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An Atpase Domain Common to Prokaryotic Cell Cycle Proteins
Proc. Natl. Acad. Sci. USA Vol. 89, pp. 7290-7294, August 1992 Biochemistry An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp7O heat shock proteins (structural comparison/property pattern/remote homology) PEER BORK, CHRIS SANDER, AND ALFONSO VALENCIA European Molecular Biology Laboratory, D-6900 Heidelberg, Federal Republic of Germany Communicated by Russell F. Doolittle, March 6, 1992 ABSTRACT The functionally diverse actin, hexokinase, and hsp7O protein families have in common an ATPase domain of known three-dimensional structure. Optimal superposition ofthe three structures and alignment ofmany sequences in each of the three families has revealed a set of common conserved residues, distributed in five sequence motifs, which are in- volved in ATP binding and in a putative interdomain hinge. From the multiple sequence aliment in these motifs a pattern of amino acid properties required at each position is defined. The discriminatory power of the pattern is in part due to the use of several known three-dimensional structures and many sequences and in part to the "property" method ofgeneralizing from observed amino acid frequencies to amino acid fitness at each sequence position. A sequence data base search with the pattern significantly matches sugar kinases, such as fuco-, glucono-, xylulo-, ribulo-, and glycerokinase, as well as the prokaryotic cell cycle proteins MreB, FtsA, and StbA. These are predicted to have subdomains with the same tertiary structure as the ATPase subdomains Ia and Ha of hexokinase, actin, and Hsc7O, a very similar ATP binding pocket, and the capacity for interdomain hinge motion accompanying func- tional state changes. -
Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of Exodeoxyribonuclease III from Crenarchaeon Sulfolobus Tokodaii Strain 7
Crystal Structure Theory and Applications, 2013, 2, 155-158 Published Online December 2013 (http://www.scirp.org/journal/csta) http://dx.doi.org/10.4236/csta.2013.24021 Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of Exodeoxyribonuclease III from Crenarchaeon Sulfolobus tokodaii Strain 7 Shuichi Miyamoto1*, Chieko Naoe2, Masaru Tsunoda3, Kazuo T. Nakamura2 1Faculty of Pharmaceutical Sciences, Sojo University, Kumamoto, Japan 2School of Pharmacy, Showa University, Tokyo, Japan 3Faculty of Pharmacy, Iwaki Meisei University, Iwaki, Japan Email: *[email protected] Received October 13, 2013; revised November 12, 2013; accepted December 6, 2013 Copyright © 2013 Shuichi Miyamoto et al. This is an open access article distributed under the Creative Commons Attribution Li- cense, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. ABSTRACT Exodeoxyribonuclease III (EXOIII) acts as a 3’→5’ exonuclease and is homologous to purinic/apyrimidinic (AP) en- donuclease (APE), which plays an important role in the base excision repair pathway. To structurally investigate the reaction and substrate recognition mechanisms of EXOIII, a crystallographic study of EXOIII from Sulfolobus tokodaii strain 7 was carried out. The purified enzyme was crystallized by using the hanging-drop vapor-diffusion method. The crystals belonged to space group C2, with unit-cell parameters a = 154.2, b = 47.7, c = 92.4 Å, β = 125.8˚ and diffracted to 1.5 Å resolution. Keywords: Crenarchaeon; Crystallization; Exodeoxyribonuclease; Sulfolobus tokodaii; X-Ray Diffraction 1. Introduction formational change upon protein binding that permits complex formation and activation of attacking water, A variety of mechanisms exist to repair damaged DNA leading to incision, in the presence of Mg2+ [10,11]. -
Non-Homologous Isofunctional Enzymes: a Systematic Analysis Of
Omelchenko et al. Biology Direct 2010, 5:31 http://www.biology-direct.com/content/5/1/31 RESEARCH Open Access Non-homologousResearch isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution Marina V Omelchenko, Michael Y Galperin*, Yuri I Wolf and Eugene V Koonin Abstract Background: Evolutionarily unrelated proteins that catalyze the same biochemical reactions are often referred to as analogous - as opposed to homologous - enzymes. The existence of numerous alternative, non-homologous enzyme isoforms presents an interesting evolutionary problem; it also complicates genome-based reconstruction of the metabolic pathways in a variety of organisms. In 1998, a systematic search for analogous enzymes resulted in the identification of 105 Enzyme Commission (EC) numbers that included two or more proteins without detectable sequence similarity to each other, including 34 EC nodes where proteins were known (or predicted) to have distinct structural folds, indicating independent evolutionary origins. In the past 12 years, many putative non-homologous isofunctional enzymes were identified in newly sequenced genomes. In addition, efforts in structural genomics resulted in a vastly improved structural coverage of proteomes, providing for definitive assessment of (non)homologous relationships between proteins. Results: We report the results of a comprehensive search for non-homologous isofunctional enzymes (NISE) that yielded 185 EC nodes with two or more experimentally characterized - or predicted - structurally unrelated proteins. Of these NISE sets, only 74 were from the original 1998 list. Structural assignments of the NISE show over-representation of proteins with the TIM barrel fold and the nucleotide-binding Rossmann fold. From the functional perspective, the set of NISE is enriched in hydrolases, particularly carbohydrate hydrolases, and in enzymes involved in defense against oxidative stress. -
Sulfite Dehydrogenases in Organotrophic Bacteria : Enzymes
Sulfite dehydrogenases in organotrophic bacteria: enzymes, genes and regulation. Dissertation zur Erlangung des akademischen Grades des Doktors der Naturwissenschaften (Dr. rer. nat.) an der Universität Konstanz Fachbereich Biologie vorgelegt von Sabine Lehmann Tag der mündlichen Prüfung: 10. April 2013 1. Referent: Prof. Dr. Bernhard Schink 2. Referent: Prof. Dr. Andrew W. B. Johnston So eine Arbeit wird eigentlich nie fertig, man muss sie für fertig erklären, wenn man nach Zeit und Umständen das möglichste getan hat. (Johann Wolfgang von Goethe, Italienische Reise, 1787) DANKSAGUNG An dieser Stelle möchte ich mich herzlich bei folgenden Personen bedanken: . Prof. Dr. Alasdair M. Cook (Universität Konstanz, Deutschland), der mir dieses Thema und seine Laboratorien zur Verfügung stellte, . Prof. Dr. Bernhard Schink (Universität Konstanz, Deutschland), für seine spontane und engagierte Übernahme der Betreuung, . Prof. Dr. Andrew W. B. Johnston (University of East Anglia, UK), für seine herzliche und bereitwillige Aufnahme in seiner Arbeitsgruppe, seiner engagierten Unter- stützung, sowie für die Übernahme des Koreferates, . Prof. Dr. Frithjof C. Küpper (University of Aberdeen, UK), für seine große Hilfsbereitschaft bei der vorliegenden Arbeit und geplanter Manuskripte, als auch für die mentale Unterstützung während der letzten Jahre! Desweiteren möchte ich herzlichst Dr. David Schleheck für die Übernahme des Koreferates der mündlichen Prüfung sowie Prof. Dr. Alexander Bürkle, für die Übernahme des Prüfungsvorsitzes sowie für seine vielen hilfreichen Ratschläge danken! Ein herzliches Dankeschön geht an alle beteiligten Arbeitsgruppen der Universität Konstanz, der UEA und des SAMS, ganz besonders möchte ich dabei folgenden Personen danken: . Dr. David Schleheck und Karin Denger, für die kritische Durchsicht dieser Arbeit, der durch und durch sehr engagierten Hilfsbereitschaft bei Problemen, den zahlreichen wissenschaftlichen Diskussionen und für die aufbauenden Worte, . -
The Rnase H-Like Superfamily: New Members, Comparative Structural Analysis and Evolutionary Classification Karolina A
4160–4179 Nucleic Acids Research, 2014, Vol. 42, No. 7 Published online 23 January 2014 doi:10.1093/nar/gkt1414 The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification Karolina A. Majorek1,2,3,y, Stanislaw Dunin-Horkawicz1,y, Kamil Steczkiewicz4, Anna Muszewska4,5, Marcin Nowotny6, Krzysztof Ginalski4 and Janusz M. Bujnicki1,3,* 1Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, ul. Ks. Trojdena 4, PL-02-109 Warsaw, Poland, 2Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA USA-22908, USA, 3Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Umultowska 89, PL-61-614 Poznan, Poland, 4Laboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Zwirki i Wigury 93, PL-02-089 Warsaw, Poland, 5Institute of Biochemistry and Biophysics PAS, Pawinskiego 5A, PL-02-106 Warsaw, Poland and 6Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, ul. Ks. Trojdena 4, PL-02-109 Warsaw, Poland Received September 23, 2013; Revised December 12, 2013; Accepted December 26, 2013 ABSTRACT revealed a correlation between the orientation of Ribonuclease H-like (RNHL) superfamily, also called the C-terminal helix with the exonuclease/endo- the retroviral integrase superfamily, groups together nuclease function and the architecture of the numerous enzymes involved in nucleic acid metab- active site. Our analysis provides a comprehensive olism and implicated in many biological processes, picture of sequence-structure-function relation- including replication, homologous recombination, ships in the RNHL superfamily that may guide func- DNA repair, transposition and RNA interference. -
Bacterial Oxidases of the Cytochrome Bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets
Published in "Antioxidants & Redox Signaling doi: 10.1089/ars.2020.8039, 2020" which should be cited to refer to this work. Bacterial Oxidases of the Cytochrome bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets Vitaliy B. Borisov,1 Sergey A. Siletsky,1 Alessandro Paiardini,2 David Hoogewijs,3 Elena Forte,2 Alessandro Giuffre`,4 and Robert K. Poole5 Abstract Significance: Cytochrome bd is a ubiquinol:oxygen oxidoreductase of many prokaryotic respiratory chains with a unique structure and functional characteristics. Its primary role is to couple the reduction of molecular oxygen, even at submicromolar concentrations, to water with the generation of a proton motive force used for adenosine triphosphate production. Cytochrome bd is found in many bacterial pathogens and, surprisingly, in bacteria for- mally denoted as anaerobes. It endows bacteria with resistance to various stressors and is a potential drug target. Recent Advances: We summarize recent advances in the biochemistry, structure, and physiological functions of cytochrome bd in the light of exciting new three-dimensional structures of the oxidase. The newly discovered roles of cytochrome bd in contributing to bacterial protection against hydrogen peroxide, nitric oxide, perox- ynitrite, and hydrogen sulfide are assessed. Critical Issues: Fundamental questions remain regarding the precise delineation of electron flow within this multihaem oxidase and how the extraordinarily high affinity for oxygen is accomplished, while endowing bacteria with resistance to other small ligands. Future Directions: It is clear that cytochrome bd is unique in its ability to confer resistance to toxic small molecules, a property that is significant for understanding the propensity of pathogens to possess this oxidase. -
Multi-Omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities
Washington University in St. Louis Washington University Open Scholarship Arts & Sciences Electronic Theses and Dissertations Arts & Sciences Summer 8-15-2019 Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities Tayte Paul Campbell Washington University in St. Louis Follow this and additional works at: https://openscholarship.wustl.edu/art_sci_etds Part of the Bioinformatics Commons, Biology Commons, and the Microbiology Commons Recommended Citation Campbell, Tayte Paul, "Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities" (2019). Arts & Sciences Electronic Theses and Dissertations. 1888. https://openscholarship.wustl.edu/art_sci_etds/1888 This Dissertation is brought to you for free and open access by the Arts & Sciences at Washington University Open Scholarship. It has been accepted for inclusion in Arts & Sciences Electronic Theses and Dissertations by an authorized administrator of Washington University Open Scholarship. For more information, please contact [email protected]. WASHINGTON UNIVERSITY IN ST. LOUIS Division of Biology and Biomedical Sciences Plant and Microbial Biosciences Dissertation Examination Committee: Gautam Dantas, Chair Arpita Bose Andrew Kau Audrey Odom-John Himadri Pakrasi Fuzhong Zhang Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities by Tayte P. Campbell A dissertation presented to The Graduate School of Washington University in partial fulfillment -
Yeast Genome Gazetteer P35-65
gazetteer Metabolism 35 tRNA modification mitochondrial transport amino-acid metabolism other tRNA-transcription activities vesicular transport (Golgi network, etc.) nitrogen and sulphur metabolism mRNA synthesis peroxisomal transport nucleotide metabolism mRNA processing (splicing) vacuolar transport phosphate metabolism mRNA processing (5’-end, 3’-end processing extracellular transport carbohydrate metabolism and mRNA degradation) cellular import lipid, fatty-acid and sterol metabolism other mRNA-transcription activities other intracellular-transport activities biosynthesis of vitamins, cofactors and RNA transport prosthetic groups other transcription activities Cellular organization and biogenesis 54 ionic homeostasis organization and biogenesis of cell wall and Protein synthesis 48 plasma membrane Energy 40 ribosomal proteins organization and biogenesis of glycolysis translation (initiation,elongation and cytoskeleton gluconeogenesis termination) organization and biogenesis of endoplasmic pentose-phosphate pathway translational control reticulum and Golgi tricarboxylic-acid pathway tRNA synthetases organization and biogenesis of chromosome respiration other protein-synthesis activities structure fermentation mitochondrial organization and biogenesis metabolism of energy reserves (glycogen Protein destination 49 peroxisomal organization and biogenesis and trehalose) protein folding and stabilization endosomal organization and biogenesis other energy-generation activities protein targeting, sorting and translocation vacuolar and lysosomal -
In-Vitro Synthesis and Reconstitution of Cytochrome Bo3 Ubiquinol Oxidase in Artificial Membranes
In-vitro Synthesis and Reconstitution of Cytochrome bo3 Ubiquinol Oxidase in Artificial Membranes Dissertation Zur Erlangung des Grades Doktor der Naturwissenschaften Am Fachbereich Biologie Der Johannes Gutenberg-Universität Mainz Ahu ARSLAN YILDIZ geboren am 20.12.1980 in Turkey Mainz, 2010 Dekan: Prof. Dr. Erwin Schmidt 1. Berichterstatter: Prof. Dr. Eva K. Sinner 2. Berichterstatter: Prof. Dr. Harald Paulsen 3. Prüfer: Prof. Dr. Wolfgang Knoll 4. Prüfer: Prof. Dr. Elmar Jaenicke Tag der mündlichen Prüfung: 29.01.2010 Abbreviations ATP Adenosine triphosphate PD Parkinson’s Disease Cyt-bo3 Cytochrome bo3 ubiquinol oxidase NADH Nicotinamide adenine dinucleotide UQ Ubiquinone UQH2 Ubiquinol Cyt-c Cytochrome c E.coli Escherichia coli Heme Heme or Haem molecule Cyt-bd Cytochrome bd ubiquinol oxidase cyo Cytochrome encoding operon CuA Copper site in subunit II CuB Copper of binuclear site CFPS Cell-free protein synthesis tRNA Transfer RNA GTP Guanidine triphosphate BLMs Black lipid membranes sBLM Supported bilayer lipid membrane tBLM Tethered lipid bilayer membrane SPR Surface Plasmon Resonance Spectroscopy SPFS Surface Plasmon Enhanced Fluorescence Spectroscopy θc Critical angle θm Minimum angle TIR Total internal reflection εd Dielectric constant n Refractive index CA Contact angle pJRHisA Subunit II histidine tagged enzyme with natural promoter pRCO3 Fused subunit II-I-III enzyme with natural promoter pETcyo Subunit II histidine tagged enzyme with T7 promoter LB Luria Bertani media ii KOH Potassium hydroxide PES Polyethylene sulfonate -
K319-100 Gluconokinase Activity Assay Kit (Colorimetric)
FOR RESEARCH USE ONLY! Gluconokinase Activity Assay Kit (Colorimetric) 7/16 (Catalog # K319-100; 100 assays; Store at -20°C) I. Introduction: Gluconokinase (ATP:D-gluconate 6-phosphotransferase or Gluconate Kinase; EC:2.7.1.12) is a key enzyme for Gluconate degradation pathway. In E. coli and yeast, Gluconokinase can convert gluconate into 6-Phosphate-D-Gluconate in an ATP dependent manner. Through Hexose Monophosphate Shunt (HMS) pathway, 6-Phosphate-D-Gluconate generates ribose-6-phosphate, which is critical for nucleotides and nucleic acid synthesis. Little is known of the mechanism of gluconate metabolism in humans despite its widespread use in medicine and consumer products. BioVision’s Gluconokinase Assay kit provides a quick and easy way for monitoring Gluconokinase activity in a variety of samples. In this kit, Gluconokinase converts Gluconate into 6-Phosphate-D-Gluconate in an ATP dependent manner. 6-Phosphate-D-Gluconate and ADP in turn undergoe a series of reactions to form an intermediate, which reacts with the probe to form a colored product with strong absorbance (OD 450 nm). The assay is simple, sensitive, and high-throughput adaptable. Detection limit: < 0.1mU. Gluconokinase D-Gluconate + ATP 6-Phosphate-D-Gluconate + ADP Intermediate + Probe Color Product (OD 450 nm) II. Application: Measurement of Gluconokinase activity in various samples Mechanistic study of Pentose Phosphate Pathway III. Sample Type: Prokaryote such as: E.coli Animal tissues such as liver, kidney, etc. Adherent or suspension cells. IV. Kit Contents: Components K319-100 Cap Code Part Number Gluconokinase Assay Buffer 25 ml WM K319-100-1 Gluconokinase Substrate 1 Vial Blue K319-100-2 ATP 1 Vial Orange K319-100-3 Gluconokinase Converting Enzyme 1 Vial Purple K319-100-4 Gluconokinase Developer 1 Vial Green K319-100-5 Gluconokinase Probe 1 Vial Red K319-100-6 NADH Standard 1 Vial Yellow K319-100-7 Gluconokinase Positive Control 1 Vial Brown K319-100-8 V. -
Supplementary Materials
Supplementary Materials COMPARATIVE ANALYSIS OF THE TRANSCRIPTOME, PROTEOME AND miRNA PROFILE OF KUPFFER CELLS AND MONOCYTES Andrey Elchaninov1,3*, Anastasiya Lokhonina1,3, Maria Nikitina2, Polina Vishnyakova1,3, Andrey Makarov1, Irina Arutyunyan1, Anastasiya Poltavets1, Evgeniya Kananykhina2, Sergey Kovalchuk4, Evgeny Karpulevich5,6, Galina Bolshakova2, Gennady Sukhikh1, Timur Fatkhudinov2,3 1 Laboratory of Regenerative Medicine, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of Ministry of Healthcare of Russian Federation, Moscow, Russia 2 Laboratory of Growth and Development, Scientific Research Institute of Human Morphology, Moscow, Russia 3 Histology Department, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia 4 Laboratory of Bioinformatic methods for Combinatorial Chemistry and Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia 5 Information Systems Department, Ivannikov Institute for System Programming of the Russian Academy of Sciences, Moscow, Russia 6 Genome Engineering Laboratory, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia Figure S1. Flow cytometry analysis of unsorted blood sample. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S2. Flow cytometry analysis of unsorted liver stromal cells. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S3. MiRNAs expression analysis in monocytes and Kupffer cells. Full-length of heatmaps are presented. -
(51) International Patent Classification: A61K 8/66 (2006.01) A61Q 11/00
( (51) International Patent Classification: A61K 8/66 (2006.01) A61Q 11/00 (2006.01) (21) International Application Number: PCT/EP20 19/08 1186 (22) International Filing Date: 13 November 2019 (13. 11.2019) (25) Filing Language: English (26) Publication Language: English (30) Priority Data: 18206133.3 14 November 2018 (14. 11.2018) EP (71) Applicant: NOVOZYMES A/S [DK/DK]; Krogshoejvej 36, 2880 Bagsvaerd (DK). (72) Inventors: DURHUUS, Thomas, Thomasen; Krogshoe¬ jvej 36, 2880 Bagsvaerd (DK). PALMEN, Lorena, Gonzalez,; Krogshoejvej 36, 2880 Bagsvaerd (DK). REISER, Anna, Verena,; Krogshoejvej 36, 2880 Bagsvaerd (DK). STREICHER, Werner, W,; Krogshoe¬ jvej 36, 2880 Bagsvaerd (DK). (81) Designated States (unless otherwise indicated, for every kind of national protection available) : AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (84) Designated States (unless otherwise indicated, for every kind of regional protection available) : ARIPO (BW, GH, GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TR), OAPI (BF, BJ, CF, CG, Cl, CM, GA, GN, GQ, GW, KM, ML, MR, NE, SN, TD, TG).