The Relevance of Transhydrogenases and Heterologous Phosphagen Kinases for Microbial Cofactor Metabolism

Total Page:16

File Type:pdf, Size:1020Kb

The Relevance of Transhydrogenases and Heterologous Phosphagen Kinases for Microbial Cofactor Metabolism Research Collection Doctoral Thesis The relevance of transhydrogenases and heterologous phosphagen kinases for microbial cofactor metabolism Author(s): Canonaco, Fabrizio Publication Date: 2003 Permanent Link: https://doi.org/10.3929/ethz-a-004525971 Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library DISS. ETH.Nr. 15040 The relevance of transhydrogenases and heterologous phosphagen kinases for microbial cofactor metabolism A dissertation submitted to the SWISS FEDERAL INSTITUTE OF TECHNOLOGY ZURICH for the degree of Doctor of Natural Science Presented by Fabrizio Canonaco Dipl. Natw. ETH born April 22nd, 1975 in Locarno, Switzerland Accepted on the recommendation of PD Dr. U. Sauer Prof. T. Wallimann PD Dr. U. Schlattner Prof. H. Hennecke 2003 Seite Leer Blank 2 ACKNOWLEDGEMENTS and further back to the When I think back to the time point where I began my PhD, in a how one recalls as have being important years of the study, it is surprising many people I owe a it is not to name them all, but to some people way or another. In this section, possible PhD. tribute, because without them I would not have succeeded in finishing my and it could not have been else. They The first big 'thank you' goes to my family, to without me in I did not want do, always played a central role in my life, pushing anything their sacrifices and their encouragements I but supporting me in everything I chose. Without would not have been writing these pages. for the sincere they offered mc To other people I owe my deepest gratitude, friendship for the stories behind the in the difficult moments I encountered. There is no place here to me alive' in the last years, and essential contribution every one of them gave 'keeping these nicknames, in neither I would be able to put them in words, so I simply list people by as casual order. Jonne, Maud, Droopy, Pimpa, Zambo, Sonda, Claudia, Mitch, your loyalty friends will never be forgotten. in Uwe Sauer. In his My scientific and professional career had a very competent mentor later as a PhD a student five and I continued group I began my scientific career as years ago, and to blame when are going bad student. As group leader, it would be easy people things Uwe had words of encouragement when congratulate them as they succeed, but always critics as small successes made motivation was low. He also had precise and appropriated my For his of 'the boss' and the me blind towards new upcoming problems. original way being I owe him contribution to my scientific maturation my deepest gratitude. kinases was conducted in collaboration The part of the project involving phosphagen the Cell Institute of the ETH Zürich. I'm with the group of Theo Wallimann, at Biology also co-referees for this deeply thankful to Uwe Schlattner and Theo Wallimann, which are had. I also thank work, for their intriguing suggestions and the stimulating discussions we in the examination of this Prof. Hauke Hennecke for having accepted the role of co-referee doctoral thesis. 3 the contribution of students I had Parts of the results presented here were achieved with Pascal Baillod and Lorena the opportunity to train. I hope I could have helped Sylvia Heri, Jaramillo, the way they helped me. is not I therefore will miss and No job results in success if the work atmosphere optimal. collaborative attitude of the Sauer Group people, where I always never forget the friendly and and Last to Marco, Eliane, Ursi, Lars, Jörg. felt part of a team. Special thanks Peter, Nicola, I the at the Institute of which had but not least, thanks to all the other people Biotechnology opportunity to know and work with. 4 TABLE OF CONTENTS 7 SUMMARY/ SOMMARIO 11 CHAPTER 1 General introduction isomerase 55 CHAPTER 2 Metabolic flux response to phosphoglucose knock-out in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA 69 CHAPTER 3 Dissecting the role of soluble and membrane-bound transhydrogenases UdhA and PntAB in Escherichia coli 95 CHAPTER 4 Functional expression of phosphagen kinase systems confers resistance to transient stresses in Saccharomyces cerevisiae by buffering the ATP pool 119 CHAPTER 5 Functional expression of arginine kinase improves recovery from pH stress of Escherichia coli 133 CONCLUSIONS AND OUTLOOK 135 ABBREVIATIONS LIST 139 CURRICULUM VITAE 5 Seite Leer / Blank leaf 6 "Obstacles are thosefrightful things you see when you take your eyes offyour goal" Henry Ford SUMMARY NADPH and how The scientific topic of this thesis is how micro-organisms generate that transient protection during they can be equipped with ATP buffering systems provide nucleotides are essential cofactors for cellular metabolism, energy stress. ATP and pyridine utilized for linking catabolism to anabolism. While NADH is almost exclusively energy reactions. generation, NADPH provides reducing power for biosynthetic construction and metabolic flux In Chapter 2 and Chapter 3, we show through mutant have distinct roles in NADPH analysis that the two transhydrogenases of Escherichia coli is an source of metabolism. The membrane-bound transhydrogenase PntAB important the of NAPDH during exponential growth on glucose by catalyzing transhydrogenation in the reverse NADH to NADPH. The soluble transhydrogenase UdhA, contrast, catalyzes on but reaction from NAPDH to NADH. This function is not necessary during growth glucose of which a of critical on substrates such as acetate, the catabolism generates higher proportion NADPH. constitute and Vertebrates contain so-called phosphagen kinase systems, which spatial demand. In to overcome of fluctuating energy temporal energy buffering systems periods kinase in Saccharomcyes cerevisiae that Chapter 4 we install such phosphagen systems show the functional of arginine normally does not contain such systems. We then expression kinase Environmental conditions of fluctuating kinase, one particular phosphagen system. S. cerevisiae in chemostat culture energy demand are installed by growing glucose-limited intracellular ATP level was with interrupted feeding. In the absence of glucose feeding, the in but it was stabilized at a much higher level shown to drop significantly in the control strain, that buffering the arginine kinase-expressing strain. Our results demonstrate temporal energy kinases that can be transferred to phylogenetically very is an intrinsic property of phosphagen distant organism. 7 of kinase in the The 5th chapter affords then a short study on the expression arginine that kinase significantly bacterium E. coli. Specifically, we could show arginine expression other that was to exert among improves the recovery after a transient pH stress, anticipated effects and ATP stress. 8 che si "GH ostacoli sono quelle cose spaventose scorgono quando si perde di vista il proprio obiettivo" Henry Ford SOMMARIO l'NADPH nei L'argomento scientifico di questa tesi è come venga generato in con sistemi per FATP microorganismi e come questi possano venire equipaggiati tampone lo stress L'ATP e i nucleotidi a grado di fornire una protezione transitoria durante energetico. metabolismo cellulare e l'anabolismo al piridina sono cofattori essenziali del collegano di catabolismo. Mentre l'NADH è utilizzato quasi esclusivamente per la produzione energia, biosintetiche. l'NADPH fornisce potere riduttivo per le reazioni tramite la costruzione di mutanti e l'analisi Nel Capitolo 2 e nel Capitolo 3 mostriamo coli hanno ruoli dei flussi metabolici che le due transidrogenasi del batterio Escherichia membranare PntAB è un distinti nel metabolismo dell'NADPH. La transidrogenasi catalizzando la importante sorgente di NADPH durante la crescita esponenziale su glucosio, necessaria durante la transidrogenazione dell'NADH in NADPH. Questa funzione non è una in corne il cui catabolismo genera crescita su glucosio, ma è critica su substrati l'acetato, proporzione più NADPH. che costituisce un I vertebrati contengono il cosddetto sistema di fosfagene chinasi, momenti di fluttuazione energetica. Nel sistema tampone spaziale e temporale per affrontare chinasi nel lievito Saccharomyces Capitolo 4, installiamo un taie sistema di fosfagene mostriamo funzionale délia cerevisiae che ne è normalmente privo. In seguito l'espressione délia délie chinasi. Condizioni arginina chinasi, un particolare membro famiglia fosfagene crescendo S. ambientali che causano fluttuazioni nella domanda di energia vengono generate con alimentazione discontinua. In cerevisiae in un medium di coltura limitato in glucosio il livello intracellulare di ATP diminuisce in assenza di una alimentazione di glucosio, ma risulta stabilizzato e mantiene un livello più maniera significativa nel ceppo di controllo, chinasi. I nostri risultati dimostrano quindi corne alto nel ceppo in grado di esprimere arginina intrinseca délie chinasi la funzione di tampone temporale sia una proprietà fosfagene trasferibile ad organismi fîlogeneticamente molto distanti. 9 chinasi nel batterio Il 5° capitolo affronta un brève studio suU'espressione dell'arginina chinasi migliori in E. coli. Nello specifico, mostriamo come l'espressione dell'arginina transiente da conosciuto per generare tra maniera significativa il recupero da uno stress pH, gli altri effetti uno stress da ATP. 10 CHAPTER 1 General introduction 11 NADH TWO FACTORS LINK CATABOLISM TO ANABOLISM: ATP AND need to survive In principle, all living organisms have two goals. Firstly,
Recommended publications
  • MITOCHONDRIAL CREATINE KINASE Some Clinical, Biochemical and Morphological Aspects
    PDF hosted at the Radboud Repository of the Radboud University Nijmegen The following full text is a publisher's version. For additional information about this publication click this link. http://hdl.handle.net/2066/114105 Please be advised that this information was generated on 2021-10-11 and may be subject to change. MITOCHONDRIAL CREATINE KINASE some clinical, biochemical and morphological aspects Jan A.M. Smeitink MITOCHONDRIAL CREATINE KINASE some clinical, biochemical and morphological aspects Jan A.M. Smeitink MITOCHONDRIAL CREATINE KINASE SOME CLINICAL, BIOCHEMICAL AND MORPHOLOGICAL ASPECTS EEN WETENSCHAPPELIJKE PROEVE OP HET GEBIED VAN DE MEDISCHE WETENSCHAPPEN, IN HET BIJZONDER DE GENEESKUNDE PROEFSCHRIFT TER VERKRIJGING VAN DE GRAAD VAN DOCTOR AAN DE KATHOLIEKE UNIVERSITEIT NIJMEGEN VOLGENS BESLUIT VAN HET COLLEGE VAN DECANEN IN HET OPENBAAR TE VERDEDIGEN OP DINSDAG 6 OKTOBER 1992, DES NAMIDDAGS TE 1.30 UUR PRECIES DOOR JOHANNES ALBERTUS MARIA SMEITINK GEBOREN OP 21 JUNI 1956 TE ARNHEM IV Promotores : Prof. Dr. R.C.A. Sengers Prof. Dr. J.M.F. Trijbels Co-Promotores : Dr. W. Ruitenbeek Dr. R.A. Wevers Aan mijn ouders AanWillemien en Mark CONTEN CHAPTER 1 Introduction and aim of the study CHAPTER 2 Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism Biochimica et Biophysica Acta (Reviews on Bioenergetics): in press I. Introduction II. Biochemical studies of Mi-CK ΠΙ. Functional studies of Mi-CK IV. Integration of Mi-CK in cellular energy metabolism V. Perspectives CHAPTER 3 A method for quantitative measurement
    [Show full text]
  • Lombricine Kinase Structure and Substrate Specificity: a Paradigm for Elucidation of Substrate Specificity in Phosphagen Kinases D
    Florida State University Libraries Electronic Theses, Treatises and Dissertations The Graduate School 2007 Lombricine Kinase Structure and Substrate Specificity: A Paradigm for Elucidation of Substrate Specificity in Phosphagen Kinases D. Jeffrey. Bush Follow this and additional works at the FSU Digital Library. For more information, please contact [email protected] THE FLORIDA STATE UNIVERSITY COLLEGE OF ARTS AND SCIENCES LOMBRICINE KINASE STRUCTURE AND SUBSTRATE SPECIFICITY: A PARADIGM FOR ELUCIDATION OF SUBSTRATE SPECIFICITY IN PHOSPHAGEN KINASES By D. JEFFREY BUSH A Dissertation submitted to the Department of Chemistry and Biochemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy Degree Awarded: Spring Semester, 2007 The members of the Committee approve the Dissertation of D. Jeffrey Bush defended on February 20, 2007. Michael S. Chapman Professor Co-Directing Dissertation John Dorsey Professor Co-Directing Dissertation W. Ross Ellington Outside Committee Member Michael Blaber Committee Member Approved: ____________________________________________ Joseph Schlenoff, Department Chair, Department of Chemistry & Biochemistry ____________________________________________ Joseph Travis, Dean, College of Arts & Sciences The Office of Graduate Studies has verified and approved the above named committee members. ii To the late Clifford M. Bush, who with statements such as “A heterogeneous compound of two or more substances whose ray through certain limits is confined to a specific area…” fostered a strong interest of the author in science at a very young age, if only just to know more about what he spoke. iii ACKNOWLEDGEMENTS I wish to first convey my sincere gratitude to my parents, Donald and Roberta for raising me in the nurture and admonition of the Almighty God.
    [Show full text]
  • Acidophilic Green Algal Genome Provides Insights Into Adaptation to an Acidic Environment
    Acidophilic green algal genome provides insights into adaptation to an acidic environment Shunsuke Hirookaa,b,1, Yuu Hirosec, Yu Kanesakib,d, Sumio Higuchie, Takayuki Fujiwaraa,b,f, Ryo Onumaa, Atsuko Eraa,b, Ryudo Ohbayashia, Akihiro Uzukaa,f, Hisayoshi Nozakig, Hirofumi Yoshikawab,h, and Shin-ya Miyagishimaa,b,f,1 aDepartment of Cell Genetics, National Institute of Genetics, Shizuoka 411-8540, Japan; bCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan; cDepartment of Environmental and Life Sciences, Toyohashi University of Technology, Aichi 441-8580, Japan; dNODAI Genome Research Center, Tokyo University of Agriculture, Tokyo 156-8502, Japan; eResearch Group for Aquatic Plants Restoration in Lake Nojiri, Nojiriko Museum, Nagano 389-1303, Japan; fDepartment of Genetics, Graduate University for Advanced Studies, Shizuoka 411-8540, Japan; gDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan; and hDepartment of Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan Edited by Krishna K. Niyogi, Howard Hughes Medical Institute, University of California, Berkeley, CA, and approved August 16, 2017 (received for review April 28, 2017) Some microalgae are adapted to extremely acidic environments in pumps that biotransform arsenic and archaeal ATPases, which which toxic metals are present at high levels. However, little is known probably contribute to the algal heat tolerance (8). In addition, the about how acidophilic algae evolved from their respective neutrophilic reduction in the number of genes encoding voltage-gated ion ancestors by adapting to particular acidic environments. To gain channels and the expansion of chloride channel and chloride car- insights into this issue, we determined the draft genome sequence rier/channel families in the genome has probably contributed to the of the acidophilic green alga Chlamydomonas eustigma and per- algal acid tolerance (8).
    [Show full text]
  • Natural Products Containing 'Rare'
    molecules Review Natural Products Containing ‘Rare’ Organophosphorus Functional Groups Janusz J. Petkowski 1,* , William Bains 2 and Sara Seager 1,3,4 1 Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA; [email protected] 2 Rufus Scientific, 37 The Moor, Melbourn, Royston, Herts SG8 6ED, UK; [email protected] 3 Department of Physics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA 4 Department of Aeronautics and Astronautics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA * Correspondence: [email protected] Received: 21 January 2019; Accepted: 22 February 2019; Published: 28 February 2019 Abstract: Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P–N (phosphoramidate), P–S (phosphorothioate), and P–C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life. In this review we thoroughly categorize P–N, P–S, and P–C natural organophosphorus compounds. Information on biological source, biological activity, and biosynthesis is included, if known. This review also summarizes the role of phosphorylation on unusual amino acids in proteins (N- and S-phosphorylation) and reviews the natural phosphorothioate (P–S) and phosphoramidate (P–N) modifications of DNA and nucleotides with an emphasis on their role in the metabolism of the cell. We challenge the commonly held notion that nonphosphate organophosphorus functional groups are an oddity of biochemistry, with no central role in the metabolism of the cell.
    [Show full text]
  • Natural Products Containing 'Rare'
    Natural Products Containing ‘Rare’ Organophosphorus Functional Groups The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Petkowski, Janusz, et al. “Natural Products Containing ‘Rare’ Organophosphorus Functional Groups.” Molecules, vol. 24, no. 5, Feb. 2019, p. 866. As Published http://dx.doi.org/10.3390/molecules24050866 Publisher Multidisciplinary Digital Publishing Institute Version Final published version Citable link http://hdl.handle.net/1721.1/120918 Terms of Use Creative Commons Attribution Detailed Terms https://creativecommons.org/licenses/by/4.0/ molecules Review Natural Products Containing ‘Rare’ Organophosphorus Functional Groups Janusz J. Petkowski 1,* , William Bains 2 and Sara Seager 1,3,4 1 Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA; [email protected] 2 Rufus Scientific, 37 The Moor, Melbourn, Royston, Herts SG8 6ED, UK; [email protected] 3 Department of Physics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA 4 Department of Aeronautics and Astronautics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA * Correspondence: [email protected] Received: 21 January 2019; Accepted: 22 February 2019; Published: 28 February 2019 Abstract: Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P–N (phosphoramidate), P–S (phosphorothioate), and P–C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life.
    [Show full text]
  • Acidophilic Green Algal Genome Provides Insights Into Adaptation To
    Acidophilic green algal genome provides insights into PNAS PLUS adaptation to an acidic environment Shunsuke Hirookaa,b,1, Yuu Hirosec, Yu Kanesakib,d, Sumio Higuchie, Takayuki Fujiwaraa,b,f, Ryo Onumaa, Atsuko Eraa,b, Ryudo Ohbayashia, Akihiro Uzukaa,f, Hisayoshi Nozakig, Hirofumi Yoshikawab,h, and Shin-ya Miyagishimaa,b,f,1 aDepartment of Cell Genetics, National Institute of Genetics, Shizuoka 411-8540, Japan; bCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan; cDepartment of Environmental and Life Sciences, Toyohashi University of Technology, Aichi 441-8580, Japan; dNODAI Genome Research Center, Tokyo University of Agriculture, Tokyo 156-8502, Japan; eResearch Group for Aquatic Plants Restoration in Lake Nojiri, Nojiriko Museum, Nagano 389-1303, Japan; fDepartment of Genetics, Graduate University for Advanced Studies, Shizuoka 411-8540, Japan; gDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan; and hDepartment of Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan Edited by Krishna K. Niyogi, Howard Hughes Medical Institute, University of California, Berkeley, CA, and approved August 16, 2017 (received for review April 28, 2017) Some microalgae are adapted to extremely acidic environments in pumps that biotransform arsenic and archaeal ATPases, which which toxic metals are present at high levels. However, little is known probably contribute to the algal heat tolerance (8). In addition, the about how acidophilic algae evolved from their respective neutrophilic reduction in the number of genes encoding voltage-gated ion ancestors by adapting to particular acidic environments. To gain channels and the expansion of chloride channel and chloride car- insights into this issue, we determined the draft genome sequence rier/channel families in the genome has probably contributed to the of the acidophilic green alga Chlamydomonas eustigma and per- algal acid tolerance (8).
    [Show full text]
  • Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles
    Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur Quetglas, Sarah Zorman, Martin Pelosse, Pierre dos Santos, Francois Boucher, Tuuli Käämbre, et al. To cite this version: Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur Quet- glas, et al.. Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling. Systems Biology of Metabolic and Sig- naling Networks, Springer, pp.261-320, 2014, 9783642385056. 10.1007/978-3-642-38505-6_11. hal- 01949810 HAL Id: hal-01949810 https://hal.univ-grenoble-alpes.fr/hal-01949810 Submitted on 26 Jun 2020 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. Chapter 11 Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur, Sarah Zorman, Martin Pelosse, Pierre Dos Santos, Franc¸ois Boucher, Tuuli Kaambre, and Rita Guzun V. Saks (*) Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia e-mail: [email protected] U.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • POLSKIE TOWARZYSTWO BIOCHEMICZNE Postępy Biochemii
    POLSKIE TOWARZYSTWO BIOCHEMICZNE Postępy Biochemii http://rcin.org.pl WSKAZÓWKI DLA AUTORÓW Kwartalnik „Postępy Biochemii” publikuje artykuły monograficzne omawiające wąskie tematy, oraz artykuły przeglądowe referujące szersze zagadnienia z biochemii i nauk pokrewnych. Artykuły pierwszego typu winny w sposób syntetyczny omawiać wybrany temat na podstawie możliwie pełnego piśmiennictwa z kilku ostatnich lat, a artykuły drugiego typu na podstawie piśmiennictwa z ostatnich dwu lat. Objętość takich artykułów nie powinna przekraczać 25 stron maszynopisu (nie licząc ilustracji i piśmiennictwa). Kwartalnik publikuje także artykuły typu minireviews, do 10 stron maszynopisu, z dziedziny zainteresowań autora, opracowane na podstawie najnow­ szego piśmiennictwa, wystarczającego dla zilustrowania problemu. Ponadto kwartalnik publikuje krótkie noty, do 5 stron maszynopisu, informujące o nowych, interesujących osiągnięciach biochemii i nauk pokrewnych, oraz noty przybliżające historię badań w zakresie różnych dziedzin biochemii. Przekazanie artykułu do Redakcji jest równoznaczne z oświadczeniem, że nadesłana praca nie była i nie będzie publikowana w innym czasopiśmie, jeżeli zostanie ogłoszona w „Postępach Biochemii”. Autorzy artykułu odpowiadają za prawidłowość i ścisłość podanych informacji. Autorów obowiązuje korekta autorska. Koszty zmian tekstu w korekcie (poza poprawieniem błędów drukarskich) ponoszą autorzy. Artykuły honoruje się według obowiązujących stawek. Autorzy otrzymują bezpłatnie 25 odbitek swego artykułu; zamówienia na dodatkowe odbitki (płatne) należy zgłosić pisemnie odsyłając pracę po korekcie autorskiej. Redakcja prosi autorów o przestrzeganie następujących wskazówek: Forma maszynopisu: maszynopis pracy i wszelkie załączniki należy nadsyłać w dwu egzem­ plarzach. Maszynopis powinien być napisany jednostronnie, z podwójną interlinią, z marginesem ok. 4 cm po lewej i ok. 1 cm po prawej stronie; nie może zawierać więcej niż 60 znaków w jednym wierszu nie więcej niż 30 wierszy na stronie zgodnie z Normą Polską.
    [Show full text]
  • 1787 Genome-Wide Identification and Characterization of Eukaryotic Protein Kinases Kanhu Charan Das1, Parismita Kalita1, Timir
    [Frontiers in Bioscience, Landmark, 25, 1787-1827, June 1, 2020] Genome-wide identification and characterization of eukaryotic protein kinases Kanhu Charan Das1, Parismita Kalita1, Timir Tripathi1 1Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Methods 3.1. F. gigantica gene sequence retrieval 3.2. Generation of hidden markov models (HMMs) 3.3. Classification and domain analysis of FgePKs 4. Results 4.1. Identification of kinase-like proteins in F. gigantica genome 4.2. Classification and domain analysis of FgePKs 4.2.1. Ser/Thr kinase group 4.2.1.1. cAMP-dependent protein kinase (AGC) group 4.2.1.1.1. Protein kinase C (PKC) 4.2.1.1.2. Protein kinase A (PKA) 4.2.1.2. Calmodulin kinase (CaMK) group 4.2.1.3. Cyclin-dependent kinase and other close relatives (CMGC) group 4.2.1.3.1. Cyclin dependent kinases (CDK) 4.2.1.3.2. Mitogen activated protein kinases (MAPK) 4.2.1.3.3. Glycogen synthase 3 kinases (GSK3) 4.2.1.3.4. Dual-specificity Tyr regulated kinases (DYRK) 4.2.1.4. Sterile Ser/Thr kinase (STE) group 4.2.1.5. Casein kinase 1 (CK1) group 4.2.2. Tyr kinase group 4.3.3. Hybrid group 4.3.3.1. Tyr kinase-like (TKL) group 4.3.3.2. Others 5. Discussion 6. Acknowledgments 7. References 1. ABSTRACT The tropical liver fluke, Fasciola gigantica is kinases (ePKs) are regulators of cellular a food-borne parasite responsible for the phosphorylation.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling
    Chapter 11 Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur, Sarah Zorman, Martin Pelosse, Pierre Dos Santos, Franc¸ois Boucher, Tuuli Kaambre, and Rita Guzun V. Saks (*) Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia e-mail: [email protected] U. Schlattner (*) • M. Tokarska-Schlattner • S. Zorman • M. Pelosse Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France e-mail: [email protected] T. Wallimann ETH Zu¨rich, Zu¨rich, Switzerland R. Bagur Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France TIMC-IMAG, Univ. Grenoble Alpes, Grenoble, France CNRS, UMR5525, Grenoble, France P.D. Santos Univ. Bordeaux, Bordeaux, France Centre de Recherche Cardiothoracique de Bordeaux, Inserm, U1045, Bordeaux, France LIRYC, L’Institut de rythmologie et mode´lisation cardiaque, Universite´ de Bordeaux, Bordeaux, France F. Boucher TIMC-IMAG, Univ. Grenoble Alpes, Grenoble, France CNRS, UMR5525, Grenoble, France M.A. Aon et al. (eds.), Systems Biology of Metabolic and Signaling Networks, 261 Springer Series in Biophysics 16, DOI 10.1007/978-3-642-38505-6_11,
    [Show full text]