DOCSLIB.ORG

Endfassung Doktorarbeit 4.10.3.Druck.DOC

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Endfassung Doktorarbeit 4.10.3.Druck.DOC Molekulare und strukturelle Charakterisierung der Flavonolsynthase aus Citrus unshiu Dissertation zur Erlangung des Doktorgrades der Naturwissenschaften (Dr. rer. nat.) dem Fachbereich Pharmazie der Philipps-Universität Marburg vorgelegt von Frank Wellmann aus Freiburg im Breisgau Marburg/ Lahn 2002 Vom Fachbereich Pharmazie der Philipps-Universität Marburg als Dissertation am 17.12.2002 angenommen. Erstgutachter: Herr Professor Dr. Ulrich Matern Zweitgutachter: Herr Professor Dr. Alfred Batschauer Tag der mündlichen Prüfung: 18.12.2002 Wesentliche Auszüge dieser Arbeit wurden veröffentlicht in: Publikationen [1] Wellmann F., Lukacin R., Moriguchi T., Britsch L., Schiltz E. & Matern U. (2002); Functional expression and mutational analysis of flavonol synthase from Citrus unshiu. Eur. J. Biochem. 269, 1-9 [2] Lukacin R., Wellmann F., Britsch L., Martens S. & Matern U. (2002); Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase. Phytochemistry, im Druck [3] Martens S., Forkmann G., Britsch L., Wellmann F., Matern U. & Lukacin R. (2002); Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. PNAS, submitted Poster [1] Wellmann F., Lukacin R. & Matern U. Functional characterization of flavonol synthase from Citrus unshiu; Deutsche Botanische Gesellschaft, Botanikertagung Freiburg i. Br. 2002 Inhaltsverzeichnis I Inhaltsverzeichnis Inhaltsverzeichnis __________________________________________________________ I Abkürzungsverzeichnis_____________________________________________________ V A Einleitung ___________________________________________________________1 A 1 Struktur und physiologische Bedeutung von Flavonoiden ___________________1 A 1.1 Einfluss der Flavonoide auf die Blütenfarben______________________________1 A 1.2 Lichtabhängige Flavonoidbildung_______________________________________2 A 1.3 Flavonoide als Wachstumsregulatoren ___________________________________4 A 1.4 Rolle der Flavonoide in der Phytopathogenabwehr _________________________4 A 1.5 Bedeutung von Flavonoiden bei Pflanze - Tier Interaktionen__________________4 A 2 Humantherapeutische Bedeutung von Flavonoiden ________________________5 A 2.1 Resorption und Metabolismus von Flavonoiden____________________________5 A 2.2 Antioxidative Eigenschaften von Flavonoiden_____________________________6 A 2.3 Tumor-protektive Wirkung von Flavonoiden______________________________7 A 2.4 Immunmodulatorische Wirkung von Flavonoiden __________________________8 A 2.5 Antivirale Wirkung von Flavonoiden ____________________________________9 A 2.6 Toxizität von Flavonoiden____________________________________________10 A 3 Flavonoidbiosynthese ________________________________________________11 A 3.1 Ort der Biosynthese _________________________________________________11 A 3.2 Biosyntheseweg____________________________________________________11 A 4 Klassifikation von Oxygenasen ________________________________________16 A 4.1 Allgemeine Unterscheidung von Monooxygenasen und Dioxygenasen_________16 A 4.2 Pharmazeutische Relevanz 2-Oxoglutarat-abhängiger Dioxygenasen und verwandter Nicht-Häm-Fe (II) Enzyme _________________________________19 A 4.3 Funktionelle und mechanistische Aspekte von 2-Oxoglutarat-abhängigen Dioxygenasen und verwandten Nicht-Häm-Fe (II) Enzymen_________________19 A 4.3.1 Penicillin- und Cephalosporin-Biosynthese____________________________19 A 4.3.2 Clavulansäure-Biosynthese ________________________________________20 A 4.3.3 Hydroxylierung von Prolinen und Prolylresten_________________________21 A 4.3.4 Ethylenbiosynthese_______________________________________________22 A 4.4 Flavonolsynthase ___________________________________________________22 A 4.5 Mechanismus von 2-Oxoglutarat-abhängigen Dioxygenasen_________________23 Inhaltsverzeichnis II A 5 Aufgabenstellung ____________________________________________________26 B Material ____________________________________________________________28 B 1 Chemikalien und Verbrauchsmaterialien________________________________28 B 2 Enzyme ____________________________________________________________29 B 3 Antiseren und Proteine _______________________________________________29 B 4 Membranen ________________________________________________________29 B 5 Dünnschichtplatten und Laufmittel_____________________________________29 B 6 Geräte _____________________________________________________________30 B 7 Stämme von E. coli __________________________________________________30 B 8 Vektoren___________________________________________________________30 B 9 Puffer und Lösungen_________________________________________________31 B 10 Medien ____________________________________________________________33 C Methoden___________________________________________________________34 C 1 Allgemeine proteinbiochemische Methoden______________________________34 C 2 Allgemeine molekularbiologische Methoden _____________________________36 C 3 In vitro-Mutagenese mit Oligonukleotiden _______________________________37 C 4 Expression der FLS in E. coli__________________________________________39 C 5 Zellaufschluss_______________________________________________________41 C 6 Reinigung der heterolog exprimierten FLS ______________________________41 C 7 Aminoterminale Sequenzierung ________________________________________42 C 8 Test auf Flavonolsynthase-Aktivität ____________________________________43 C 9 Präparative Gewinnung von Quercetin__________________________________44 C 10 Massenspektroskopie ________________________________________________45 C 11 CD-Spektroskopie ___________________________________________________45 C 12 FLS-Antiserum _____________________________________________________45 Inhaltsverzeichnis III D Ergebnisse und Diskussion __________________________________________46 D 1 FLS-Klonierung _____________________________________________________46 D 2 Heterologe Expression der FLS ________________________________________46 D 3 Test auf FLS-Aktivität _______________________________________________48 D 4 Reinigung der rekombinanten FLS _____________________________________49 D 4.1 Ammoniumsulfatfällung _____________________________________________49 D 4.2 Größenausschlusschromatographie an Fractogel EMD Bio SEC ______________49 D 4.3 Anionenaustauschchromatographie an Fractogel EMD DEAE _______________51 D 4.4 Reinigungstabelle __________________________________________________52 D 5 Biochemische Charakterisierung der rekombinanten FLS__________________54 D 5.1 Polypeptidanalyse __________________________________________________54 D 5.2 Präparativer Enzymtest ______________________________________________54 D 5.3 HPLC-Analyse ____________________________________________________55 D 5.4 Zeit- und Proteinlinearität ____________________________________________57 D 5.5 pH-Optimum ______________________________________________________58 D 5.6 Temperaturoptimum ________________________________________________60 D 5.7 Kinetische Konstanten für 2-Oxoglutarat und Fe2+_________________________60 D 5.8 Bestimmung der apparenten Michaelis Konstante für DHQ und DHK _________62 D 6 Datenbankanalyse der FLS ___________________________________________64 D 6.1 Ermittlung einer FLS-Konsensussequenz ________________________________64 D 6.2 Aminosäuresequenzanalysen__________________________________________66 D 7 In vitro-Mutagenesestudien____________________________________________67 D 7.1 Expression der FLS-Mutanten_________________________________________69 D 7.2 Reinigung der FLS-Mutanten _________________________________________70 D 7.3 Bestimmung der spezifischen Aktivitäten der FLS-Mutanten ________________71 D 8 Strukturelle Charakterisierung der FLS ________________________________72 D 8.1 CD-Spektrum der FLS_______________________________________________72 D 8.2 Serologische Verwandschaften der FLS _________________________________74 D 9 Strukturvorhersage der FLS __________________________________________75 D 10 Charakterisierung des aktiven Zentrums des FLS-Proteinmodells ___________83 Inhaltsverzeichnis IV D 11 Funktionelle Charakterisierung der FLS ________________________________85 D 11.1 Überprüfung der FLS auf ANS-Aktivität ________________________________85 D 11.2 Überprüfung der FLS auf FHT-Aktivität ________________________________86 D 11.3 Stereospezifität der FLS für Flavanon-Substrate __________________________88 E Schlussbetrachtung _________________________________________________93 E 1 Klonierung und Expression der FLS ____________________________________93 E 2 Reinigung der rekombinanten FLS _____________________________________94 E 3 Biochemische Charakterisierung _______________________________________95 E 4 Datenbankanalyse und Strukturvorhersage der FLS ______________________97 E 5 In vitro-Mutagenese__________________________________________________98 E 6 Strukturelle Untersuchungen der FLS _________________________________104 E 7 Substratspezifität der FLS ___________________________________________105 F Zusammenfassung _________________________________________________111 G Literaturverzeichnis _______________________________________________113 Abkürzungsverzeichnis V Abkürzungsverzeichnis A Absorption amp Ampicillin ANS Anthocyanidinsynthase ACV d-(L-a-aminoadipyl)-L-cysteinyl-D-valin ATP Adenosin-5'-triphosphat BCIP 5-Bromo-4-chloro-3-indolylphosphat bp Basenpaare Bq Bequerel BSA Rinderserumalbumin cDNA komplementäre DNA Da Dalton DAOCS Deacetoxycephalosporin C-Synthase DEAE Diethylaminoethyl DMSO Dimethylsulfoxid DNA Desoxyribonukleinsäure ds doppelsträngig (double-stranded)
Load more

Recommended publications
  • Transcriptome Analysis of Differential Gene Expression in Dichomitus Squalens
    bioRxiv preprint doi: https://doi.org/10.1101/359646; this version posted June 30, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Transcriptome analysis of differential gene expression in Dichomitus squalens 2 during interspecific mycelial interactions and the potential link with laccase 3 induction 4 Zixuan Zhong1, Nannan Li1, Binghui He, Yasuo Igarashi, Feng Luo* 5 6 Research Center of Bioenergy and Bioremediation, College of Resources and Environment, 7 Southwest University, Beibei, Chongqing 400715, People’s Republic of China 8 9 *corresponding author: Feng Luo (FL) [email protected] 10 11 1These authors contributed equally to the paper 12 13 ABSTRACT 14 Interspecific mycelial interactions between white rot fungi are always accompanied by increased 15 production of laccase. In this study, the potential of white rot fungi Dichomitus squalens for 16 enhancing laccase production during interaction with two other white rot fungi Trametes 17 versicolor or Pleurotus ostreatus was identified. To probe the mechanism of laccase induction and 18 the role of laccase played during the combative interaction, we analyzed the laccase induction 19 response to stressful conditions during fungal interaction related to the differential gene expression 20 profile. We further confirmed the expression patterns of 16 selected genes by qRT-PCR analysis. 21 We noted that many differential expression genes (DEGs) encoding proteins were involved in 22 xenobiotics detoxification and ROS generation or reduction, including aldo/keto reductase, 23 glutathione S-transferases, cytochrome P450 enzymes, alcohol oxidases and dehydrogenase, 24 manganese peroxidase and laccase.
    [Show full text]
  • Relating Metatranscriptomic Profiles to the Micropollutant
    1 Relating Metatranscriptomic Profiles to the 2 Micropollutant Biotransformation Potential of 3 Complex Microbial Communities 4 5 Supporting Information 6 7 Stefan Achermann,1,2 Cresten B. Mansfeldt,1 Marcel Müller,1,3 David R. Johnson,1 Kathrin 8 Fenner*,1,2,4 9 1Eawag, Swiss Federal Institute of Aquatic Science and Technology, 8600 Dübendorf, 10 Switzerland. 2Institute of Biogeochemistry and Pollutant Dynamics, ETH Zürich, 8092 11 Zürich, Switzerland. 3Institute of Atmospheric and Climate Science, ETH Zürich, 8092 12 Zürich, Switzerland. 4Department of Chemistry, University of Zürich, 8057 Zürich, 13 Switzerland. 14 *Corresponding author (email: [email protected] ) 15 S.A and C.B.M contributed equally to this work. 16 17 18 19 20 21 This supporting information (SI) is organized in 4 sections (S1-S4) with a total of 10 pages and 22 comprises 7 figures (Figure S1-S7) and 4 tables (Table S1-S4). 23 24 25 S1 26 S1 Data normalization 27 28 29 30 Figure S1. Relative fractions of gene transcripts originating from eukaryotes and bacteria. 31 32 33 Table S1. Relative standard deviation (RSD) for commonly used reference genes across all 34 samples (n=12). EC number mean fraction bacteria (%) RSD (%) RSD bacteria (%) RSD eukaryotes (%) 2.7.7.6 (RNAP) 80 16 6 nda 5.99.1.2 (DNA topoisomerase) 90 11 9 nda 5.99.1.3 (DNA gyrase) 92 16 10 nda 1.2.1.12 (GAPDH) 37 39 6 32 35 and indicates not determined. 36 37 38 39 S2 40 S2 Nitrile hydration 41 42 43 44 Figure S2: Pearson correlation coefficients r for rate constants of bromoxynil and acetamiprid with 45 gene transcripts of ECs describing nucleophilic reactions of water with nitriles.
    [Show full text]
  • Exploring the Role of Glutamate Signaling in the Regulation of The
    Exploring the Role of Glutamate Signaling in the Regulation of the Aiptasia-Symbiodiniaceae Symbiosis Thesis by Migle Kotryna Konciute In Partial Fulfillment of the Requirements For the Degree of Master of Science King Abdullah University of Science and Technology, Thuwal, Kingdom of Saudi Arabia April, 2020 Migle Kotryna Konciute 2 EXAMINATION COMMITTEE PAGE The thesis of student Migle Kotryna Konciute is approved by the examination committee. Committee chairperson: Assoc. Prof. Manuel Aranda Committee Members: Asst. Prof. Kyle J. Lauersen, Assoc. Prof. Xose Anxelu G. Moran 3 COPYRIGHT PAGE ©April, 2020 Migle Kotryna Konciute All Rights Reserved 4 5 ABSTRACT Exploring the Role of Glutamate Signaling in the Regulation of the Aiptasia- Symbiodiniaceae Symbiosis Migle Kotryna Konciute The symbiotic relationship between cnidarians and their photosynthetic dinoflagellate symbionts underpins the success of coral reef communities in oligotrophic, tropical seas. Despite several decades of study, the cellular and molecular mechanisms that regulate the symbiotic relationship between the dinoflagellate algae and the coral hosts are still not clear. One of the hypotheses on the metabolic interactions between the host and the symbiont suggests that ammonium assimilation by the host can be the underlying mechanism of this endosymbiosis regulation. An essential intermediate of the ammonium assimilation pathway is glutamate, which is also known for its glutamatergic signaling function. Interestingly, recent transcriptomic level and DNA methylation studies on sea anemone Aiptasia showed differences in metabotropic glutamate signaling components when comparing symbiotic and non-symbiotic animals. The changes in this process on transcriptional and epigenetic levels indicate the importance of glutamate signaling in regard to cnidarian symbiosis.
    [Show full text]
  • Oxidative Demethylation of DNA Damage by Escherichia Coli Alkb
    Oxidative déméthylation of DNA damage by Escherichia coli AlkB and its human homologs ABH2 and ABH3 A thesis submitted for the degree of Ph D. by Sarah Catherine Trewick Clare Hall Laboratories Cancer Research UK London Research Institute South Mimms, Potters Bar Hertfordshire, EN6 3LD and Department of Biochemistry University College London Gower Street, London, WCIE 6BT ProQuest Number: U642489 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. uest. ProQuest U642489 Published by ProQuest LLC(2015). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States Code. Microform Edition © ProQuest LLC. ProQuest LLC 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106-1346 ABSTRACT The E. coli AlkB protein was implicated in the repair or tolerance of DNA méthylation damage. However, despite the early isolation of an E. coli alkB mutant, the function of the AlkB protein had not been resolved (Kataoka et al, 1983). The E. coli alkB mutant is defective in processing methylated single stranded DNA, therefore, it was suggested that the AlkB protein either repairs or tolerates lesions generated in single stranded DNA, such as 1-methyladenine (1-meA) or 3-methylcytosine (3-meC), or that AlkB only acts on single stranded DNA (Dinglay et al, 2000).
    [Show full text]
  • Catalytic Triad' in Directing Promiscuous Substrate-Specificity
    Spectroscopic and mechanistic investigation of the enzyme mercaptopropionic acid dioxygenase (MDO), the role of the conserved outer-sphere 'catalytic triad' in directing promiscuous substrate-specificity A DISSERTATION Presented to the faculty of the Graduate School of The University of Texas at Arlington in Partial fulfillment Of the requirements of the Degree of Doctor in Philosophy in CHEMISTRY by SINJINEE SARDAR Under the guidance of Dr. Brad S. Pierce 2nd May, 2018 ACKNOWLEDGEMENT It gives me immense pleasure to thank my compassionate guide Dr. Brad S. Pierce, for his exemplary guidance to accomplish this work. It has been an extraordinary pleasure and privilege to work under his guidance for the past few years. I express my sincere gratitude to my doctoral committee members Prof. Frederick. MacDonnell, Dr. Rasika Dias, and Dr. Jongyun Heo for their valuable advice and constant help. I would also like to thank the Department of Chemistry and Biochemistry of UTA for bestowing me the opportunity to have access to all the departmental facilities required for my work. Here, I express my heartiest gratitude to the ardent and humane guidance of my senior lab mates Dr. Josh Crowell and Dr. Bishnu Subedi which was indispensable. I am immeasurably thankful to my lab mates Wei, Mike, Phil, Nick, Jared and Sydney for their constant support and help. It has been a pleasure to working with all of you. The jokes and laughter we shared have reduced the hardships and stress of graduate school and had made the stressful journey fun. To end with, I utter my heartfelt gratefulness to my parents and my sister for their lifelong support and encouragement which helped me chase my dreams and aspirations and sincere appreciation towards my friends who are my extended family for their lively and spirited encouragement.
    [Show full text]
  • Inhibition and Cofactor Targeting of Hypoxia-Sensing Proteins
    University of Massachusetts Amherst ScholarWorks@UMass Amherst Doctoral Dissertations Dissertations and Theses August 2015 Inhibition and Cofactor Targeting of Hypoxia-Sensing Proteins Cornelius Y. Taabazuing University of Massachusetts Amherst Follow this and additional works at: https://scholarworks.umass.edu/dissertations_2 Part of the Biochemistry Commons, Inorganic Chemistry Commons, and the Structural Biology Commons Recommended Citation Taabazuing, Cornelius Y., "Inhibition and Cofactor Targeting of Hypoxia-Sensing Proteins" (2015). Doctoral Dissertations. 409. https://doi.org/10.7275/6956835.0 https://scholarworks.umass.edu/dissertations_2/409 This Open Access Dissertation is brought to you for free and open access by the Dissertations and Theses at ScholarWorks@UMass Amherst. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of ScholarWorks@UMass Amherst. For more information, please contact [email protected]. INHIBITION AND COFACTOR TARGETING OF HYPOXIA-SENSING PROTEINS A Dissertation Presented by CORNELIUS TAABAZUING Submitted to the Graduate School of the University of Massachusetts Amherst in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY May 2015 Department of Chemistry © Copyright by Cornelius Taabazuing 2015 All Rights Reserved INHIBITION AND COFACTOR TARGETING OF HYPOXIA-SENSING PROTEINS A Dissertation Presented by CORNELIUS TAABAZUING Approved as to style and content by: ______________________________ Michael J. Knapp, Chair ______________________________ Michael J. Maroney, Member ______________________________ Nathan A. Schnarr, Member ______________________________ Scott C. Garman, Outside Member ______________________________ Craig T. Martin, Department Head Department of Chemistry DEDICATION To my mom, Barbara Soonyime, thank you for the sacrifices you have made to make it possible to pursue my dreams. To my wife Rachelle Taabazuing, thank you for providing me with your love, motivation, and patience.
    [Show full text]
  • Structural and Mechanistic Studies on 2-Oxoglutarate-Dependent Oxygenases and Related Enzymes Christopher J Schofield and Zhihong Zhang
    722 Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes Christopher J Schofield and Zhihong Zhang Mononuclear nonheme-Fe(II)-dependent oxygenases comprise The 2OG-dependent oxygenases have emerged as the an extended family of oxidising enzymes, of which the largest known family of nonheme oxidising enzymes [7,8] 2-oxoglutarate-dependent oxygenases and related enzymes are (Figure 1a). Their occurrence is ubiquitous, having been the largest known subgroup. Recent crystallographic and identified in many organisms ranging from prokaryotes to mechanistic studies have helped to define the overall fold of eukaryotes. Recent evidence also indicates that a 2OG- the 2-oxoglutarate-dependent enzymes and have led to the dependent oxygenase, prolyl 4-hydroxylase, is expressed by identification of coordination chemistry closely related to that of the P. bursaria Chlorella virus-1 [9]. Oxidative reactions catal- other nonheme-Fe(II)-dependent oxygenases, suggesting ysed by 2OG-dependent dioxygenases are steps in the related mechanisms for dioxygen activation that involve iron- biosynthesis of a variety of metabolites, including materials mediated electron transfer. of medicinal or agrochemical importance, such as plant ‘hor- mones’ (e.g. gibberellins) and antibiotics (e.g. cephalosporins Address and the β-lactamase inhibitor clavulanic acid). The Oxford Centre for Molecular Sciences and the Department of Chemistry, The Dyson Perrins Laboratory, South Parks Road, Oxford In mammals, the best-characterised 2OG-dependent oxy- OX1 3QY, UK genase is prolyl-4-hydroxylase, which catalyses the Current Opinion in Structural Biology 1999, 9:722–731 post-translational hydroxylation of proline residues in col- lagen. Mammalian prolyl-4-hydroxylase is an α β 0959-440X/99/$ — see front matter © 1999 Elsevier Science Ltd.
    [Show full text]
  • Oxidative Cyclizations in Orthosomycin Biosynthesis Expand the Known Chemistry of an Oxygenase Superfamily
    Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily Kathryn M. McCullocha, Emilianne K. McCranieb, Jarrod A. Smithc, Maruf Sarwara, Jeannette L. Mathieua, Bryan L. Gitschlaga,YuDub, Brian O. Bachmannb,c,1, and T. M. Iversona,c,1 aDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232; bDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235; and cDepartment of cBiochemistry, Vanderbilt University, Nashville, TN 37232 Edited by John T. Groves, Princeton University, Princeton, NJ, and approved July 2, 2015 (received for review January 26, 2015) Orthosomycins are oligosaccharide antibiotics that include avila- and avilamycin, which each contain two orthoester linkages (Fig. mycin, everninomicin, and hygromycin B and are hallmarked by a 1A, red) and a methylenedioxy bridge (Fig. 1A, blue). Methyl- rigidifying interglycosidic spirocyclic ortho-δ-lactone (orthoester) enedioxy bridge formation has previously been attributed to cy- linkage between at least one pair of carbohydrates. A subset of tochrome P450 enzymes (7, 8). However, orthoester linkage orthosomycins additionally contain a carbohydrate capped by a biosynthesis has not previously been described. Orthoester linkage methylenedioxy bridge. The orthoester linkage is necessary for formation is associated with especially demanding steric con- antibiotic activity but rarely observed in natural products. straints and substrates that are already highly oxygenated, and its Orthoester linkage and methylenedioxy bridge biosynthesis re- biosynthesis results in a unique trioxaspiro functional group. quire similar oxidative cyclizations adjacent to a sugar ring. We Everninomicin and avilamycin biosynthetic gene clusters en- have identified a conserved group of nonheme iron, α-ketogluta- code upwards of 50 enzymes with many lacking assigned func- rate–dependent oxygenases likely responsible for this chemistry.
    [Show full text]
  • Identification Et Caractérisation Fonctionnelle De Gènes Impliqués Dans La Voie De Biosynthèse Des Furocoumarines Chez Les Végétaux Supérieurs Guilhem Vialart
    Identification et caractérisation fonctionnelle de gènes impliqués dans la voie de biosynthèse des furocoumarines chez les végétaux supérieurs Guilhem Vialart To cite this version: Guilhem Vialart. Identification et caractérisation fonctionnelle de gènes impliqués dans la voiede biosynthèse des furocoumarines chez les végétaux supérieurs. Agronomie. Université de Lorraine, 2012. Français. NNT : 2012LORR0390. tel-01750069 HAL Id: tel-01750069 https://hal.univ-lorraine.fr/tel-01750069 Submitted on 29 Mar 2018 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. AVERTISSEMENT Ce document est le fruit d'un long travail approuvé par le jury de soutenance et mis à disposition de l'ensemble de la communauté universitaire élargie. Il est soumis à la propriété intellectuelle de l'auteur. Ceci implique une obligation de citation et de référencement lors de l’utilisation de ce document. D'autre part, toute contrefaçon, plagiat, reproduction illicite encourt une poursuite pénale. Contact : [email protected] LIENS Code de la Propriété Intellectuelle. articles L 122. 4 Code de la Propriété Intellectuelle. articles L 335.2- L 335.10 http://www.cfcopies.com/V2/leg/leg_droi.php http://www.culture.gouv.fr/culture/infos-pratiques/droits/protection.htm UMR 1121, Université de Lorraine-INRA, RP2E Laboratoire Agronomie et Environnement Thèse de recherche Identification et caractérisation fonctionnelle de gènes impliqués dans la voie de biosynthèse des furocoumarines chez les végétaux supérieurs.
    [Show full text]
  • Annual Research Report 2005
    INSTITUTE OF CATALYSIS AND SURFACE CHEMISTRY POLISH ACADEMY OF SCIENCES ANNUAL RESEARCH REPORT 2005 Krakow, January 2006 CONTENTS Preface 3 Research Teams of the Institute 7 Research Subjects and Projects in 2005 39 Reports on Research Activities in 2005 43 Scientific Output of the Institute in 2005 159 1 2 INSTITUTE OF CATALYSIS AND SURFACE CHEMISTRY Polish Academy of Sciences From theory to experiment and application Institute of Catalysis and Surface Chemistry (ICSC) of the Polish Academy of Sciences in Cracow is the only scientific institution in Poland and one of eight in the world devoted entirely to research in catalysis and chemistry of interfaces. The Institute pursues interdisciplinary studies of the phenomena occurring at gas/solid, gas/liquid and liquid/solid interfaces, with emphasis on their significance in catalysis, materials engineering, adsorption, coating technologies, flotation and detergency. ICSC integrates fundamental theoretical and experimental studies, and combines them with applied research so that the results obtained can be used directly to improve technological processes. The number of employees is about 100, of which a half are research staff. Over 20 PhD students are also involved in the research. ICSC is equipped with state-of-the-art research instrumentation, which serves not only Institute’s employees but is also available to the whole scientific community. Theory An important aspect of the research carried out at ICSC is to provide the theoretical background for experimental studies. The methodologies employed involve quantum chemistry and solid state physics modelling methods, as well as molecular mechanics and Monte-Carlo simulation techniques. The field of expertise ranges from elucidating catalytic reaction mechanisms and modelling the structures of transition metal oxides, composite nanomaterials and enzyme active centres, to describing surfactant adsorption at liquid/gas and liquid/liquid interfaces, and simulating polymer particle adsorption on solid homogenous surfaces.
    [Show full text]
  • Characterization of Natural Product Biological Imprints for Computer-Aided Drug Design Applications Noe Sturm
    Characterization of natural product biological imprints for computer-aided drug design applications Noe Sturm To cite this version: Noe Sturm. Characterization of natural product biological imprints for computer-aided drug design applications. Cheminformatics. Université de Strasbourg, 2015. English. NNT : 2015STRAF059. tel-01300872 HAL Id: tel-01300872 https://tel.archives-ouvertes.fr/tel-01300872 Submitted on 11 Apr 2016 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. UNIVERSITÉ DE STRASBOURG ÉCOLE DOCTORALE DES SCIENCES CHIMIQUES Laboratoire d’Innovation Thérapeutique, UMR 7200 en cotutelle avec Eskitis Institute for Drug Discovery, Griffith University THÈSE présentée par Noé STURM soutenue le : 8 Décembre 2015 pour obtenir le grade de : Docteur de l’université de Strasbourg Discipline/Spécialité : Chimie/Chémoinformatique Caractérisation de l’empreinte biologique des produits naturels pour des applications de conception rationnelle de médicament assistée par ordinateur THÈSE dirigée par : KELLENBERGER Esther Professeur, Université de Strasbourg QUINN Ronald Professeur, Université de Griffith, Brisbane, Australie RAPPORTEURS : IORGA Bogdan Chargé de recherche HDR, Institut de Chimie des Substances Naturelles, Gif-sur-Yvette GÜNTHER Stefan Professeur, Université Albert Ludwigs, Fribourg, Allemagne Acknowledgments First of all, I would like to thank my two supervisors Professor Kellenberger Esther and Professor Quinn Ronald for their excellent assistance, both academic and personal in nature.
    [Show full text]
  • Monooxygenase Diversity and Oxygen Activation Within Polyketide Antibiotic Biosynthesis
    MONOOXYGENASE DIVERSITY AND OXYGEN ACTIVATION WITHIN POLYKETIDE ANTIBIOTIC BIOSYNTHESIS Thadée Remy Pierre Grocholski TURUN YLIOPISTON JULKAISUJA – ANNALES UNIVERSITATIS TURKUENSIS Sarja - ser. AI osa - tom. 535 | Astronomica - Chemica - Physica - Mathematica | Turku 2016 University of Turku Faculty of Mathematics and Natural Sciences Department of Biochemistry Biochemistry Doctoral Programme in Molecular Life Sciences Supervised by Docent Mikko Metsä-Ketelä, Ph.D. Docent Jarmo Niemi, Ph.D. Department of Biochemistry Department of Biochemistry University of Turku University of Turku Reviewed by Nina Hakulinen, Ph.D. (Academy Research Fellow) Robert Schnell, Ph.D. (senior researcher) Department of Chemistry Department of Medical Biochemistry University of Eastern Finland and Biophysics Joensuu, Finland Karolinska Institutet, MBB, Stockholm, Sweden Opponent Professor Timothy Bugg, Ph.D. Department of Chemistry University of Warwick Coventry, UK The originality of this thesis has been checked in accordance with the University of Turku quality assurance system using the Turnitin OriginalityCheck service. ISBN 978-951-29-6421-5 (PRINT) ISBN 978-951-29-6422-2 (PDF) ISSN 0082-7002 (Print) ISSN 2343-3175 (Online) Painosalama Oy - Turku, Finland 2016 Contents 3 CONTENTS LIST OF ORIGINAL PUBLICATIONS ........................................................................................... 4 ABSTRACT .............................................................................................................................. 5 TIIVISTELMÄ ..........................................................................................................................
    [Show full text]