Academic literature on the topic 'Ubiquinone biosynthesis'
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Journal articles on the topic "Ubiquinone biosynthesis":
Lee, Pyung Cheon, Christine Salomon, Benjamin Mijts, and Claudia Schmidt-Dannert. "Biosynthesis of Ubiquinone Compounds with Conjugated Prenyl Side Chains." Applied and Environmental Microbiology 74, no. 22 (September 26, 2008): 6908–17. http://dx.doi.org/10.1128/aem.01495-08.
Wilton, D. C. "The effect of excess mevalonic acid on ubiquinone and tetrahymanol biosynthesis in Tetrahymena pyriformis." Biochemical Journal 229, no. 2 (July 15, 1985): 551–53. http://dx.doi.org/10.1042/bj2290551.
Szkopińska, A. "Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization." Acta Biochimica Polonica 47, no. 2 (June 30, 2000): 469–80. http://dx.doi.org/10.18388/abp.2000_4027.
Meganathan, R. "Ubiquinone biosynthesis in microorganisms." FEMS Microbiology Letters 203, no. 2 (September 2001): 131–39. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10831.x.
Rötig, Agnès. "News in Ubiquinone Biosynthesis." Chemistry & Biology 17, no. 5 (May 2010): 415–16. http://dx.doi.org/10.1016/j.chembiol.2010.05.001.
Kaneshiro, Edna S., Donggeun Sul, and Banasri Hazra. "Effects of Atovaquone and Diospyrin-Based Drugs on Ubiquinone Biosynthesis in Pneumocystis carinii Organisms." Antimicrobial Agents and Chemotherapy 44, no. 1 (January 1, 2000): 14–18. http://dx.doi.org/10.1128/aac.44.1.14-18.2000.
Bekker, Martijn, Svetlana Alexeeva, Wouter Laan, Gary Sawers, Joost Teixeira de Mattos, and Klaas Hellingwerf. "The ArcBA Two-Component System of Escherichia coli Is Regulated by the Redox State of both the Ubiquinone and the Menaquinone Pool." Journal of Bacteriology 192, no. 3 (November 20, 2009): 746–54. http://dx.doi.org/10.1128/jb.01156-09.
Wang, Ying, and Siegfried Hekimi. "Mitochondrial respiration without ubiquinone biosynthesis." Human Molecular Genetics 22, no. 23 (July 11, 2013): 4768–83. http://dx.doi.org/10.1093/hmg/ddt330.
Soubeyrand, Eric, Megan Kelly, Shea A. Keene, Ann C. Bernert, Scott Latimer, Timothy S. Johnson, Christian Elowsky, Thomas A. Colquhoun, Anna K. Block, and Gilles J. Basset. "Arabidopsis 4-COUMAROYL-COA LIGASE 8 contributes to the biosynthesis of the benzenoid ring of coenzyme Q in peroxisomes." Biochemical Journal 476, no. 22 (November 27, 2019): 3521–32. http://dx.doi.org/10.1042/bcj20190688.
Kalén, A., E. L. Appelkvist, G. Dallner, Bertil Andersson, and Hans-Erik Åkerlund. "Biosynthesis of Ubiquinone in Rat Liver." Acta Chemica Scandinavica 41b (1987): 70–72. http://dx.doi.org/10.3891/acta.chem.scand.41b-0070.
Dissertations / Theses on the topic "Ubiquinone biosynthesis":
Storey, Benjamin 1973. "AQX : a novel gene in plant ubiquinone biosynthesis." Thesis, McGill University, 2002. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=80882.
Ismail, Alexandre. "Molecular modeling of Coq6, a ubiquinone biosynthesis flavin-dependent hydroxylase. Evidence of a substrate access channel." Electronic Thesis or Diss., Paris 6, 2016. http://www.theses.fr/2016PA066044.
Coq6 is an enzyme involved in the biosynthesis of coenzyme Q, a polyisoprenylated benzoquinone lipid essential to the function of the mitochondrial respiratory chain. In the yeast Saccharomyces cerevisiae, this putative flavin-dependent monooxygenase is proposed to hydroxylate the benzene ring of coenzyme Q (ubiquinone) precursor at position C5. We show here through biochemical studies that Coq6 is a flavoprotein using FAD as a cofactor. Homology models of the Coq6-FAD complex are constructed and studied through molecular dynamics and substrate docking calculations of 3-hexaprenyl-4-hydroxyphenol (4-HP6), a bulky hydrophobic model substrate. We identify a putative access channel for Coq6 in a wild type model and propose in silico mutations positioned at its entrance capable of partially (G248R and L382E single mutations) or completely (a G248R-L382E double-mutation) blocking access of the substrate to thechannel . Further in vivo assays support the computational predictions, thus explaining the decreased activities or inactivation of the mutated enzymes. This work provides the first detailed structural information of an important and highly conserved enzyme of ubiquinone biosynthesis
Nordman, Tomas. "In vitro studies on the biosynthesis and reduction of ubiquinone /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-475-5/.
Wang, Ying. "Mitochondrial function in cells, tissues and animals without ubiquinone biosynthesis." Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=122994.
L'ubiquinone (coenzyme Q, UQ, CoQ) est essentielle pour toutes les formes de vie qui s'appuient sur la respiration mitochondriale pour la production d'énergie. Elle fonctionne comme un transporteur d'électrons dans la chaîne respiratoire mitochondriale (ETC) et joue un rôle dans de nombreuses autres fonctions cellulaires. Au cours de la dernière décennie, un nombre croissant de patients ont été décrits comme ayant un défaut génétique produisant un problème de synthèse de l'UQ et présentant des manifestations cliniques graves et diversifiées. Ma thèse s'est concentrée sur une enzyme particulière de la synthèse de l'UQ chez la souris, codée par le gène Mclk1/Coq7 et responsable de l'hydroxylation du DMQ (demethoxy-UQ). Ici je décris 3 modèles de knockout (KO) conditionnels que j'ai créés qui permettent de contourner la létalité embryonnaire de Mclk1. Ces modèles nous permettent d'examiner les conséquences de la perte complète de la fonction de Mclk1 in vitro et in vivo chez les animaux adultes. Premièrement, j'ai créé des lignées de fibroblastes embryonnaires (MEFs) de souris KO pour Mclk1. Ces cellules ne synthétisent pas d'UQ et accumulent le DMQ. Elles sont viables dans les conditions standards de culture et en présence de glucose. De plus, malgré le manque d'UQ, elles ont encore une ETC fonctionnelle. Pour comprendre ce phénomène, j'ai généré des MEFs KO pour Pdss2 qui sont dépourvus de DMQ et d'UQ. À notre surprise, ces cellules sont également capables de respiration mitochondriale. Ces observations suggèrent que 1) le phénotype respiratoire des mutants Mclk1 peut être considéré essentiellement comme un phénotype dû à un manque d'UQ, et 2) la respiration mitochondriale peut se produire en l'absence d'UQ. Les MEFs KO pour Mclk1 ne peuvent survivre dans un milieu qui les forcerait à dépendre de la respiration mitochondriale pour la production d'ATP. Ces caractéristiques font de ces cellules un outil unique pour tester l'efficacité des analogues de l'UQ dans la ETC de mammifères. J'ai aussi créé un modèle de souris produisant une ablation hépatique de Mclk1. Il est intéressant de noter qu'une perte sévère d'UQ dans les hépatocytes ne cause qu'une diminution légère de l'activité de la ETC et que les souris ne présentent aucune anomalie flagrante. Par conséquent, la fonction mitochondriale du foie semble être capable de tolérer de graves carences en UQ. En utilisant ce modèle, nous avons aussi démontré que de l'UQ10 exogène peut être utilisé par le foie et rétablir la fonction de la ETC. J'ai aussi construit un modèle pour lequel Mclk1 est absent chez les souris adultes. Ces animaux ont une survie moyenne de 9 mois après la perte totale de Mclk1. Une très lente diminution du contenu en UQ des tissus après l'ablation de Mclk1 a été observée, ce qui pourrait expliquer la détérioration très lente de ces souris. J'ai trouvé que dans le cœur, les reins et les muscles squelettiques de profonds déficits en UQ compromettent gravement la respiration mitochondriale. Contrairement au foie il semblerait que ces tissus nécessitent de hauts niveaux d'UQ afin de maintenir une fonction respiratoire suffisante. J'ai trouvé que l'UQ10 exogène ne peut être utilisé que par le foie et que, même dans ce cas, il était presque totalement incapable d'aider les souris déficientes en Mclk1. Par contre, le traitement des animaux mutants avec l'acide 2,4 -dihydroxybenzoïque (2,4-diHB; un analogue synthétique de l'acide 4-hydroxybenzoïque (4-HB), qui est le précurseur naturel dans la biosynthèse de l'UQ) mène à une nette amélioration des symptômes de maladie des souris mutantes incluant la létalité précoce. Le 2,4 -diHB diffère structurellement du 4-HB par un groupe hydroxyle à la position où l'enzyme MCLK1 catalyse l'hydroxylation du DMQ. Ces données suggèrent que les symptômes de certaines déficiences en UQ pourraient être allégés par le traitement à l'aide de précurseurs non-naturels qui permettraient de contourner les voies de biosynthèses défectueuses.
Ismail, Alexandre. "Molecular modeling of Coq6, a ubiquinone biosynthesis flavin-dependent hydroxylase. Evidence of a substrate access channel." Thesis, Paris 6, 2016. http://www.theses.fr/2016PA066044/document.
Coq6 is an enzyme involved in the biosynthesis of coenzyme Q, a polyisoprenylated benzoquinone lipid essential to the function of the mitochondrial respiratory chain. In the yeast Saccharomyces cerevisiae, this putative flavin-dependent monooxygenase is proposed to hydroxylate the benzene ring of coenzyme Q (ubiquinone) precursor at position C5. We show here through biochemical studies that Coq6 is a flavoprotein using FAD as a cofactor. Homology models of the Coq6-FAD complex are constructed and studied through molecular dynamics and substrate docking calculations of 3-hexaprenyl-4-hydroxyphenol (4-HP6), a bulky hydrophobic model substrate. We identify a putative access channel for Coq6 in a wild type model and propose in silico mutations positioned at its entrance capable of partially (G248R and L382E single mutations) or completely (a G248R-L382E double-mutation) blocking access of the substrate to thechannel . Further in vivo assays support the computational predictions, thus explaining the decreased activities or inactivation of the mutated enzymes. This work provides the first detailed structural information of an important and highly conserved enzyme of ubiquinone biosynthesis
Soballe, Britta. "Ubiquinone in the facultatively anaerobic bacterium Escherichia coli : function in respiration and regulation of biosynthesis." Thesis, King's College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267980.
Launay, Romain. "Computational characterization and understanding of protein assemblies : the case of the Escherichia coli Ubi metabolon involved in ubiquinone biosynthesis." Electronic Thesis or Diss., Toulouse, INSA, 2023. http://www.theses.fr/2023ISAT0055.
Protein-protein interactions (PPIs) and supramolecular assemblies are essential for the functions of living cells. They play an important role in various biological functions, such as signal transduction, cell-cell communication, transcription, replication and membrane transport. Determining and characterizing such interfaces remains a challenge in structural biology. However, advances in the development of computational methods and the power of the computing resources available today have led to a considerable improvement in the accuracy of in silico predictions of three-dimensional models of protein assemblies.In this thesis, the aim was to predict the structure of a supramolecular assembly, called the Ubi metabolon, involved in the ubiquinone (UQ8) biosynthesis pathway in Escherichia coli. Ubiquinone is a prenol with oxido-reducing properties, localized in membranes, and highly conserved throughout evolution but also in different cells of organisms. It is composed of two main parts, an aromatic group with oxido-reducing properties, known as quinone or polar head, and a polyisoprenoid tail which is hydrophobic in nature. In this study, we are interested in the final stages of the biosynthetic pathway, in particular the modifications (methylations and hydroxylations) of the polar head. These reactions take place within the Ubi metabolon. The latter is made up of seven different proteins (UbiE, UbiG, UbiF, UbiH, UbiI, UbiJ, UbiK) catalysing six consecutive enzymatic reactions.In this work, we sought to predict the structure of the metabolon and were thus able to propose a protein subset that we called the 'core subunit'. This sub-unit includes all the partners and could be biologically functional. In parallel, a study was carried out on the UbiJ-UbiK2 heterotrimer, an essential molecular brick of the Ubi metabolon. A three-dimensional model of UbiJ-UbiK2 was proposed. Using a multi-scale modelling study, it was shown that it could be involved in the release of ubiquinone from membranes. Finally, the last part of this work focused on studying the behavior of a particular family of enzymes, the class A flavin mono-oxygenases, to which UbiF, UbiH and UbiI belong. A comparative study between a representative enzyme from this family, called PHBH, and UbiI was carried out, concluding that interactions with partners were necessary to stabilize these proteins within the Ubi metabolon.Taken together, this work and the proposed hypotheses provide a new insight into the supramolecular organization of the Ubi metabolon, both structurally and functionally. Our results open up new prospects for their experimental study
Vo, Chau Duy Tam. "Etude biochimique de trois nouvelles protéines impliquées dans la biosynthèse de l’ubiquinone en anaérobie chez Escherichia coli : UbiT, UbiU et UbiV A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone Ubiquinone Biosynthesis over the Entire O 2 Range: Characterization of a Conserved O 2-Independent Pathway." Thesis, Sorbonne université, 2019. https://accesdistant.sorbonne-universite.fr/login?url=http://theses-intra.upmc.fr/modules/resources/download/theses/2019SORUS401.pdf.
Ubiquinone (UQ) is a polyprenylated lipid that plays an important role in electron transport in the respiratory chains of E. coli. The aerobic biosynthesis of UQ in E. coli requires eight reactions and involves at least twelve proteins (UbiA-UbiK and UbiX). In this work, we demonstrate that seven Ubi proteins form the Ubi complex, a stable metabolon that catalyzes the last six reactions of the UQ biosynthetic pathway. The X-Ray structure of the SCP2 domain of UbiJ forms an extended hydrophobic cavity that could bind UQ intermediates inside the 1-MDa Ubi complex. The Ubi complex is purified from cytoplasmic extracts and UQ biosynthesis occurs in this fraction, challenging the current thinking of a membrane-associated biosynthetic process. UQ is reported to be biosynthesized under both anerobic and anaerobic conditions. We characterize a novel, O2-independent pathway for the biosynthesis of UQ. This pathway relies on three proteins, UbiT, UbiU, and UbiV. UbiT contains an SCP2 lipid-binding domain and is likely an accessory factor of the biosynthetic pathway, while UbiU and UbiV (UbiU-UbiV) are involved in hydroxylation reactions and represent a novel class of O2-independent hydroxylases. We demonstrate that UbiU-UbiV from E.coli form a heterodimer, wherein each protein binds a [4Fe-4S] cluster via conserved cysteines that are essential for activity. Moreover, we show that purified UbiU from P. aeruginosa is able to bind UQ, suggesting a different role of UbiU and UbiV. UbiU and UbiV belong to peptidase U32 family whose function remains questionable. By bioinformatic analyses, we demonstrated that U32 proteins were characterized by four conserved cysteines important for their enzymatic activities and by biochemical tools, we confirmed that RlhA and TrhP, two others U32 subfamilies, like UbiU and UbiV, are all Fe-S proteins
Hajj, Chehade Mahmoud. "Élucidation du rôle de nouveaux acteurs de la biosynthèse de Q8 chez Escherichia coli et caractérisation du complexe protéique de biosynthèse de Q8." Thesis, Université Grenoble Alpes (ComUE), 2015. http://www.theses.fr/2015GREAV010/document.
Ubiquinone (Q) is a lipophilic compound that plays an important role in electron and proton transport in the respiratory chains of Escherichia coli. Besides this important role in energy production, Q also functions as a membrane soluble antioxidant. The biosynthesis of Q8 requires eight reactions and involves at least nine proteins (UbiA-UbiH and UbiX) in Escherichia coli. Three of these reactions are hydroxylations resulting in the introduction of a hydroxyl group on carbon atoms at position 1, 5 and 6 of the aromatic ring. The C1 and C6 hydroxylation are well characterized whereas the C5 hydroxylation has been proposed to involve UbiB, a protein kinase without any sequence homology with monooxygenase. In this work, by genetic and biochemical methods we provide evidence that VisC which we renamed UbiI, displays sequence homology with monooxygenases and catalyzes the C5 hydroxylation, not UbiB. We have identified two new genes, yqiC and yigP (renammed UbiJ and UbiK) which are required only for Q8 biosynthesis in aerobic conditions. The exact role of the corresponding proteins, renamed UbiJ and UbiK, remains unknown. These proteins are able to interact with other Ubi proteins to be able to produce Q supporting the protein complex hypothesis. Our progress on the characterization of an Ubi-complex regrouping several Ubi proteins suggest that UbiJ and UbiK may fulfill functions related to the Ubi-complex stability. Mutants affected in hydroxylation steps are deficient for Q8 in aerobic conditions but recover a wild type Q8 content when grown in anaerobic conditions. This intriguing observation supports the existence of an alternative hydroxylation system independent from dioxygen which has not been characterized so far. By phylogenetic studies, we have identified a new gene in which the deletion affect the biosynthesis of Q only in anaerobic conditions suggesting a reorganization of Q biosynthesis in these two conditions. Our results has improved our knowledge of the prokaryotic Q biosynthetic pathway through the discovery of new genes involved in this process and through the identification of the molecular function of some proteins
Book chapters on the topic "Ubiquinone biosynthesis":
Löffler, Monika, Johannes Jöckel, Gertrud Schuster, and Cornelia Becker. "Dihydroorotat-ubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides." In Detection of Mitochondrial Diseases, 125–29. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-6111-8_19.
Rudney, Harry, and Takashi Sugimura. "Studies on the Biosynthesis of the Ubiquinone (Coenzyme Q) Series in Animals and Micro-Organisms." In Novartis Foundation Symposia, 211–32. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470719213.ch10.
Wiss, U. Gloor, and F. Weber. "Biosynthesis of Ubiquinones." In Novartis Foundation Symposia, 264–83. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470719213.ch13.
Cohen, G. N. "Biosynthesis of Carotene, Vitamin A, Sterols, Ubiquinones and Menaquinones." In Microbial Biochemistry, 471–85. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9437-7_36.
Cohen, G. N. "Biosynthesis of Carotene, Vitamin A, Sterols, Ubiquinones and Menaquinones." In Microbial Biochemistry, 523–38. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8908-0_36.
Cohen, Georges N. "Biosynthesis of Carotene, Vitamin A, Sterols, Ubiquinones and Menaquinones." In Microbial Biochemistry, 663–83. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7579-3_36.
Cohen, Georges N. "Biosynthesis of carotene, vitamin A, sterols, ubiquinones and menaquinones." In Microbial Biochemistry, 271–77. Dordrecht: Springer Netherlands, 2004. http://dx.doi.org/10.1007/978-1-4020-2237-1_33.
Meganathan, R. "Menaquinone/Ubiquinone Biosynthesis and Enzymology." In Comprehensive Natural Products II, 411–44. Elsevier, 2010. http://dx.doi.org/10.1016/b978-008045382-8.00142-8.
Lütke-Brinkhaus, Friedhelm, and Hans Kleinig. "[45] Ubiquinone biosynthesis in plant mitochondria." In Methods in Enzymology, 486–90. Elsevier, 1987. http://dx.doi.org/10.1016/0076-6879(87)48047-6.
Niitsu, Akemi L., Elesandro Bornhofen, and Tábata Bergonci. "Biosynthesis of Terpenoids By Plants." In Terpenoids: Recent Advances in Extraction, Biochemistry and Biotechnology, 1–16. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9781681089645122010003.