DOCSLIB.ORG

Biocatalysis-2019.Pdf

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Biocatalysis-2019.Pdf INTERNATIONAL CONFERENCE BC - 2019 BIOCATALYSIS: FUNDAMENTALS & APPLICATIONS 12th INTERNATIONAL CONFERENCE BIOCATALYSIS-2019: FUNDAMENTALS & APPLICATIONS ABSTRACTS June, 24-28, 2019 St. Petersburg - Valaam - Kizhi Russian Federation th INTERNATIONAL CONFERENCE 12 INTERNATIONAL CONFERENCE BC - 2019 BIOCATALYSIS-2019: BIOCATALYSIS: FUNDAMENTALS & APPLICATIONS FUNDAMENTALS & APPLICATIONS ORGANIZING COMMITTEE Chairman: Prof. S. Varfolomeyev Vice-Chairman: Prof. I. Kurochkin Secretary: Dr. T. Osipova Members: Prof. Gabibov A. Prof. Sinyashin O. Prof. Popov V. Prof. Bachurin S. Prof. Bonch-Osmolovskaya E. Prof. Tishkov V. Prof. Klyachko N. Prof. Nemukhin A. Dr. Knorre V. Dr. Gachok I. Dr. Zaitseva E. Mr. Rybalov A. PROGRAMME COMMITTEE Chairman: Prof. V. Tishkov Vice-Chairman: Dr. A.Pometun Members: Prof. Gabibov A. Prof. Kurochkin I. Prof. Švedas V. Prof. Klyachko N. Prof. Ugarova N. Dr. Belogurov A. Prof. Bonch-Osmolovskaya E. Dr. Savin S. Sponsored by Technical secretariat ©2019 Innovations and High Technologies MSU Ltd. INTERNATIONAL CONFERENCE BC - 2019 BIOCATALYSIS: FUNDAMENTALS & APPLICATIONS 12th INTERNATIONAL CONFERENCE BIOCATALYSIS-2019: FUNDAMENTALS & APPLICATIONS ABSTRAСTS St.Petersburg – Valaam – Kizhi June, 24-28, 2019 ©2019 Innovations and High Technologies MSU Ltd. УДК 577(035.3) Biocatalysis-2019: Abstracts of 12th International Conference “Biocatalysis: Fundamentals and Applications” / Editor V. Tishkov [Electronic resource] – Moscow: Innovations and High Technologies MSU Ltd, 2019 – 1 electronic optical disk (CD-ROM); 12 cm. – System requirements: Personal computer with processor 486+, Windows 95, CD-drive; Adobe Acrobat Reader. ISBN 978-5-9651-1245-6 The 12th International сonference “Biocatalysis-2019” was organized with the financial support of the Russian Foundation for Basic Research, project No. 19-04-20065 "12th International Conference “Biocatalysis. Fundamentals and application” (“Biocatalysis-2019”)". Биокатализ – 2019: Тезисы 12-ой Международной конференции «Биокатализ: Фундаментальные основы и применение» / Редактор В.И.Тишков [Электронный ресурс] – М.: ООО «Иннотех МГУ», 2019. – 1 электрон. опт. диск (CD-ROM); 12 см. – Системные требования: ПК с процессором 486+; Windows 95; дисковод CD-ROM; Adobe Acrobat Reader. – 250 экз. ISBN 978-5-9651-1245-6 12-я Международная конференция «Biocatalysis-2019» была организована при финансовой поддержке Российского Фонда Фундаментальных Исследований, проект № 19-04-20065 "12-я Международная конференция «Биокатализ. Фундаментальные основы и применение» («Биокатализ-2019»)". The Organizing Committee is also grateful to the sponsors - organizations and individuals, who participated in the financing of the conference: – Ministry of Education and Science of the Russian Federation – M.V. Lomonosov Moscow State University – RUSNANO – BioChemMack, JSC – “Plastic polymetal” – DIA.M – Dr. B. Kim (QIWI Bank) – Dr. D. Medman ©2019 Innovations and High Technologies MSU Ltd. TABLE OF CONTENT Lectures List Plenary Lectures 6 Fundamental Biocatalysis 7 Applied Bioctalysis 9 Medicine 9 Analytics 10 Nano 11 Extremophiles 12 Posters List 13 Lectures Abstract 17 Posters Abstract 104 - 5 - LECTURES LIST Plenary Lectures Gabibov Aleksander 18 Novel approaches for screening biodiversity Vladimirov Yury 19 Enzymes, radicals, deseases and agening Bonch-Osmolovskaya Elizaveta 20 New thermophilic prokaryotes, new metabolic pathways Wohlgemuth Roland 21 Extremophilic Enzymes for resource-efficient, robust and selective biocatalytic syn- thesis of small molecules Varfolomeev Sergey 22 Neuroenzymology: kinetics of biocatalytical reactions in human brain Masson Patrick 23 Competing substrate kinetics for michaelian enzymes and for enzymes showing activation/inhibition by excess substrate: application to kinetic analysis of cholines- terases Tishkov Vladimir 24 New biocatalysts for processes of fine organic and chiral synthesis with oxidoreduc- tases Švedas Vytas 25 Knowledge-based modulation of enzyme functional properties Egorov Aleksey 26 Beta-lactamases - drivers of bacterial antibiotic resistance Savitsky Alexander 27 Development of new enzyme mechanisms of animal antiviral resistance using Afri- can swine fever virus model Nemukhin Aleksander 28 Diversity of mechanisms in enzyme-catalyzed phosphorus-oxygen bond cleavage reactions Ugarova Natalia 29 The emitter as an intramolecular probe in the luciferase active center Bronich Tatyana 30 Nanotechnology platforms in cancer therapy (Engineering Targeted Polymeric Nanocarriers for Drug Delivery) Deev Sergey 31 Smart nanomaterials for biomedical application Kurochkin Ilya 32 Highly sensitive bioanalytical systems based on plasmonic and polymer nanocom- posites Klyachko Natalia 33 Overcoming Biological Barriers in Proteins Drug Delivery - 6 - Fundamental Biocatalysis General Aspects Miroshnikov Konstantin 34 Bacteriophage tail spike proteins: Enzymatic interaction with bacterial polysaccharide directs viral specificity Smirnov Ivan 35 Amicoumacin A kinases: structure, kinetics and function Eldarov Mikhail, Tishkov Vladimir 36 Genetic, biochemical and physiological characterization of novel D-amino acid oxidases from Ogataea parapolymorpha DL-1 Muronetz Vladimir 37 Effect of post-translational modifications on the amyloid transformation of proteins Rozova Olga 38 Malic enzymes in the metabolism of obligate methanotrophs Martirosyan Levon 39 Changes in peroxidase activity in horseradish (Armoracia rusticana) roots with red light additional irradiation under conditions of aeroponic phytotron Likhtenstein Gerz 40 Orbital Factors Affected on Electron Transfer and Light Energy Conversion in Pho- toenzymes and Model Systems: A Connection between Spin Exchange and Elec- tron Transfer Dokudovskaya Svetlana 41 Regulation of mTORC1 pathway Bacheva Anna 42 Non-protein effectors of the proteasome Gromova Elizaveta 43 Functional role of DNMT3a DNA methyltransferase mutations observed in acute myeloid leukemia Rao Desirazu 44 Deciphering the functional requirement of Zinc finger motif(s) in Helicobacter pylori Topoisomerase I catalysis Kubareva Elena 45 Bacterial DNA-mismatch repair endonucleases MutL: structure and interaction with molecular partners - 7 - Structural Aspects of Biocatalysis Phillips Robert 46 Structure and mechanism of D-ornithine/D-lysine decarboxylase, a stereoinverting Fold-III decarboxylase Rakitina Tatyana 47 Application of X-ray crystallography, comparative modeling and molecular dynam- ics to investigation of structural determinants of enzymatic activation and sub- strate specificity. Boyko Konstantin 48 3D structure of the natural tetrameric form of human butyrylcholinesterase as re- vealed by cryoEM, MD and SAXS Demidkina Tatyana] 49 Sulfoxides of sulfur-containing amino acids - suicidal substrates of methionine gamma-lyase as antimicrobial and antimycotic prodrugs. Bezsudnova Ekaterina 50 Effects of amino acid substitutions in the characteristic sequence motifs on the profile of substrate specificity of PLP fold type IV transaminases Tishchenko Svetlana 51 Investigation of T2 channel of two-domain laccases Computer Modeling and Bioinformatics Hayashi Hideyuki 52 Quantum-chemical analysis of the catalytic reaction of aspartate aminotransferase Sokalski Waclaw 53 Origins of enzyme catalytic activity explored within theory of intermolecular inter- actions and biocatalyst design using catalytic fields Khrenova Maria 54 Towards deep insight into the cephalosporin hydrolysis in the active site of metal- lo-beta-lactamase Zlobin Aleksandr 55 Towards application of deep convolutional neural networks to enzyme design Zalevsky Artur 56 Unraveling Na+ dependent thrombin activation with large-scale QM/MM simula- tions Mikoulinskaia Galina 57 L,D-peptidases of coliphages: structure, properties, regulation and biotechnologi- cal potential - 8 - Applied Biocatalysis Littlechild-Bond Jennifer 58 Thermophilic Enzymes for Industrial Biocatalysis Gusakov Aleksander 59 Lytic polysaccharide monooxygenases: structure, mechanism and function Batyrova Khorcheska 60 Novel enzymes for biosynthesis and biotransformation of adipic acid You Delin 61 Baeyer-Villiger Monooxygenases XanO4 Catalyzes Cyclic Ether Formation Atroshenko Denis 62 Multipoint mutants of TvDAAO with improved catalytic properties and stability Medicine Trudil David 63 Use of Bacteriophage and lytic enzymes for the detection, treatment and prevention of bacterial infections Maksimenko Aleksander 64 New challenges of contemporary healthcare. Enzyme derivatives of combined action and conjunctive courses of biocatalysts Klochkov Sergey 65 Natural scaffolds as modulators of farnesyltransferase activity Yakovlev Aleksey 66 1H NMR in vivo study of inhibitory neurotransmitter impact to human brain in videost- imulation Filatova Lubov 67 Interaction of lysozyme with mucoadhesive polymers Belogurov Aleksey 68 Charge-mediated proteasome targeting as a novel type of ubiquitin-independent degrons Herrmann Martin 69 Aggregated neutrophil extracellular traps are multifaceted biocatalysts. Gazaryan Irina 70 Activation of antioxidant genetic program: a mechanistic insight Makhaeva Galina 71 From acetylcholinesterase inhibitors to multitarget ligands: a step forward in Alz- heimer‘s disease drug discovery Abramov Andrey 72 The role reactive oxygen species production in physiology and in mechanisms of neurodegeneration Demina Olga 73 Design and development of antiplatelet agents. - 9 - Analytical Application of Biocatalysis Zvereva Maria 74 Oligonucleotide functionalized nanoparticles for SERRS detection
Load more

Recommended publications
  • UC Berkeley UC Berkeley Electronic Theses and Dissertations
    UC Berkeley UC Berkeley Electronic Theses and Dissertations Title Analyzing Microbial Physiology and Nutrient Transformation in a Model, Acidophilic Microbial Community using Integrated `Omics' Technologies Permalink https://escholarship.org/uc/item/259113st Author Justice, Nicholas Bruce Publication Date 2013 Supplemental Material https://escholarship.org/uc/item/259113st#supplemental Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California Analyzing Microbial Physiology and Nutrient Transformation in a Model, Acidophilic Microbial Community using Integrated ‘Omics’ Technologies By Nicholas Bruce Justice A dissertation submitted in partial satisfaction of the requirements for the degree of Doctor of Philosophy in Microbiology in the Graduate Division of the University of California, Berkeley Committee in charge: Professor Jillian Banfield, Chair Professor Mary Firestone Professor Mary Power Professor John Coates Fall 2013 Abstract Analyzing Microbial Physiology and Nutrient Transformation in a Model, Acidophilic Microbial Community using Integrated ‘Omics’ Technologies by Nicholas Bruce Justice Doctor of Philosophy in Microbiology University of California, Berkeley Professor Jillian F. Banfield, Chair Understanding how microorganisms contribute to nutrient transformations within their community is critical to prediction of overall ecosystem function, and thus is a major goal of microbial ecology. Communities of relatively tractable complexity provide a unique opportunity to study the distribution of metabolic characteristics amongst microorganisms and how those characteristics subscribe diverse ecological functions to co-occurring, and often closely related, species. The microbial communities present in the low-pH, metal-rich environment of the acid mine drainage (AMD) system in Richmond Mine at Iron Mountain, CA constitute a model microbial community due to their relatively low diversity and extensive characterization over the preceding fifteen years.
    [Show full text]
  • Microbial Biochemistry, 2Nd Edition
    Microbial Biochemistry . G.N. Cohen Microbial Biochemistry Second Edition Prof. G.N. Cohen Institut Pasteur rue du Docteur Roux 28 75724 Paris France [email protected] ISBN 978-90-481-9436-0 e-ISBN 978-90-481-9437-7 DOI 10.1007/978-90-481-9437-7 Springer Dordrecht Heidelberg London New York Library of Congress Control Number: 2010938472 # Springer Science+Business Media B.V. 2011 No part of this work may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording or otherwise, without written permission from the Publisher, with the exception of any material supplied specifically for the purpose of being entered and executed on a computer system, for exclusive use by the purchaser of the work. Printed on acid-free paper Springer is part of Springer Science+Business Media (www.springer.com) Foreword This book originates from almost 60 years of living in the company of micro- organisms, mainly with Escherichia coli. My scientific life has taken place almost exclusively at the Institut Pasteur in Paris, where many concepts of modern molecular biology were born or developed. The present work emphasizes the interest of microbial physiology, biochemistry and genetics. It takes into account the considerable advances which have been made in the field in the last 30 years by the introduction of gene cloning and sequencing and by the exponential development of physical methods such as X-ray crystallog- raphy of proteins. The younger generation of biochemists is legitimately interested in the problems raised by differentiation and development in higher organisms, and also in neuros- ciences.
    [Show full text]
  • Product Sheet Info
    Master Clone List for NR-19279 ® Vibrio cholerae Gateway Clone Set, Recombinant in Escherichia coli, Plates 1-46 Catalog No. NR-19279 Table 1: Vibrio cholerae Gateway® Clones, Plate 1 (NR-19679) Clone ID Well ORF Locus ID Symbol Product Accession Position Length Number 174071 A02 367 VC2271 ribD riboflavin-specific deaminase NP_231902.1 174346 A03 336 VC1877 lpxK tetraacyldisaccharide 4`-kinase NP_231511.1 174354 A04 342 VC0953 holA DNA polymerase III, delta subunit NP_230600.1 174115 A05 388 VC2085 sucC succinyl-CoA synthase, beta subunit NP_231717.1 174310 A06 506 VC2400 murC UDP-N-acetylmuramate--alanine ligase NP_232030.1 174523 A07 132 VC0644 rbfA ribosome-binding factor A NP_230293.2 174632 A08 322 VC0681 ribF riboflavin kinase-FMN adenylyltransferase NP_230330.1 174930 A09 433 VC0720 phoR histidine protein kinase PhoR NP_230369.1 174953 A10 206 VC1178 conserved hypothetical protein NP_230823.1 174976 A11 213 VC2358 hypothetical protein NP_231988.1 174898 A12 369 VC0154 trmA tRNA (uracil-5-)-methyltransferase NP_229811.1 174059 B01 73 VC2098 hypothetical protein NP_231730.1 174075 B02 82 VC0561 rpsP ribosomal protein S16 NP_230212.1 174087 B03 378 VC1843 cydB-1 cytochrome d ubiquinol oxidase, subunit II NP_231477.1 174099 B04 383 VC1798 eha eha protein NP_231433.1 174294 B05 494 VC0763 GTP-binding protein NP_230412.1 174311 B06 314 VC2183 prsA ribose-phosphate pyrophosphokinase NP_231814.1 174603 B07 108 VC0675 thyA thymidylate synthase NP_230324.1 174474 B08 466 VC1297 asnS asparaginyl-tRNA synthetase NP_230942.2 174933 B09 198
    [Show full text]
  • Comparative Genomics Study of Polyhydroxyalkanoates (PHA) and Ectoine Relevant Genes from Halomonas Sp
    Cai et al. Microbial Cell Factories 2011, 10:88 http://www.microbialcellfactories.com/content/10/1/88 RESEARCH Open Access Comparative genomics study of polyhydroxyalkanoates (PHA) and ectoine relevant genes from Halomonas sp. TD01 revealed extensive horizontal gene transfer events and co-evolutionary relationships Lei Cai1†, Dan Tan1†, Gulsimay Aibaidula2, Xin-Ran Dong3, Jin-Chun Chen1, Wei-Dong Tian3* and Guo-Qiang Chen1* Abstract Background: Halophilic bacteria have shown their significance in industrial production of polyhydroxyalkanoates (PHA) and are gaining more attention for genetic engineering modification. Yet, little information on the genomics and PHA related genes from halophilic bacteria have been disclosed so far. Results: The draft genome of moderately halophilic bacterium, Halomonas sp. TD01, a strain of great potential for industrial production of short-chain-length polyhydroxyalkanoates (PHA), was analyzed through computational methods to reveal the osmoregulation mechanism and the evolutionary relationship of the enzymes relevant to PHA and ectoine syntheses. Genes involved in the metabolism of PHA and osmolytes were annotated and studied in silico. Although PHA synthase, depolymerase, regulator/repressor and phasin were all involved in PHA metabolic pathways, they demonstrated different horizontal gene transfer (HGT) events between the genomes of different strains. In contrast, co-occurrence of ectoine genes in the same genome was more frequently observed, and ectoine genes were more likely under coincidental horizontal gene transfer than PHA related genes. In addition, the adjacent organization of the homologues of PHA synthase phaC1 and PHA granule binding protein phaP was conserved in the strain TD01, which was also observed in some halophiles and non-halophiles exclusively from g- proteobacteria.
    [Show full text]
  • Systems Metabolic Engineering of Basfia Succiniciproducens For
    Systems metabolic engineering of Corynebacterium glutamicum for production of L-lysine and ectoine Dissertation zur Erlangung des Grades des Doktors der Ingenieurwissenschaften der Naturwissenschaftlich-Technischen Fakultät der Universität des Saarlandes von Gideon Gießelmann Saarbrücken 2019 Tag des Kolloquiums: 16.7.2019 Dekan: Prof. Guido Kickelbick Berichterstatter 1: Prof. Christoph Wittmann Berichterstatter 2: Prof. Gert-Wieland Kohring Vorsitz: Prof. Bruce Morgan Akad. Mitarbeiter: Dr. Björn Becker Publications Partial results of this work have been published previously. This was authorized by the Institute of Systems Biotechnology, represented by Prof. Dr. Christoph Wittmann. Peer-reviewed articles: Gießelmann G, D. Dietrich, L. Jungmann, M. Kohlstedt, E. Jung Jeon, S. Sun Yim, F. Sommer, D. Zimmer, T. Mühlhaus, M. Schroda, K. Jun Jeong, J. Becker, and C. Wittmann, 2019. Metabolic engineering of Corynebacterium glutamicum for high-level ectoine production – design, combinatorial assembly and implementation of a transcriptionally balanced heterologous ectoine pathway. Biotechnology Journal, under revision Becker J, G. Gießelmann, SL. Hoffmann, C. Wittmann, 2016: Corynebacterium glutamicum for sustainable bioproduction: from metabolic physiology to systems metabolic engineering. In: Zhao H., Zeng AP. (eds) Synthetic Biology – Metabolic Engineering. Advances in Biochemical Engineering/Biotechnology, vol 162. Springer, Cham The following peer-reviewed articles were published during this work, but are not part of the dissertation: Rohles CM, L. Gläser, M. Kohlstedt, G. Gießelmann, S. Pearson, A. del Campo, J. Becker, C. Wittmann, 2018. A bio-based route to the carbon-5 chemical glutaric acid and to bionylon-6,5 using metabolically engineered Corynebacterium glutamicum, Green Chemistry 20:4662-4674. Vassilev I, G. Gießelmann, SK. Schwechheimer, C. Wittmann, B Virdis, JO.
    [Show full text]
  • Metabolic Engineering of Escherichia Coli for Ectoine Production with the Fermentation Strategy of Supplementing Amino Donor
    Metabolic Engineering of Escherichia Coli for Ectoine Production With the Fermentation Strategy of Supplementing Amino Donor Hao Zhang Nanjing Tech University Yingying Cao Nanjing Tech University Yingsheng Dong Nanjing Tech University Ming Zhao Nanjing Tech University Yanqin Ma Nanjing Tech University Zhengshan Luo Nanjing Tech University Sha Li ( [email protected] ) Nanjing Tech University https://orcid.org/0000-0001-8256-1263 Hong Xu Nanjing Tech University Research Keywords: Ectoine, Escherichia coli, Metabolic engineering, Medium optimization, Amino donor, RT qPCR Posted Date: December 28th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-134030/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/17 Abstract Background: Ectoine, a compatible solute, has broad application prospects in food biotechnology, agriculture, medicine, and cosmetics because of its protective action on biological compounds. Industrially, ectoine is produced by halophilic bacteria in a complex process. Recently, various works focus on improving ectoine production by using engineered strains, but there are still problems of low yield and low ectoine production eciency. Results: To overcome the drawback, a nal metabolic engineered strain E. coli ET08 was constructed by eliminating lysine synthesis branch and by-product metabolic pathways, and ectoine production reached 10.2 g/L through culture medium optimization. Compared with nitrate, addition of ammonium salt contributed more to the ectoine synthesis. Furthermore, the ammonium sulphate boosted more ectoine titers than ammonium chloride and sodium glutamate. The analysis of transcriptional levels revealed that the ammonium sulfate enhanced ectoine biosynthesis by enhancing metabolic ux toward ectoine biosynthesis and providing auent synthetic precursors.
    [Show full text]
  • Pseudomonas/Brachypodium As a Model System for Studying Rhizosphere Plant Microbe Interactions Under Water Stress
    The University of Southern Mississippi The Aquila Digital Community Master's Theses Fall 12-1-2018 Pseudomonas/Brachypodium as a Model System for Studying Rhizosphere Plant Microbe Interactions Under Water Stress Janiece McWilliams University of Southern Mississippi Follow this and additional works at: https://aquila.usm.edu/masters_theses Recommended Citation McWilliams, Janiece, "Pseudomonas/Brachypodium as a Model System for Studying Rhizosphere Plant Microbe Interactions Under Water Stress" (2018). Master's Theses. 602. https://aquila.usm.edu/masters_theses/602 This Masters Thesis is brought to you for free and open access by The Aquila Digital Community. It has been accepted for inclusion in Master's Theses by an authorized administrator of The Aquila Digital Community. For more information, please contact [email protected]. PSEUDOMONAS/BRACHYPODIUM AS A MODEL SYSTEM FOR STUDYING RHIZOSPHERE PLANT-MICROBE INTERACTIONS UNDER WATER STRESS by Janiece Hutchins McWilliams A Thesis Submitted to the Graduate School, the College of Arts and Sciences and the School of Biological, Environmental, and Earth Sciences at The University of Southern Mississippi in Partial Fulfillment of the Requirements for the Degree of Master of Science Approved by: Dr. Dmitri Mavrodi, Committee Chair Dr. Kevin Kuehn Dr. Micheal Davis ____________________ ____________________ ____________________ Dr. Dmitri Mavrodi Dr. Jake Schaefer Dr. Karen S. Coats Committee Chair Director of School Dean of the Graduate School December 2018 ABSTRACT In contrast to well-studied mechanisms of drought tolerance in plants, the interactions between plants and their microbiome during water stress are still poorly understood. This missing knowledge is crucial for the exploitation of beneficial microbial communities to improve the sustainability of agriculture under changing climatic conditions.
    [Show full text]
  • Cellular Adjustments of Bacillus Subtilis and Other Bacilli to Fluctuating Salinities
    Chapter 15 Cellular Adjustments of Bacillus subtilis and Other Bacilli to Fluctuating Salinities Marco Pittelkow and Erhard Bremer 15.1 The Osmotic Challenge Bacilli are exposed, either suddenly or on a sustained basis, to changes in the osmotic conditions of the varied ecological niches that they can colonize. This can be vividly visualized by considering the main habitat of Bacillus subtilis, the upper layers of the soil (Earl et al. 2008). Rainfall and drying of the soil cause fluctuations in water availability and in the osmotic potential of this ecological niche. Such changes pose a considerable challenge to the microbial cell since they elicit water fluxes across the cytoplasmic membrane. These water fluxes are driven by the differential in the osmotic potential between the cell’s interior and that of the surrounding microenvironment (Bremer and Kr€amer 2000). Water entry at low osmolarity can increase turgor to such an extent that the elastic and stress-bearing peptidoglycan sacculus can no longer cope with it and the cell will rupture. Water efflux at high osmolarity will trigger dehydration of the cytoplasm and the ensuing reduction or even collapse of turgor will cause growth arrest or even cell death. Turgor, an intracellular hydrostatic pressure considered to be essential for cell expansion and growth, is difficult to determine experimentally but has been estimated at 1.9 MPa (19.37 atm) for B. subtilis (Whatmore and Reed 1990), a pressure that is close to ten times the pressure present in a standard car tire. To maintain turgor within physiologically acceptable boundaries, the B. subtilis cell needs to take active countermeasures to redirect the flow of water in or out of the cell when it faces decreases or increases in the external osmolarity.
    [Show full text]
  • SI Appendix Index 1
    SI Appendix Index Calculating chemical attributes using EC-BLAST ................................................................................ 2 Chemical attributes in isomerase reactions ............................................................................................ 3 Bond changes …..................................................................................................................................... 3 Reaction centres …................................................................................................................................. 5 Substrates and products …..................................................................................................................... 6 Comparative analysis …........................................................................................................................ 7 Racemases and epimerases (EC 5.1) ….................................................................................................. 7 Intramolecular oxidoreductases (EC 5.3) …........................................................................................... 8 Intramolecular transferases (EC 5.4) ….................................................................................................. 9 Supporting references …....................................................................................................................... 10 Fig. S1. Overview …............................................................................................................................
    [Show full text]
  • "Ectoine Synthase: an Iron-Dependent Member of the Cupin Superfamily" In
    Ectoine synthase: an iron-dependent member of the cupin superfamily Laura Czech†,‡, Astrid Hoeppner§, Sander HJ Smits§,¶, and Erhard Bremer†,‡ †Department of Biology, Laboratory for Microbiology, Philipps-University Marburg, Marburg, Germany ‡SYNMIKRO Research Center, Philipps-University Marburg, Marburg, Germany §Center for Structural Studies, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany ¶Institute of Biochemistry, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany FUNCTIONAL CLASS harbors a catalytically critical Fe2+ ion. The three residues Enzyme; ectoine synthase (EctC), EC 4.2.1.108. EctC coordinating this metal protrude into the lumen of the belongs to the carbon–oxygen lyases (EC 4.2) and cupin barrel in which the EctC-promoted enzyme reaction, more specifically to the hydro-lyases (EC 4.2.1), a a water elimination, is catalyzed, using N-γ-ADABA as the 1 group of enzymes that cleaves carbon–oxygen bonds. substrate. The EctC enzyme catalyzes in an Fe2+-dependent fashion the last step of ectoine [(S)-2-methyl-1,4,5,6- tetrahydropyrimidine-4-carboxylic acid] synthesis through OCCURENCE cyclocondensation of the EctA-formed substrate N- γ-acetyl-L-2,4-diaminobutyric acid (N-γ-ADABA) via a EctC is the diagnostic enzyme of the ectoine biosynthetic 7–10 water-elimination reaction. The reaction product, ectoine, route, a set of three enzymes that produces this effective 11–13 is a member of the so-called compatible solutes and microbial stress-protectant and chemical chaperone. 14 serves as a cytoprotectant against osmotic stress and Biosynthesis of ectoine initiates from the central micro- 9,10,15–17 growth temperature extremes. It also functions as a bial metabolite L-aspartate-β-semialdehyde.
    [Show full text]
  • Table 4. V. Cholerae Flexgene ORF Collection
    Table 4. V. cholerae FLEXGene ORF collection Reference Clone protein PlasmID clone GenBank Locus tag Symbol accession identifier FLEX clone name accession Product name VC0001 NP_062585 VcCD00019918 FLH200476.01F DQ772770 hypothetical protein VC0002 mioC NP_062586 VcCD00019938 FLH200506.01F DQ772771 mioC protein VC0003 thdF NP_062587 VcCD00019958 FLH200531.01F DQ772772 thiophene and furan oxidation protein ThdF VC0004 yidC NP_062588 VcCD00019970 FLH200545.01F DQ772773 inner membrane protein, 60 kDa VC0005 NP_062589 VcCD00061243 FLH236482.01F DQ899316 conserved hypothetical protein VC0006 rnpA NP_062590 VcCD00025697 FLH214799.01F DQ772774 ribonuclease P protein component VC0007 rpmH NP_062591 VcCD00061229 FLH236450.01F DQ899317 ribosomal protein L34 VC0008 NP_062592 VcCD00019917 FLH200475.01F DQ772775 amino acid ABC transporter, ATP-binding protein VC0009 NP_062593 VcCD00019966 FLH200540.01F DQ772776 amino acid ABC transproter, permease protein VC0010 NP_062594 VcCD00019152 FLH199275.01F DQ772777 amino acid ABC transporter, periplasmic amino acid-binding portion VC0011 NP_062595 VcCD00019151 FLH199274.01F DQ772778 hypothetical protein VC0012 dnaA NP_062596 VcCD00017363 FLH174286.01F DQ772779 chromosomal DNA replication initiator DnaA VC0013 dnaN NP_062597 VcCD00017316 FLH174063.01F DQ772780 DNA polymerase III, beta chain VC0014 recF NP_062598 VcCD00019182 FLH199319.01F DQ772781 recF protein VC0015 gyrB NP_062599 VcCD00025458 FLH174642.01F DQ772782 DNA gyrase, subunit B VC0016 NP_229675 VcCD00019198 FLH199346.01F DQ772783 hypothetical protein
    [Show full text]
  • Metabolic Engineering of Corynebacterium Glutamicum for Production of the Chemical Chaperone Ectoine
    Metabolic engineering of Corynebacterium glutamicum for the production of L-aspartate and its derivatives β-alanine and ectoine Dissertation zur Erlangung des akademischen Grades Doktor der Naturwissenschaften (Dr. rer. nat.) Fakultät für Biologie Universität Bielefeld vorgelegt von Christian Ziert aus Fulda Ebersberg, April 2014 Table of contents Table of figures .................................................................................................8 List of tables ......................................................................................................9 Abbreviations .................................................................................................. 10 Summary ......................................................................................................... 11 Zusammenfassung .......................................................................................... 12 1 Introduction .............................................................................................. 13 1.1 Characteristics of Corynebacterium glutamicum and its application in biotechnology ........... 13 1.2 The central metabolism of C. glutamicum ............................................................................... 14 1.2.1 Carbon source uptake ...................................................................................................... 16 1.2.2 Glycolysis .......................................................................................................................... 17 1.2.3 Pentose
    [Show full text]