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Relevant bibliographies by topics / Glyoxylate metabolism

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Academic literature on the topic 'Glyoxylate metabolism'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Glyoxylate metabolism"

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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Glyoxylate metabolism"

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Giafi, Chrysanthi Foteini. "Characterisation of human D-glycerate dehydrogenase/glyoxylate reductase." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287896.

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Blume, Christian [Verfasser]. "Glycolate and glyoxylate metabolism in higher plants : how natural and artificial pathways contribute to plant metabolism / Christian Blume." Hannover : Technische Informationsbibliothek (TIB), 2013. http://d-nb.info/1130810666/34.

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Crombie, Andrew. "Metabolism of methane and propane and the role of the glyoxylate bypass enzymes in Methylocella silvestris BL2." Thesis, University of Warwick, 2011. http://wrap.warwick.ac.uk/45158/.

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Methylocella silvestris BL2 is a moderately acidophilic facultative methanotroph isolated from forest soil in 2003. Uniquely, it has the ability to grow on a wide range of multi-carbon compounds in addition to methane. An analysis of growth conditions identified the requirements for robust and predictable growth on a wide range of substrates. A simple and effective method of targeted mutagenesis was developed, which relies on electroporation with a linear DNA fragment, and several strains with deletions of key enzymes were constructed using this method. Deletion of isocitrate lyase demonstrate

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Sutherland, Steven Thomas. "Studies on the metabolism of oxalate, glyoxylate, glycolate and glycine by peroxisomes and mitochondria from rat liver /." The Ohio State University, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487693923196163.

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Burdin, Dmitry V., Alexey A. Kolobov, Chad Brocker та ін. "Diabetes-linked transcription factor HNF4α regulates metabolism of endogenous methylarginines and β-aminoisobutyric acid by controlling expression of alanine-glyoxylate aminotransferase 2". Nature Publishing Group, 2016. https://tud.qucosa.de/id/qucosa%3A30404.

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Elevated levels of circulating asymmetric and symmetric dimethylarginines (ADMA and SDMA) predict and potentially contribute to end organ damage in cardiovascular diseases. Alanine-glyoxylate aminotransferase 2 (AGXT2) regulates systemic levels of ADMA and SDMA, and also of beta-aminoisobutyric acid (BAIB)-a modulator of lipid metabolism. We identified a putative binding site for hepatic nuclear factor 4 α (HNF4α) in AGXT2 promoter sequence. In a luciferase reporter assay we found a 75% decrease in activity of Agxt2 core promoter after disruption of the HNF4α binding site. Direct binding of HN

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Burdin, Dmitry V., Alexey A. Kolobov, Chad Brocker та ін. "Diabetes-linked transcription factor HNF4α regulates metabolism of endogenous methylarginines and β-aminoisobutyric acid by controlling expression of alanine-glyoxylate aminotransferase 2". Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-226882.

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Elevated levels of circulating asymmetric and symmetric dimethylarginines (ADMA and SDMA) predict and potentially contribute to end organ damage in cardiovascular diseases. Alanine-glyoxylate aminotransferase 2 (AGXT2) regulates systemic levels of ADMA and SDMA, and also of beta-aminoisobutyric acid (BAIB)-a modulator of lipid metabolism. We identified a putative binding site for hepatic nuclear factor 4 α (HNF4α) in AGXT2 promoter sequence. In a luciferase reporter assay we found a 75% decrease in activity of Agxt2 core promoter after disruption of the HNF4α binding site. Direct binding of HN

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Book chapters on the topic "Glyoxylate metabolism"

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Peña Mattozzi, M., Yisheng Kang, and Jay D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism." In Cellular Ecophysiology of Microbe: Hydrocarbon and Lipid Interactions. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-50542-8_52.

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Peña Mattozzi, M., Yisheng Kang, and Jay D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism." In Cellular Ecophysiology of Microbe. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20796-4_52-1.

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de la Peña Mattozzi, M., Y. Kang, and J. D. Keasling. "Feast: Choking on Acetyl-CoA, the Glyoxylate Shunt, and Acetyl-CoA-Driven Metabolism." In Handbook of Hydrocarbon and Lipid Microbiology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-77587-4_116.

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Thompson, G. N., P. Purkiss, and C. J. Danpure. "The Subcellular Metabolism of Glyoxylate in Primary Hyperoxaluria Type 1: The Relationship Between Glycine Production and Oxalate Overproduction." In Studies in Inherited Metabolic Disease. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1259-5_34.

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Kleczkowski, Leszek A., Douglas D. Randall, and Dale G. Blevins. "Identification and Some Characteristics of Two Nadph-Dependent Reductases Involved in Glyoxylate and Hydroxypyruvate Metabolism in Leaves." In Progress in Photosynthesis Research. Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-017-0516-5_119.

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Danpure, C. J., and P. R. Jennings. "Enzymatic Heterogeneity in Primary Hyperoxaluria Type 1 (Hepatic Peroxisomal Alanine: Glyoxylate Aminotransferase Deficiency)." In Studies in Inherited Metabolic Disease. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1259-5_32.

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Wanders, R. J. A., C. W. T. van Roermund, S. Jurriaans, et al. "Diversity in Residual Alanine Glyoxylate Aminotransferase Activity in Hyperoxaluria Type I: Correlation with Pyridoxine Responsiveness." In Studies in Inherited Metabolic Disease. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1259-5_33.

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Fargue, Sonia, Dawn S. Milliner, and Christopher J. Danpure. "Hereditary disorders of oxalate metabolism: The primary hyperoxalurias." In Oxford Textbook of Medicine, edited by Timothy M. Cox. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0237.

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Primary hyperoxalurias (PHs) are rare inherited disorders characterized by an increased endogenous synthesis of oxalate caused by a deficiency in one of several liver and kidney enzymes involved in glyoxylate metabolism. The excess oxalate is eliminated from the body by the kidneys. High concentrations of oxalate in the urine increase the risk of calcium oxalate deposition in the kidney (resulting in nephrocalcinosis) and in the urinary tract (leading to urinary stones). Primary hyperoxaluria is characterized by recurring calcium oxalate stones, presenting from early childhood to late adult life. Over time, deposition of calcium oxalate crystals in kidney tissue leads to kidney damage with progressive loss of kidney function. Primary hyperoxaluria type 1 is the most severe form with a median age at end-stage renal failure reached during young adulthood. Patients with PH type 2 and PH type 3 may show preservation of kidney function well into adulthood. Systemic deposition of calcium oxalate (oxalosis) can follow kidney failure and increased plasma oxalate levels. Diagnosis is made by DNA analysis of peripheral blood samples, or more rarely by enzyme assay of liver biopsy tissue. Treatment relies on high fluid intake, inhibitors of calcium oxalate crystallization, and, when required, urological procedures for stone removal. Some patients with PH1 respond to vitamin B<sub>6</sub> treatment. Management of end-stage renal failure is difficult as dialysis, whether haemo- or peritoneal, cannot match oxalate production. Isolated kidney transplantation places patients at risk of recurring oxalate deposition in the graft in PH1 patients not responsive to vitamin B<sub>6</sub>. Liver transplantation, usually combined with kidney transplantation, is a curative treatment for PH1 but carries significant risks.

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