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Journal articles on the topic 'Glyoxylate metabolism'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Dellero, Younès, Mathieu Jossier, Jessica Schmitz, Veronica G. Maurino, and Michael Hodges. "Photorespiratory glycolate–glyoxylate metabolism." Journal of Experimental Botany 67, no. 10 (2016): 3041–52. http://dx.doi.org/10.1093/jxb/erw090.

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2

Baker, Paul R. S., Scott D. Cramer, Martha Kennedy, Dean G. Assimos, and Ross P. Holmes. "Glycolate and glyoxylate metabolism in HepG2 cells." American Journal of Physiology-Cell Physiology 287, no. 5 (2004): C1359—C1365. http://dx.doi.org/10.1152/ajpcell.00238.2004.

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Oxalate synthesis in human hepatocytes is not well defined despite the clinical significance of its overproduction in diseases such as the primary hyperoxalurias. To further define these steps, the metabolism to oxalate of the oxalate precursors glycolate and glyoxylate and the possible pathways involved were examined in HepG2 cells. These cells were found to contain oxalate, glyoxylate, and glycolate as intracellular metabolites and to excrete oxalate and glycolate into the medium. Glycolate was taken up more effectively by cells than glyoxylate, but glyoxylate was more efficiently converted

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3

Han, Qian, Cihan Yang, Jun Lu, Yinai Zhang, and Jianyong Li. "Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Betalyase Plays in Hyperoxaluria." Current Medicinal Chemistry 26, no. 26 (2019): 4944–63. http://dx.doi.org/10.2174/0929867326666190325095223.

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Hyperoxaluria, excessive urinary oxalate excretion, is a significant health problem worldwide. Disrupted oxalate metabolism has been implicated in hyperoxaluria and accordingly, an enzymatic disturbance in oxalate biosynthesis can result in the primary hyperoxaluria. Alanine-glyoxylate aminotransferase-1 and glyoxylate reductase, the enzymes involving glyoxylate (precursor for oxalate) metabolism, have been related to primary hyperoxalurias. Some studies suggest that other enzymes such as glycolate oxidase and alanine-glyoxylate aminotransferase-2 might be associated with primary hyperoxaluria

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4

Puckett, Susan, Carolina Trujillo, Zhe Wang, et al. "Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation inMycobacterium tuberculosis." Proceedings of the National Academy of Sciences 114, no. 11 (2017): E2225—E2232. http://dx.doi.org/10.1073/pnas.1617655114.

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The glyoxylate shunt is a metabolic pathway of bacteria, fungi, and plants used to assimilate even-chain fatty acids (FAs) and has been implicated in persistence ofMycobacterium tuberculosis(Mtb). Recent work, however, showed that the first enzyme of the glyoxylate shunt, isocitrate lyase (ICL), may mediate survival ofMtbduring the acute and chronic phases of infection in mice through physiologic functions apart from fatty acid metabolism. Here, we report that malate synthase (MS), the second enzyme of the glyoxylate shunt, is essential for in vitro growth and survival ofMtbon even-chain fatty

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5

Grostern, Ariel, Christopher M. Sales, Wei-Qin Zhuang, Onur Erbilgin, and Lisa Alvarez-Cohen. "Glyoxylate Metabolism Is a Key Feature of the Metabolic Degradation of 1,4-Dioxane by Pseudonocardia dioxanivorans Strain CB1190." Applied and Environmental Microbiology 78, no. 9 (2012): 3298–308. http://dx.doi.org/10.1128/aem.00067-12.

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ABSTRACTThe groundwater contaminant 1,4-dioxane (dioxane) is transformed by several monooxygenase-expressing microorganisms, but only a few of these, includingPseudonocardia dioxanivoransstrain CB1190, can metabolize the compound as a sole carbon and energy source. However, nothing is yet known about the genetic basis of dioxane metabolism. In this study, we used a microarray to study differential expression of genes in strain CB1190 grown on dioxane, glycolate (a previously identified intermediate of dioxane degradation), or pyruvate. Of eight multicomponent monooxygenase gene clusters carrie

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6

Knight, John, Ross P. Holmes, Scott D. Cramer, Tatsuya Takayama, and Eduardo Salido. "Hydroxyproline metabolism in mouse models of primary hyperoxaluria." American Journal of Physiology-Renal Physiology 302, no. 6 (2012): F688—F693. http://dx.doi.org/10.1152/ajprenal.00473.2011.

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Primary hyperoxaluria type 1 (PH1) and type 2 (PH2) are rare genetic diseases that result from deficiencies in glyoxylate metabolism. The increased oxalate synthesis that occurs can lead to kidney stone formation, deposition of calcium oxalate in the kidney and other tissues, and renal failure. Hydroxyproline (Hyp) catabolism, which occurs mainly in the liver and kidney, is a prominent source of glyoxylate and could account for a significant portion of the oxalate produced in PH. To determine the sensitivity of mouse models of PH1 and PH2 to Hyp-derived oxalate, animals were fed diets containi

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7

Donini, Stefano, Manuela Ferrari, Chiara Fedeli, et al. "Recombinant production of eight human cytosolic aminotransferases and assessment of their potential involvement in glyoxylate metabolism." Biochemical Journal 422, no. 2 (2009): 265–72. http://dx.doi.org/10.1042/bj20090748.

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PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Even though pre-genomic studies indicate that other human transaminases can convert glyoxylate into glycine, in PH1 patients these enzymes are apparently unable to compensate for the lack of AGXT, perhaps due to their limited levels of expression, their localization in an inappropriate cell compartment or the scarcity of the

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8

NUÑEZ, M. Felisa, M. Teresa PELLICER, Josefa BADIA, Juan AGUILAR, and Laura BALDOMA. "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli." Biochemical Journal 354, no. 3 (2001): 707–15. http://dx.doi.org/10.1042/bj3540707.

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Glyoxylate is an important intermediate of the central microbial metabolism formed from acetate, allantoin or glycolate. Depending on the physiological conditions, glyoxylate is incorporated into the central metabolism by the combined actions of the activity of malate synthase and the D-glycerate pathway, or alternatively it can be reduced to glycolate by constitutive glyoxylate reductase activity. At present no information is available on this latter enzyme in Escherichia coli, although similar enzymes, classified as 2-hydroxyacid dehydrogenases, have been characterized in other organisms. A

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9

Kleczkowski, L. A., D. D. Randall, and G. E. Edwards. "Oxalate as a potent and selective inhibitor of spinach (Spinacia oleracea) leaf NADPH-dependent hydroxypyruvate reductase." Biochemical Journal 276, no. 1 (1991): 125–27. http://dx.doi.org/10.1042/bj2760125.

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Purified spinach (Spinacia oleracea) NADPH-preferring hydroxypyruvate reductase (HPR-2) was potently and selectively inhibited by oxalate, an end product of metabolism in plants. Both hydroxypyruvate- and glyoxylate-dependent rates of the HPR-2 enzyme were affected. Oxalate acted as an uncompetitive inhibitor of the enzyme, with Ki values of 7 and 36 microM for the NADPH/hydroxypyruvate and NADPH/glyoxylate pairs of reactants respectively. Oxalate, at millimolar levels, caused less than 10% inhibition of purified spinach NADH-preferring HPR (HPR-1) and had no effect on purified spinach NADPH-p

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10

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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11

Noguchi, Tomoo, Satoko Fujiwara, and Sueko Hayashi. "Amino Acid and Glyoxylate Metabolism in Animal Peroxisomes." Journal of the Kyushu Dental Society 57, no. 4 (2003): 85–93. http://dx.doi.org/10.2504/kds.57.85.

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12

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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13

NISHIJIMA, Saori, Kimio SUGAYA, Sanehiro HOKAMA, et al. "Effect of vitamin B6 deficiency on glyoxylate metabolism in rats with or without glyoxylate overload." Biomedical Research 27, no. 3 (2006): 93–98. http://dx.doi.org/10.2220/biomedres.27.93.

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14

Pey, Angel L., Armando Albert, and Eduardo Salido. "Protein Homeostasis Defects of Alanine-Glyoxylate Aminotransferase: New Therapeutic Strategies in Primary Hyperoxaluria Type I." BioMed Research International 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/687658.

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Alanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine and glyoxylate to produce pyruvate and glycine using pyridoxal 5′-phosphate (PLP) as cofactor. Human alanine-glyoxylate aminotransferase is a peroxisomal enzyme expressed in the hepatocytes, the main site of glyoxylate detoxification. Its deficit causes primary hyperoxaluria type I, a rare but severe inborn error of metabolism. Single amino acid changes are the main type of mutation causing this disease, and considerable effort has been dedicated to the understanding of the molecular consequences of such missens

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15

Kleczkowski, L. A., D. D. Randall, and D. G. Blevins. "Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase." Biochemical Journal 239, no. 3 (1986): 653–59. http://dx.doi.org/10.1042/bj2390653.

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A novel reductase displaying high specificity for glyoxylate and NADPH was purified 3343-fold from spinach leaves. The enzyme was found to be an oligomer of about 125 kDa, composed of four equal subunits of 33 kDa each. A Km for glyoxylate was about 14-fold lower with NADPH than with NADH (0.085 and 1.10 mM respectively), but the maximal activity, 210 mumol/min per mg of protein, was similar with either cofactor. Km values for NADPH and NADH were 3 and 150 microM respectively. Optimal rates with either NADPH or NADH were found in the pH range 6.5-7.4. The enzyme also showed some reactivity tow

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16

Nikiforova, Victoria J., Pieter Giesbertz, Jan Wiemer, et al. "Glyoxylate, a New Marker Metabolite of Type 2 Diabetes." Journal of Diabetes Research 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/685204.

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Type 2 diabetes (T2D) is characterized by a variety of metabolic impairments that are closely linked to nonenzymatic glycation reactions of proteins and peptides resulting in advanced glycation end-products (AGEs). Reactive aldehydes derived from sugars play an important role in the generation of AGEs. Using metabolite profiling to characterize human plasma from diabetic versus nondiabetic subjects we observed in a recent study that the reactive aldehyde glyoxylate was increased before high levels of plasma glucose, typical for a diabetic condition, could be measured. Following this observatio

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17

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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18

Bais, Renze, Allan M. Rofe, and Robert A. J. Conyers. "Inhibition of endogenous oxalate production: biochemical considerations of the roles of glycollate oxidase and lactate dehydrogenase." Clinical Science 76, no. 3 (1989): 303–9. http://dx.doi.org/10.1042/cs0760303.

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1. Both the peroxisomal, flavin-linked glycollate oxidase [(S)-2-hydroxy-acid oxidase; EC 1.1.3.15] and the cytosolic, nicotinamide–adenine dinucleotide (NAD)-linked lactate dehydrogenase (l-lactate dehydrogenase; EC 1.1.1.27) are thought to contribute to the formation of oxalate from its immediate precursors, glycollate and glyoxylate, but the relative contributions of each enzyme to endogenous oxalate production is not known. 2. In rat liver homogenates, [14C]oxalate production from labelled glycollate is halved and that from labelled glyoxylate is increased fourfold by the addition of eithe

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19

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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20

Jiang, Juquan, Lynnette C. Johnson, John Knight, et al. "Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria." American Journal of Physiology-Gastrointestinal and Liver Physiology 302, no. 6 (2012): G637—G643. http://dx.doi.org/10.1152/ajpgi.00331.2011.

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Hydroxyproline (Hyp) metabolism is a key source of glyoxylate production in the body and may be a major contributor to excessive oxalate production in the primary hyperoxalurias where glyoxylate metabolism is impaired. Important gaps in our knowledge include identification of the tissues with the capacity to degrade Hyp and the development of model systems to study this metabolism and how to suppress it. The expression of mRNA for enzymes in the pathway was examined in 15 different human tissues. Expression of the complete pathway was identified in liver, kidney, pancreas, and small intestine.

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21

Behnam, Joseph T., Emma L. Williams, Susanne Brink, Gill Rumsby, and Christopher J. Danpure. "Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells." Biochemical Journal 394, no. 2 (2006): 409–16. http://dx.doi.org/10.1042/bj20051397.

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Failure to detoxify the intermediary metabolite glyoxylate in human hepatocytes underlies the metabolic pathology of two potentially lethal hereditary calcium oxalate kidney stone diseases, PH (primary hyperoxaluria) types 1 and 2. In order to define more clearly the roles of enzymes involved in the metabolism of glyoxylate, we have established singly, doubly and triply transformed CHO (Chinese-hamster ovary) cell lines, expressing all combinations of normal human AGT (alanine:glyoxylate aminotransferase; the enzyme deficient in PH1), GR/HPR (glyoxylate/hydroxypyruvate reductase; the enzyme de

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22

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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23

Holmes, R. P., C. H. Hurst, D. G. Assimos, and H. O. Goodman. "Glucagon increases urinary oxalate excretion in the guinea pig." American Journal of Physiology-Endocrinology and Metabolism 269, no. 3 (1995): E568—E574. http://dx.doi.org/10.1152/ajpendo.1995.269.3.e568.

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Factors that influence hepatic oxalate synthesis are poorly defined. Hormones are important regulators of hepatic metabolism and could potentially be involved. The effects of hyperglucagonemia were examined in guinea pigs injected with either saline or pharmacological doses of glucagon for 4 days. Glucagon treatment increased mean urinary oxalate excretion by 77% in male and 34% in female animals. The levels of hepatic peroxisomal enzymes involved in oxalate synthesis declined with glucagon treatment, but experiments with isolated peroxisomes indicated that oxalate synthesis in vitro was unaff

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24

Kukreja, Anjli, Melissa Lasaro, Christian Cobaugh, et al. "Systemic Alanine Glyoxylate Aminotransferase mRNA Improves Glyoxylate Metabolism in a Mouse Model of Primary Hyperoxaluria Type 1." Nucleic Acid Therapeutics 29, no. 2 (2019): 104–13. http://dx.doi.org/10.1089/nat.2018.0740.

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25

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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26

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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27

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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28

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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29

Rojony, Rajoana, Lia Danelishvili, Anaamika Campeau, Jacob M. Wozniak, David J. Gonzalez, and Luiz E. Bermudez. "Exposure of Mycobacterium abscessus to Environmental Stress and Clinically Used Antibiotics Reveals Common Proteome Response among Pathogenic Mycobacteria." Microorganisms 8, no. 5 (2020): 698. http://dx.doi.org/10.3390/microorganisms8050698.

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Mycobacterium abscessus subsp. abscessus (MAB) is a clinically important nontuberculous mycobacterium (NTM) causing pulmonary infection in patients such as cystic fibrosis and bronchiectasis. MAB is naturally resistant to the majority of available antibiotics. In attempts to identify the fundamental response of MAB to aerobic, anaerobic, and biofilm conditions (as it is encountered in patients) and during exposure to antibiotics, we studied bacterial proteome using tandem mass tag mass spectrometry sequencing. Numerous de novo synthesized proteins belonging to diverse metabolic pathways were f

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Okubo, Yoko, Song Yang, Ludmila Chistoserdova, and Mary E. Lidstrom. "Alternative Route for Glyoxylate Consumption during Growth on Two-Carbon Compounds by Methylobacterium extorquens AM1." Journal of Bacteriology 192, no. 7 (2010): 1813–23. http://dx.doi.org/10.1128/jb.01166-09.

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ABSTRACT Methylobacterium extorquens AM1 is a facultative methylotroph capable of growth on both single-carbon and multicarbon compounds. Mutants defective in a pathway involved in converting acetyl-coenzyme A (CoA) to glyoxylate (the ethylmalonyl-CoA pathway) are unable to grow on both C1 and C2 compounds, showing that both modes of growth have this pathway in common. However, growth on C2 compounds via the ethylmalonyl-CoA pathway should require glyoxylate consumption via malate synthase, but a mutant lacking malyl-CoA/β-methylmalyl-CoA lyase activity (MclA1) that is assumed to be responsibl

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31

Hoover, Gordon J., Owen R. Van Cauwenberghe, Kevin E. Breitkreuz, Shawn M. Clark, A. Rod Merrill, and Barry J. Shelp. "Characteristics of an Arabidopsis glyoxylate reductase: general biochemical properties and substrate specificity for the recombinant protein, and developmental expression and implications for glyoxylate and succinic semialdehyde metabolism in planta." Canadian Journal of Botany 85, no. 9 (2007): 883–95. http://dx.doi.org/10.1139/b07-081.

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Constitutive expression of an Arabidopsis thaliana (L.) Heynh cDNA (GenBank accession No. AY044183 ) in a succinic semialdehyde (SSA) dehydrogenase-deficient yeast ( Saccharomyces cerevisiae Hansen) mutant enables growth on γ-aminobutyrate and significantly enhances the accumulation of γ-hydroxybutyrate. In this report, the cDNA (designated hereinafter as AtGR1) was functionally expressed in Escherichia coli , and the recombinant protein purified to homogeneity. Kinetic analysis of substrate specificity revealed that the enzyme catalyzed the conversion of glyoxylate to glycolate (Km, glyoxylat

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32

Liberti, D., J. A. Rollins, and K. F. Dobinson. "Peroxysomal Carnitine Acetyl Transferase Influences Host Colonization Capacity in Sclerotinia sclerotiorum." Molecular Plant-Microbe Interactions® 26, no. 7 (2013): 768–80. http://dx.doi.org/10.1094/mpmi-03-13-0075-r.

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In lower eukaryotes, the glyoxylate cycle allows cells to utilize two-carbon compounds when simple sugars are not available. In filamentous fungi, glyoxylate metabolism is coupled with β-oxidation of fatty acids, and both are localized to ubiquitous eukaryotic organelles called peroxisomes. Acetyl coenzyme A (acetyl-CoA) produced during β-oxidation is transported via the cytosol into mitochondria for further metabolism. A peroxisomal-specific pathway for acetyl-CoA transport requiring peroxisomal carnitine acetyl transferase (CAT) activity has been identified in Magnaporthe grisea peroxisomes.

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Ramírez, Melissa A., and Michael C. Lorenz. "Mutations in Alternative Carbon Utilization Pathways in Candida albicans Attenuate Virulence and Confer Pleiotropic Phenotypes." Eukaryotic Cell 6, no. 2 (2006): 280–90. http://dx.doi.org/10.1128/ec.00372-06.

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ABSTRACT The interaction between Candida albicans and cells of the innate immune system is a key determinant of disease progression. Transcriptional profiling has revealed that C. albicans has a complex response to phagocytosis, much of which is similar to carbon starvation. This suggests that nutrient limitation is a significant stress in vivo, and we have shown that glyoxylate cycle mutants are less virulent in mice. To examine whether other aspects of carbon metabolism are important in vivo during an infection, we have constructed strains lacking FOX2 and FBP1, which encode key components o

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Caterino, Marianna, Margherita Ruoppolo, Guglielmo Rosario Domenico Villani, et al. "Influence of Sex on Urinary Organic Acids: A Cross-Sectional Study in Children." International Journal of Molecular Sciences 21, no. 2 (2020): 582. http://dx.doi.org/10.3390/ijms21020582.

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The characterization of urinary metabolome, which provides a fingerprint for each individual, is an important step to reach personalized medicine. It is influenced by exogenous and endogenous factors; among them, we investigated sex influences on 72 organic acids measured through GC-MS analysis in the urine of 291 children (152 males; 139 females) aging 1–36 months and stratified in four groups of age. Among the 72 urinary metabolites, in all age groups, 4-hydroxy-butirate and homogentisate are found only in males, whereas 3-hydroxy-dodecanoate, methylcitrate, and phenylacetate are found only

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35

Donèche, Bernard. "Carbohydrate metabolism and gluconic acid synthesis by Botrytis cinerea." Canadian Journal of Botany 67, no. 10 (1989): 2888–93. http://dx.doi.org/10.1139/b89-370.

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The pathways of glucose catabolism were examined in a B. cinerea strain isolated from grape. Respirometric and enzymatic studies indicated that this plant parasite catabolized glucose through the Embden–Meyerhof and hexose monophosphate shunt pathways. Data also suggested functioning of an active tricarboxylic acid cycle and presence of the glyoxylate cycle. Direct oxidation of glucose by means of glucose oxidase led to gluconic acid accumulation in the medium during the stationary phase of growth. Part of the glucose oxidase was extracellular and could have technological consequences in wine

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McCammon, Mark T. "Mutants of Saccharomyces cerevisiae with Defects in Acetate Metabolism: Isolation and Characterization of Acn− Mutants." Genetics 144, no. 1 (1996): 57–69. http://dx.doi.org/10.1093/genetics/144.1.57.

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Abstract The two carbon compounds, ethanol and acetate, can be oxidatively metabolized as well as assimilated into carbohydrate in the yeast Saccharomyces cerevisiae. The distribution of acetate metabolic enzymes among several cellular compartments, mitochondria, peroxisomes, and cytoplasm makes it an intriguing system to study complex metabolic interactions. To investigate the complex process of carbon catabolism and assimilation, mutants unable to grow on acetate were isolated. One hundred five Acn− (“Acetate Nonutilizing”) mutants were sorted into 21 complementation groups with an additiona

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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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Shelp, Barry J., Gale G. Bozzo, Christopher P. Trobacher, Greta Chiu та Vikramjit S. Bajwa. "Strategies and tools for studying the metabolism and function of γ-aminobutyrate in plants. I. Pathway structure". Botany 90, № 8 (2012): 651–68. http://dx.doi.org/10.1139/b2012-030.

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γ-Aminobutyrate (GABA) is a ubiquitous four-C, nonprotein, amino acid that has been linked to stress, signaling, and storage in plants. In this paper, we discuss analytical, enzyme-linked, and colorimetric methods for analyzing GABA and related metabolites, and review tracer evidence for the derivation of GABA from glutamate and its subsequent catabolism to succinic semialdehyde and either succinate or γ-hydroxybutyrate. Also, we describe biochemical, complementation, bioinformatic, recombinant, and modelling strategies for identifying genes and investigating properties of the encoded proteins

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Meijer, S., J. Otero, R. Olivares, M. R. Andersen, L. Olsson, and J. Nielsen. "Overexpression of isocitrate lyase—glyoxylate bypass influence on metabolism in Aspergillus niger." Metabolic Engineering 11, no. 2 (2009): 107–16. http://dx.doi.org/10.1016/j.ymben.2008.12.002.

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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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Belostotsky, Ruth, James Jonathon Pitt, and Yaacov Frishberg. "Primary hyperoxaluria type III—a model for studying perturbations in glyoxylate metabolism." Journal of Molecular Medicine 90, no. 12 (2012): 1497–504. http://dx.doi.org/10.1007/s00109-012-0930-z.

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Dean, Jason T., Matthew L. Rizk, Yikun Tan, Katrina M. Dipple, and James C. Liao. "Ensemble Modeling of Hepatic Fatty Acid Metabolism with a Synthetic Glyoxylate Shunt." Biophysical Journal 98, no. 8 (2010): 1385–95. http://dx.doi.org/10.1016/j.bpj.2009.12.4308.

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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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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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McVey, Alyssa C., Sean Bartlett, Mahmud Kajbaf, et al. "2-Aminopyridine Analogs Inhibit Both Enzymes of the Glyoxylate Shunt in Pseudomonas aeruginosa." International Journal of Molecular Sciences 21, no. 7 (2020): 2490. http://dx.doi.org/10.3390/ijms21072490.

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Pseudomonas aeruginosa is an opportunistic pathogen responsible for many hospital-acquired infections. P. aeruginosa can thrive in diverse infection scenarios by rewiring its central metabolism. An example of this is the production of biomass from C2 nutrient sources such as acetate via the glyoxylate shunt when glucose is not available. The glyoxylate shunt is comprised of two enzymes, isocitrate lyase (ICL) and malate synthase G (MS), and flux through the shunt is essential for the survival of the organism in mammalian systems. In this study, we characterized the mode of action and cytotoxic

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Tang, Yinjie J., Judy S. Hwang, David E. Wemmer, and Jay D. Keasling. "Shewanella oneidensis MR-1 Fluxome under Various Oxygen Conditions." Applied and Environmental Microbiology 73, no. 3 (2006): 718–29. http://dx.doi.org/10.1128/aem.01532-06.

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ABSTRACT The central metabolic fluxes of Shewanella oneidensis MR-1 were examined under carbon-limited (aerobic) and oxygen-limited (microaerobic) chemostat conditions, using 13C-labeled lactate as the sole carbon source. The carbon labeling patterns of key amino acids in biomass were probed using both gas chromatography-mass spectrometry (GC-MS) and 13C nuclear magnetic resonance (NMR). Based on the genome annotation, a metabolic pathway model was constructed to quantify the central metabolic flux distributions. The model showed that the tricarboxylic acid (TCA) cycle is the major carbon meta

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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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Han, Qian, Seong Ryul Kim, Haizhen Ding, and Jianyong Li. "Evolution of two alanine glyoxylate aminotransferases in mosquito." Biochemical Journal 397, no. 3 (2006): 473–81. http://dx.doi.org/10.1042/bj20060469.

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In the mosquito, transamination of 3-HK (3-hydroxykynurenine) to XA (xanthurenic acid) is catalysed by an AGT (alanine glyoxylate aminotransferase) and is the major branch pathway of tryptophan metabolism. Interestingly, malaria parasites hijack this pathway to use XA as a chemical signal for development in the mosquito. Here, we report that the mosquito has two AGT isoenzymes. One is the previously cloned AeHKT [Aedes aegypti HKT (3-HK transaminase)] [Han, Fang and Li (2002) J. Biol. Chem. 277, 15781–15787], similar to hAGT (human AGT), which primarily catalyses 3-HK to XA in mosquitoes, and

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Harambat, Jérôme, Sonia Fargue, Justine Bacchetta, Cécile Acquaviva, and Pierre Cochat. "Primary Hyperoxaluria." International Journal of Nephrology 2011 (2011): 1–11. http://dx.doi.org/10.4061/2011/864580.

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Primary hyperoxalurias (PH) are inborn errors in the metabolism of glyoxylate and oxalate. PH type 1, the most common form, is an autosomal recessive disorder caused by a deficiency of the liver-specific enzyme alanine, glyoxylate aminotransferase (AGT) resulting in overproduction and excessive urinary excretion of oxalate. Recurrent urolithiasis and nephrocalcinosis are the hallmarks of the disease. As glomerular filtration rate decreases due to progressive renal damage, oxalate accumulates leading to systemic oxalosis. Diagnosis is often delayed and is based on clinical and sonographic findi

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NISHIJIMA, SAORI, KIMIO SUGAYA, MAKOTO MOROZUMI, TADASHI HATANO, and YOSHIHIDE OGAWA. "Hepatic Alanine-glyoxylate Aminotransferase Activity and Oxalate Metabolism in Vitamin B6 Deficient Rats." Journal of Urology 169, no. 2 (2003): 683–86. http://dx.doi.org/10.1016/s0022-5347(05)63992-4.

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