an oversimplification of the situation in many other bacteria. The aim of this review is to

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8

Zhou, X. "The glyoxylate cycle in Candida albicans infection." Trends in Biotechnology 19, no. 9 (2001): 330. http://dx.doi.org/10.1016/s0167-7799(01)01773-5.

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9

Alberty, Robert A. "Thermodynamics and Kinetics of the Glyoxylate Cycle†." Biochemistry 45, no. 51 (2006): 15838–43. http://dx.doi.org/10.1021/bi061829e.

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10

Pistelli, L., P. Perata, and A. Alpi. "Effect of Leaf Senescence on Glyoxylate Cycle Enzyme Activities." Functional Plant Biology 19, no. 6 (1992): 723. http://dx.doi.org/10.1071/pp9920723.

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In 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 time. The increased activities of malate synthase, isocitrate lyase, malate dehydrogenase and citrate synthase indicate that the glyoxylate cycle might be activated during the foliar senescence of leaf beet.

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11

Park, Yangshin, and Sangkee Rhee. "Crystal structure of isocitrate lyase from Magnaporthe grisea." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1667. http://dx.doi.org/10.1107/s2053273314083326.

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Glyoxylate cycle is a branched metabolic pathway in the TCA cycle that was initially discovered in microorganisms. The branched cycle plays an essential role in those organisms by providing the means for microorganisms to utilize acetate, ethanol, or fatty acids as carbon sources. In fact, pathogenic microorganisms rely on the glyoxylate cycle, rather than the TCA cycle, during infection. Therefore, the enzymes in the glyoxylate cycle of pathogens were suggested to be one of drug target molecules. Magnaporthe grisea isocitrate lyase (MgICL), a key enzyme in the cycle, is highly expressed durin

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12

Ritson, Dougal J. "A cyanosulfidic origin of the Krebs cycle." Science Advances 7, no. 33 (2021): eabh3981. http://dx.doi.org/10.1126/sciadv.abh3981.

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The centrality of the Krebs cycle in metabolism has long been interpreted as evidence of its antiquity, and consequently, questions regarding its provenance, and whether it initially functioned as a cycle or not, have received much attention. The present report shows that prebiotic oxidation of α-hydroxy carboxylates can be achieved by UV photolysis of a simple geochemical species (HS−), which leads to α-oxo carboxylates that feature in the Krebs cycle and glyoxylate shunt. Further reaction of these products leads to almost all intermediates of the Krebs cycle proper, succinate semialdehyde by

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13

García-de los Santos, Alejandro, Alejandro Morales, Laura Baldomá, et al. "TheglcBlocus ofRhizobium leguminosarumVF39 encodes an arabinose-inducible malate synthase." Canadian Journal of Microbiology 48, no. 10 (2002): 922–32. http://dx.doi.org/10.1139/w02-091.

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In the course of a study conducted to isolate genes upregulated by plant cell wall sugars, we identified an arabinose-inducible locus from a transcriptional fusion library of Rhizobium leguminosarum VF39, carrying random insertions of the lacZ transposon Tn5B22. Sequence analysis of the locus disrupted by the transposon revealed a high similarity to uncharacterized malate synthase G genes from Sinorhizobium meliloti, Agrobacterium tumefaciens, and Mesorhizobium loti. This enzyme catalyzes the condensation of glyoxylate and acetyl-CoA to yield malate and CoA and is thought to be a component of

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14

Lorenz, Michael C., and Gerald R. Fink. "The glyoxylate cycle is required for fungal virulence." Nature 412, no. 6842 (2001): 83–86. http://dx.doi.org/10.1038/35083594.

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15

Savvi, Suzana, Digby F. Warner, Bavesh D. Kana, John D. McKinney, Valerie Mizrahi, and Stephanie S. Dawes. "Functional Characterization of a Vitamin B12-Dependent Methylmalonyl Pathway in Mycobacterium tuberculosis: Implications for Propionate Metabolism during Growth on Fatty Acids." Journal of Bacteriology 190, no. 11 (2008): 3886–95. http://dx.doi.org/10.1128/jb.01767-07.

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ABSTRACT Mycobacterium tuberculosis is predicted to subsist on alternative carbon sources during persistence within the human host. Catabolism of odd- and branched-chain fatty acids, branched-chain amino acids, and cholesterol generates propionyl-coenzyme A (CoA) as a terminal, three-carbon (C3) product. Propionate constitutes a key precursor in lipid biosynthesis but is toxic if accumulated, potentially implicating its metabolism in M. tuberculosis pathogenesis. In addition to the well-characterized methylcitrate cycle, the M. tuberculosis genome contains a complete methylmalonyl pathway, inc

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16

Takada, Y., and T. Noguchi. "Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates." Biochemical Journal 231, no. 1 (1985): 157–63. http://dx.doi.org/10.1042/bj2310157.

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Alanine: glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had Mr about 80 000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5′-phosphate as cofactor. The apparent Km values were 2.1 mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkab

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17

Lee, Yong Joo, Jin Won Jang, Kyung Jin Kim, and Pil Jae Maeng. "TCA cycle-independent acetate metabolism via the glyoxylate cycle in Saccharomyces cerevisiae." Yeast 28, no. 2 (2010): 153–66. http://dx.doi.org/10.1002/yea.1828.

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18

Asakura, Makoto, Tetsuro Okuno, and Yoshitaka Takano. "Multiple Contributions of Peroxisomal Metabolic Function to Fungal Pathogenicity in Colletotrichum lagenarium." Applied and Environmental Microbiology 72, no. 9 (2006): 6345–54. http://dx.doi.org/10.1128/aem.00988-06.

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ABSTRACT In Colletotrichum lagenarium, which is the causal agent of cucumber anthracnose, PEX6 is required for peroxisome biogenesis and appressorium-mediated infection. To verify the roles of peroxisome-associated metabolism in fungal pathogenicity, we isolated and functionally characterized ICL1 of C. lagenarium, which encodes isocitrate lyase involved in the glyoxylate cycle in peroxisomes. The icl1 mutants failed to utilize fatty acids and acetate for growth. Although Icl1 has no typical peroxisomal targeting signals, expression analysis of the GFP-Icl1 fusion protein indicated that Icl1 l

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19

Ruch, Donald G., Kevin W. Burton, and Lee A. Ingram. "Occurrence of the Glyoxylate Cycle in Basidiospores of Homobasidiomycetes." Mycologia 83, no. 6 (1991): 821. http://dx.doi.org/10.2307/3760442.

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20

NAKATA, MITSUNORI, and CLAUDE P. SELITRENNIKOFF. "A Method to Assay Glyoxylate Cycle Inhibitors for Antifungals." Journal of Antibiotics 55, no. 6 (2002): 602–4. http://dx.doi.org/10.7164/antibiotics.55.602.

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21

Eley, James H. "GLYOXYLATE CYCLE ENZYME ACTIVITIES IN THE CYANOBACTERIUM ANACYSTIS NIDULANS." Journal of Phycology 24, no. 4 (1988): 586–88. http://dx.doi.org/10.1111/j.1529-8817.1988.tb04266.x.

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22

Ruch, Donald G., Kevin W. Burton, and Lee A. Ingram. "Occurrence of the Glyoxylate Cycle in Basidiospores of Homobasidiomycetes." Mycologia 83, no. 6 (1991): 821–25. http://dx.doi.org/10.1080/00275514.1991.12026089.

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23

Pistelli, Laura, Luigi De Bellis, and Amedeo Alpi. "Evidences of glyoxylate cycle in peroxisomes of senescent cotyledons." Plant Science 109, no. 1 (1995): 13–21. http://dx.doi.org/10.1016/0168-9452(95)04151-j.

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24

Erb, Tobias J., Lena Frerichs-Revermann, Georg Fuchs та Birgit E. Alber. "The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3S)-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3S)- Malyl-CoA Thioesterase". Journal of Bacteriology 192, № 5 (2010): 1249–58. http://dx.doi.org/10.1128/jb.01267-09.

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ABSTRACT Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the condensation of acetyl-CoA with glyoxylate. In the glyoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway the reaction is separated into two proteins: malyl-CoA lyase, a well-known enzyme catalyzing the Claisen condensation of acetyl-CoA with glyoxylate and yielding malyl-CoA, and an uniden

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25

Herter, Sylvia, Andreas Busch та Georg Fuchs. "l-Malyl-Coenzyme A Lyase/β-Methylmalyl-Coenzyme A Lyase from Chloroflexus aurantiacus, a Bifunctional Enzyme Involved in Autotrophic CO2 Fixation". Journal of Bacteriology 184, № 21 (2002): 5999–6006. http://dx.doi.org/10.1128/jb.184.21.5999-6006.2002.

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ABSTRACT The 3-hydroxypropionate cycle is a bicyclic autotrophic CO2 fixation pathway in the phototrophic Chloroflexus aurantiacus (Bacteria), and a similar pathway is operating in autotrophic members of the Sulfolobaceae (Archaea). The proposed pathway involves in a first cycle the conversion of acetyl-coenzyme A (acetyl-CoA) and two bicarbonates to l-malyl-CoA via 3-hydroxypropionate and propionyl-CoA; l-malyl-CoA is cleaved by l-malyl-CoA lyase into acetyl-CoA and glyoxylate. In a second cycle, glyoxylate and another molecule of propionyl-CoA (derived from acetyl-CoA and bicarbonate) are co

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26

Herter, Sylvia, Jan Farfsing, Nasser Gad'On, et al. "Autotrophic CO2 Fixation by Chloroflexus aurantiacus: Study of Glyoxylate Formation and Assimilation via the 3-Hydroxypropionate Cycle." Journal of Bacteriology 183, no. 14 (2001): 4305–16. http://dx.doi.org/10.1128/jb.183.14.4305-4316.2001.

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ABSTRACT In the facultative autotrophic organism Chloroflexus aurantiacus, a phototrophic green nonsulfur bacterium, the Calvin cycle does not appear to be operative in autotrophic carbon assimilation. An alternative cyclic pathway, the 3-hydroxypropionate cycle, has been proposed. In this pathway, acetyl coenzyme A (acetyl-CoA) is assumed to be converted to malate, and two CO2 molecules are thereby fixed. Malyl-CoA is supposed to be cleaved to acetyl-CoA, the starting molecule, and glyoxylate, the carbon fixation product. Malyl-CoA cleavage is shown here to be catalyzed by malyl-CoA lyase; th

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27

Nanchen, Annik, Alexander Schicker, and Uwe Sauer. "Nonlinear Dependency of Intracellular Fluxes on Growth Rate in Miniaturized Continuous Cultures of Escherichia coli." Applied and Environmental Microbiology 72, no. 2 (2006): 1164–72. http://dx.doi.org/10.1128/aem.72.2.1164-1172.2006.

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ABSTRACT A novel mini-scale chemostat system was developed for the physiological characterization of 10-ml cultures. The parallel operation of eight such mini-scale chemostats was exploited for systematic 13C analysis of intracellular fluxes over a broad range of growth rates in glucose-limited Escherichia coli. As expected, physiological variables changed monotonously with the dilution rate, allowing for the assessment of maintenance metabolism. Despite the linear dependence of total cellular carbon influx on dilution rate, the distribution of almost all major fluxes varied nonlinearly with d

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Nanchen, Annik, Alexander Schicker, Olga Revelles, and Uwe Sauer. "Cyclic AMP-Dependent Catabolite Repression Is the Dominant Control Mechanism of Metabolic Fluxes under Glucose Limitation in Escherichia coli." Journal of Bacteriology 190, no. 7 (2008): 2323–30. http://dx.doi.org/10.1128/jb.01353-07.

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ABSTRACT Although a whole arsenal of mechanisms are potentially involved in metabolic regulation, it is largely uncertain when, under which conditions, and to which extent a particular mechanism actually controls network fluxes and thus cellular physiology. Based on 13C flux analysis of Escherichia coli mutants, we elucidated the relevance of global transcriptional regulation by ArcA, ArcB, Cra, CreB, CreC, Crp, Cya, Fnr, Hns, Mlc, OmpR, and UspA on aerobic glucose catabolism in glucose-limited chemostat cultures at a growth rate of 0.1 h−1. The by far most relevant control mechanism was cycli

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29

Davis, W. L., R. G. Jones, and D. B. Goodman. "Cytochemical localization of malate synthase in amphibian fat body adipocytes: possible glyoxylate cycle in a vertebrate." Journal of Histochemistry & Cytochemistry 34, no. 5 (1986): 689–92. http://dx.doi.org/10.1177/34.5.3701032.

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The adipocytes of amphibian abdominal fat bodies contain typical microperoxisomes, as indicated by their fine structure. Electron microscopic cytochemistry showed that these organelles contain the enzymes catalase, typical for peroxisomes, and malate synthase. The latter is an enzymatic component characteristic of the glyoxylate cycle, a biochemical pathway known to exist in plant glyoxysomes (peroxisomes). This metabolic pathway makes possible the net conversion of lipid to carbohydrate. Toad adipocytes may represent yet another example of vertebrate peroxisomes which contain one of the marke

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30

Sarao, Renu, Howard D. McCurdy, and Luciano Passador. "Enzymes of the intermediary carbohydrate metabolism of Polyangium cellulosum." Canadian Journal of Microbiology 31, no. 12 (1985): 1142–46. http://dx.doi.org/10.1139/m85-215.

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Crude extracts of vegetative cells of the cellulolytic myxobacter Polyangium cellulosum contained significant levels of the enzymes of the tricarboxylic acid cycle and the glyoxylate cycle. Key enzymes of glycolysis and the pentose phosphate shunt were also detected. Specific activities of hexokinase and fructose- 1,6-diphosphate aldolase exhibited a 10-fold increase when the cells were grown in complex medium containing glucose. Cytochromes of a, b, and c type were demonstrated. By the use of a dispersly growing strain of P. cellulosum, its generation time was determined to be 22–24 h. This s

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31

Graham, Ian A., Katherine J. Denby, and Christopher J. Leaver. "Carbon Catabolite Repression Regulates Glyoxylate Cycle Gene Expression in Cucumber." Plant Cell 6, no. 5 (1994): 761. http://dx.doi.org/10.2307/3869878.

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32

Eastmond, Peter J., and Ian A. Graham. "Re-examining the role of the glyoxylate cycle in oilseeds." Trends in Plant Science 6, no. 2 (2001): 72–78. http://dx.doi.org/10.1016/s1360-1385(00)01835-5.

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Smith, S. "Does the glyoxylate cycle have an anaplerotic function in plants?" Trends in Plant Science 7, no. 1 (2002): 12–13. http://dx.doi.org/10.1016/s1360-1385(01)02189-6.

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Ensign, Scott A. "Revisiting the glyoxylate cycle: alternate pathways for microbial acetate assimilation." Molecular Microbiology 61, no. 2 (2006): 274–76. http://dx.doi.org/10.1111/j.1365-2958.2006.05247.x.

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35

Lee, Seung-Ho, You-Kyoung Han, Sung-Hwan Yun, and Yin-Won Lee. "Roles of the Glyoxylate and Methylcitrate Cycles in Sexual Development and Virulence in the Cereal Pathogen Gibberella zeae." Eukaryotic Cell 8, no. 8 (2009): 1155–64. http://dx.doi.org/10.1128/ec.00335-08.

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ABSTRACT The glyoxylate and methylcitrate cycles are involved in the metabolism of two- or three-carbon compounds in fungi. To elucidate the role(s) of these pathways in Gibberella zeae, which causes head blight in cereal crops, we focused on the functions of G. zeae orthologs (GzICL 1 and GzMCL1) of the genes that encode isocitrate lyase (ICL) and methylisocitrate lyase (MCL), respectively, key enzymes in each cycle. The deletion of GzICL1 (ΔGzICL1) caused defects in growth on acetate and in perithecium (sexual fruiting body) formation but not in virulence on barley and wheat, indicating that

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Korotkova, Natalia, Ludmila Chistoserdova, Vladimir Kuksa, and Mary E. Lidstrom. "Glyoxylate Regeneration Pathway in the Methylotroph Methylobacterium extorquens AM1." Journal of Bacteriology 184, no. 6 (2002): 1750–58. http://dx.doi.org/10.1128/jb.184.6.1750-1758.2002.

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ABSTRACT Most serine cycle methylotrophic bacteria lack isocitrate lyase and convert acetyl coenzyme A (acetyl-CoA) to glyoxylate via a novel pathway thought to involve butyryl-CoA and propionyl-CoA as intermediates. In this study we have used a genome analysis approach followed by mutation to test a number of genes for involvement in this novel pathway. We show that methylmalonyl-CoA mutase, an R-specific crotonase, isobutyryl-CoA dehydrogenase, and a GTPase are involved in glyoxylate regeneration. We also monitored the fate of 14C-labeled carbon originating from acetate, butyrate, or bicarbo

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Padilla-Guerrero, Israel Enrique, Larissa Barelli, Gloria Angélica González-Hernández, Juan Carlos Torres-Guzmán, and Michael J. Bidochka. "Flexible metabolism in Metarhizium anisopliae and Beauveria bassiana: role of the glyoxylate cycle during insect pathogenesis." Microbiology 157, no. 1 (2011): 199–208. http://dx.doi.org/10.1099/mic.0.042697-0.

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Insect pathogenic fungi such as Metarhizium anisopliae and Beauveria bassiana have an increasing role in the control of agricultural insect pests and vectors of human diseases. Many of the virulence factors are well studied but less is known of the metabolism of these fungi during the course of insect infection or saprobic growth. Here, we assessed enzyme activity and gene expression in the central carbon metabolic pathway, including isocitrate dehydrogenase, aconitase, citrate synthase, malate synthase (MLS) and isocitrate lyase (ICL), with particular attention to the glyoxylate cycle when M.

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Friedmann, Silke, Birgit E. Alber, and Georg Fuchs. "Properties of R-Citramalyl-Coenzyme A Lyase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of Chloroflexus aurantiacus." Journal of Bacteriology 189, no. 7 (2007): 2906–14. http://dx.doi.org/10.1128/jb.01620-06.

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ABSTRACT The autotrophic CO2 fixation pathway (3-hydroxypropionate cycle) in Chloroflexus aurantiacus results in the fixation of two molecules of bicarbonate into one molecule of glyoxylate. Glyoxylate conversion to the CO2 acceptor molecule acetyl-coenzyme A (CoA) requires condensation with propionyl-CoA (derived from one molecule of acetyl-CoA and one molecule of CO2) to β-methylmalyl-CoA, which is converted to citramalyl-CoA. Extracts of autotrophically grown cells contained both S- and R-citramalyl-CoA lyase activities, which formed acetyl-CoA and pyruvate. Pyruvate is taken out of the cyc

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Friedmann, Silke, Birgit E. Alber, and Georg Fuchs. "Properties of Succinyl-Coenzyme A:d-Citramalate Coenzyme A Transferase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of Chloroflexus aurantiacus." Journal of Bacteriology 188, no. 18 (2006): 6460–68. http://dx.doi.org/10.1128/jb.00659-06.

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ABSTRACT The phototrophic bacterium Chloroflexus aurantiacus uses the 3-hydroxypropionate cycle for autotrophic CO2 fixation. This cycle starts with acetyl-coenzyme A (CoA) and produces glyoxylate. Glyoxylate is an unconventional cell carbon precursor that needs special enzymes for assimilation. Glyoxylate is combined with propionyl-CoA to β-methylmalyl-CoA, which is converted to citramalate. Cell extracts catalyzed the succinyl-CoA-dependent conversion of citramalate to acetyl-CoA and pyruvate, the central cell carbon precursor. This reaction is due to the combined action of enzymes that were

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40

Meister, Michael, Stephan Saum, Birgit E. Alber та Georg Fuchs. "l-Malyl-Coenzyme A/β-Methylmalyl-Coenzyme A Lyase Is Involved in Acetate Assimilation of the Isocitrate Lyase-Negative Bacterium Rhodobacter capsulatus". Journal of Bacteriology 187, № 4 (2005): 1415–25. http://dx.doi.org/10.1128/jb.187.4.1415-1425.2005.

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ABSTRACT Cell extracts of Rhodobacter capsulatus grown on acetate contained an apparent malate synthase activity but lacked isocitrate lyase activity. Therefore, R. capsulatus cannot use the glyoxylate cycle for acetate assimilation, and a different pathway must exist. It is shown that the apparent malate synthase activity is due to the combination of a malyl-coenzyme A (CoA) lyase and a malyl-CoA-hydrolyzing enzyme. Malyl-CoA lyase activity was 20-fold up-regulated in acetate-grown cells versus glucose-grown cells. Malyl-CoA lyase was purified 250-fold with a recovery of 6%. The enzyme cataly

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Ostrenko, K. S., V. P. Galochkina, V. О. Lemiasheuski, et al. "Correlation of dicarboxylic acid cycle with tricarboxylic acid cycle in highly productive pigs." Proceedings of the National Academy of Sciences of Belarus. Agrarian Series 58, no. 2 (2020): 215–25. http://dx.doi.org/10.29235/1817-7204-2020-58-2-215-225.

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The paper is the fundamental beginning of research series aimed at understanding the processes associated with high performance in higher animals. The research aim is to study correlation of dicarboxylic acid cycle with tricarboxylic acid cycle with establishment of activity and dislocation of enzymes, confirming the hypothesis of availability and active metabolic participation of peroxisome in highly productive animals. Research was conducted on the basis of the VNIIFBiP animal vivarium in 2019 with a group of piglets of the Irish Landrace breed (n = 10). After slaughter at the age of 210 day

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Piekarska, Katarzyna, Els Mol, Marlene van den Berg та ін. "Peroxisomal Fatty Acid β-Oxidation Is Not Essential for Virulence of Candida albicans". Eukaryotic Cell 5, № 11 (2006): 1847–56. http://dx.doi.org/10.1128/ec.00093-06.

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ABSTRACT Phagocytic cells form the first line of defense against infections by the human fungal pathogen Candida albicans. Recent in vitro gene expression data suggest that upon phagocytosis by macrophages, C. albicans reprograms its metabolism to convert fatty acids into glucose by inducing the enzymes of the glyoxylate cycle and fatty acid β-oxidation pathway. Here, we asked whether fatty acid β-oxidation, a metabolic pathway localized to peroxisomes, is essential for fungal virulence by constructing two C. albicans double deletion strains: a pex5Δ/pex5Δ mutant, which is disturbed in the imp

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Han, Sung Ok, Masayuki Inui, and Hideaki Yukawa. "Transcription of Corynebacterium glutamicum Genes Involved in Tricarboxylic Acid Cycle and Glyoxylate Cycle." Journal of Molecular Microbiology and Biotechnology 15, no. 4 (2008): 264–76. http://dx.doi.org/10.1159/000117614.

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Hooks, Mark A., J. William Allwood, Joanna K. D. Harrison, et al. "Selective induction and subcellular distribution of ACONITASE 3 reveal the importance of cytosolic citrate metabolism during lipid mobilization in Arabidopsis." Biochemical Journal 463, no. 2 (2014): 309–17. http://dx.doi.org/10.1042/bj20140430.

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The cytosolic location of AtACO3 and its importance in citrate metabolism support the operation of the classic glyoxylate cycle and not direct mitochondrial metabolism of citrate during lipid mobilization in seedlings of oilseed plants, such as Arabidopsis.

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Wendisch, Volker F., Albert A. de Graaf, Hermann Sahm, and Bernhard J. Eikmanns. "Quantitative Determination of Metabolic Fluxes during Coutilization of Two Carbon Sources: Comparative Analyses withCorynebacterium glutamicum during Growth on Acetate and/or Glucose." Journal of Bacteriology 182, no. 11 (2000): 3088–96. http://dx.doi.org/10.1128/jb.182.11.3088-3096.2000.

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ABSTRACT Growth of Corynebacterium glutamicum on mixtures of the carbon sources glucose and acetate is shown to be distinct from growth on either substrate alone. The organism showed nondiauxic growth on media containing acetate-glucose mixtures and simultaneously metabolized these substrates. Compared to those for growth on acetate or glucose alone, the consumption rates of the individual substrates were reduced during acetate-glucose cometabolism, resulting in similar total carbon consumption rates for the three conditions. By13C-labeling experiments with subsequent nuclear magnetic resonanc

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Umair, Saleh, Charlotte Bouchet, Nikola Palevich, and Heather V. Simpson. "Characterisation and structural analysis of glyoxylate cycle enzymes of Teladorsagia circumcincta." Molecular and Biochemical Parasitology 240 (November 2020): 111335. http://dx.doi.org/10.1016/j.molbiopara.2020.111335.

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Yang, Y., H. Murayama, and T. Fukushima. "Activation of Glyoxylate Cycle Enzymes in Cucumber Fruits Exposed to CO2." Plant and Cell Physiology 39, no. 5 (1998): 533–39. http://dx.doi.org/10.1093/oxfordjournals.pcp.a029401.

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ONO, KOUKI, MAKI KONDO, TETSUAKI OSAFUNE, et al. "Presence of Glyoxylate Cycle Enzymes in the Mitochondria of Euglena gracilis." Journal of Eukaryotic Microbiology 50, no. 2 (2003): 92–96. http://dx.doi.org/10.1111/j.1550-7408.2003.tb00239.x.

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Han, L., and K. A. Reynolds. "A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes." Journal of bacteriology 179, no. 16 (1997): 5157–64. http://dx.doi.org/10.1128/jb.179.16.5157-5164.1997.

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de Bellis, Luigi, Makoto Hayashi, Mikio Nishimura, and Amedeo Alpi. "Cytosolic Aconitase Participates in the Glyoxylate Cycle in Etiolated Pumpkin Cotyledons." Giornale botanico italiano 129, no. 4 (1995): 940. http://dx.doi.org/10.1080/11263509509440869.

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