DOCSLIB.ORG

Mai Motomontant De Llu to Mo Na Mini

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

MAIMOTOMONTANT US009828618B2 DE LLU TO MO NA MINI (12 ) United States Patent ( 10 ) Patent No. : US 9 ,828 ,618 B2 Hidesaki et al. (45 ) Date of Patent: *Nov . 28 , 2017 (54 ) MICROORGANISM HAVING CARBON EP 2 738 247 Al 6 / 2014 DIOXIDE FIXATION CYCLE INTRODUCED TW 201311889 3 / 2013 THEREINTO WO WO - 2009 /046929 A2 4 / 2009 WO WO - 2009 /094485 A1 7 / 2009 WO WO - 2010 /071697 A1 6 / 2010 ( 71 ) Applicant: Mitsui Chemicals , Inc . , Tokyo ( JP ) WO WO - 2011 /099006 A2 8 / 2011 ( 72 ) Inventors: Tomonori Hidesaki, Singapore (SG ) ; WO WO 2013 /018734 A12 / 2013 Ryota Fujii, Chiba ( JP ); Yoshiko Matsumoto , Mobara ( JP ) ; Anjali OTHER PUBLICATIONS Madhavan , Singapore ( SG ) ; Su Sun Wendisch et al. , Current Opinion in Microbiology 2006, vol . 9 , p . Chong, Singapore ( SG ) 268 - 274 . * Chistoserdova et al. , Journal of Bacteriology , 1994 , vol. 176 , No . ( 73 ) Assignee : MITSUI CHEMICALS , INC . , Tokyo 23 , p . 7398 - 7404. * ( JP ) Schneider et al. , The Journal of Biological Chemistry , 2012 , vol . 287 , No. 1 , p . 757 - 766 Only . * ( * ) Notice : Subject to any disclaimer , the term of this Office Action issued in Chinese Patent Application No . patent is extended or adjusted under 35 201480002416 . 5 dated Jun . 23 , 2016 . U . S .C . 154 (b ) by 0 days . Erb et al. , “ The Apparent Malate Synthase Activity of Rhodobacter sphaeroides is Due to Two Paralogous Enzymes , (3S ) -Malyl - Co This patent is subject to a terminal dis enzyme A (COA ) B -Methylmalyl - CoA Lyase and (3S ) -Malyl -CoA claimer . Thioesterase ” , J . Bacteriol, Sep . 2009 , pp . 1249 - 1258 , vol. 192 , No . (21 ) Appl. No. : 14 /428 , 928 Yim et al. , “ Metabolic engineering of Escherichia coli for direct production of 1 , 4 -butanediol ,” Nature Chemical Biology , vol. 7 , ( 22 ) PCT Filed : Jan . 23, 2014 Jul. 2011, pp . 445 -452 . Atomi, Haruyuki, “ Review Microbial Enzymes Involved in Carbon ( 86 ) PCT No. : PCT / JP2014 / 051402 Dioxide Fixation, ” Journal of Bioscience and Bioengineering , vol. $ 371 ( c ) ( 1 ) , 94 , No . 6 , 2002 , pp . 497 - 505 . ( 2 ) Date : Mar. 17, 2015 Berg , Ivan A . , “Minireview Ecological Aspects of the Distribution of Different Autotrophic CO2 Fixation Pathways, ” Applied and (87 ) PCT Pub . No .: WO2014 / 115815 Environmental Microbiology , vol. 77 , No . 6 , Mar. 2011, pp . 1925 1936 . PCT Pub . Date : Jul. 31, 2014 Atsumi et al ., Non -fermentative pathways for synthesis of branched - chain higher alcohols as biofuels , Nature vol . 451 ( 3 ) Jan . (65 ) Prior Publication Data 2008, pp . 86 - 89 . US 2015 /0232903 A1 Aug. 20 , 2015 International Search Report dated Apr . 8 , 2014 issued in Application No. PCT/ JP2014 /051402 . ( 30 ) Foreign Application Priority Data ( Continued ) Jan . 24 , 2013 ( JP ) .. .. .. .. .. .. .. .. 2013 -011536 Jan . 24 , 2013 ( JP ) . .. .. .. .. 2013 - 011538 Primary Examiner — Kade Ariani (51 ) Int. CI. ( 74 ) Attorney , Agent, or Firm — Foley & Lardner LLP C12P 19 /32 ( 2006 .01 ) C12P 7 / 04 ( 2006 .01 ) ABSTRACT C12P 7 / 28 ( 2006 .01 ) (57 ) C12P 13 / 14 ( 2006 .01 ) An acetyl -CoA producing microorganism obtained by C12P 7748 ( 2006 .01 ) imparting at least one enzymatic activity selected from the C12P 7 /46 ( 2006 . 01 ) group consisting of malate thiokinase , malyl- CoA lyase , C12P 7 /62 ( 2006 . 01) glyoxylate carboligase , 2 -hydroxy - 3 - oxopropionate reduc (52 ) U . S . CI. tase , and hydroxypyruvate reductase , to a microorganism CPC .. ... C12P 19 /32 (2013 .01 ) ; C12P 7 / 04 that does not have any of the following (a ), ( b ), ( c ) , ( d ) or ( 2013 .01 ) ; C12P 7 /28 ( 2013 . 01 ) ; C12P 7 /46 ( C ): ( a ) a carbon dioxide fixation cycle including an enzy (2013 .01 ) ; C12P 7748 ( 2013 .01 ) ; C12P 77625 matic reaction from malonyl- CoA to malonate semialdehyde (2013 . 01 ) ; C12P 13 / 14 ( 2013 . 01 ) or 3 - hydroxypropionate ; (b ) a carbon dioxide fixation cycle ( 58 ) Field of Classification Search including an enzymatic reaction from acetyl - CoA and CO2 None to pyruvate ; ( c ) a carbon dioxide fixation cycle including an See application file for complete search history. enzymatic reaction from crotonyl - CoA and Co , to ethylma lonyl- CoA or glutaconyl -CoA ; ( d ) a carbon dioxide fixation (56 ) References Cited cycle including an enzymatic reaction from CO2 to formate ; or ( e ) at least one selected from the group consisting of FOREIGN PATENT DOCUMENTS malate thiokinase and malyl -CoA lyase . DE 10 2007 047 206 AL 4 / 2009 DE 1020070 59 248 A1 6 /2009 10 Claims, 2 Drawing Sheets US 9 ,828 ,618 B2 Page 2 ( 56 ) References Cited OTHER PUBLICATIONS Notice of Submission of Opinion issued in Korean Patent Appli cation No . 10 - 2015 -7006510 dated Mar . 28, 2016 . Chatsurachai et al. , “ An in silico platform for the design of heterologous pathways in nonnative metabolite production ,” BMC Bioinformatics 13 :93 ( 2012 ) . Melzer et al. , “ Flux Design : In silico design of cell factories based on correlation of pathway fluxes to desired properties, ” BMC Systems Biology 3 : 120 ( 2009 ) . Extended European Search Report issued in European Patent Appli cation No . 14743436 . 9 dated Sep . 7 , 2016 . Office Action dated Mar. 15 , 2017 in corresponding Chinese Patent Application No . 201480002416 . 5 . Office Action issued in Taiwan patent application No . 103102745 dated Aug . 28 , 2017 . * cited by examiner U . S . Patent Nov. 28 , 2017 Sheet 1 of 2 US 9 ,828 ,618 B2 * * * * * * * * W * * W * * WWW om c * : WW * W * M WOW X W o M now W . Ww * M W X W X WWW on 2 wW K W noonn.ex:* mci *Wwwww ww 1000 Malyl-CoA hyi w OOOOXXOOXXOOOOSSSOOS 0 deincomemoltinSuccinate 2-Hydroxy3 w Glyoxylate Hydroxypyruvate w CO2eminoch frd,sdh cano w Oba 0tonexMe* oxopropionate WU* mik *w * OMMIGRANKENONCONCHAKOMAX CIXR ycdw white oano wwww #44 Acetyl-CoA w w o 0 Fumarate ?{} Glyceratewhether w w w :*X OxaloacetatemannensomMalate * ** NK#KKMKM* * * CO glxx * 1.FIG ** gark nnoono *DO306 W wwwwww * x o D * wwww o 200 xW Ond.209200 W MAW Acetyl-CoAproductioncycle ensta XX MOM SK x* Yeew'vols ?{“????1} ond UX*w * *om 70% w ,ppc w oncuts w o eno wd6 w ock VVXboxopok w n w 3-Phosphoglycerate w in 2-Phosphoglycerate w ? ? ? ? ? ? ? ? ??? ??? ??? ?? w * * wuuu ? ? ? ? ? ? ? ? ? ? o ACCOUKKO (glucose,etc.) pood wwwwwwww mePhosphoenolpyruvate TxRd Pyruvate Acetyl-CoA 200 Intendedproduct(IPA ,glutamicacid,etc.) * * * Carbonsourcematerial * wwwpuukautuuwwe * * www www mmmmmwwwwwwwwww U . S . Patent Nov. 28 , 2017 Sheet 2 of 2 US 9 ,828 ,618 B2 * * * * * * * * * * * * * * * * * * * * * * * * A DO C O M O Malyl-COA Glyoxylate Glycine (03) Hydroxypyruvate ppopo 93)( o pogoon (13) (3) Acetyl-CoA CO2 GOOOD HOMWAKIERONDHATRONIKKOKOHAMEDHONINGCHAWI ERACEEANCAK DOOLERO Glycerateoffre Glycinepathway OxaloacetatereserverenenbesoMalate(C3) (C3) Serine (53) " FIG.2 HONCERNASONONO O (h3) (€9) 99004 2-Phosphoglycerate (m3) N3 A 2 4 www * w 4 LR 4 - AR * w w K w w (glucose,etc.)Opony careajeansdousoydsoudwo w cocco como W om kkxxi Acetyl-CoA Pyruvate * Phosphoglycerate3-)etc,aciditaconic,acidcitric( O w 00 Intendedproduct w Carbonsourcematerial w ARAKARRAGAWARABARAW w +w #" ttab xHxa > * A * * * * * * #* US 9 , 828 ,618 B2 MICROORGANISM HAVING CARBON by formate dehydrogenase , CO dehydrogenase , etc . , and , DIOXIDE FIXATION CYCLE INTRODUCED ultimately converted into acetyl- CoA . The 3 -hydroxypropi THEREINTO onate cycle is found in Chloroflexus bacteria and the like , and comprises 13 enzymes. In the 3 -hydroxypropionate CROSS REFERENCE TO RELATED 5 cycle , CO2 is fixed by the action of acetyl- CoA (propionyl APPLICATIONS COA ) carboxylase , and acetyl- CoA is produced via malonyl COA and the like . The 4 -hydroxybutyrate cycle exists in This application is the National Phase of PCT/ JP2014 ) archaebacteria and the like . In the 4 -hydroxybutyrate cycle , 051402 , filed Jan . 23 , 2014 , which claims priority to Japa CO , is fixed by the actions of pyruvate synthase , acetyl -CoA nese Application No . 2013 -011536 , filed Jan . 24 , 2013 and 10 (propionyl -CoA ) carboxylase , and phosphoenolpyruvate Japanese Application No . 2013 -011538 , filed Jan . 24 , 2013 . carboxylase , whereby acetyl - CoA is produced via 4 -hy droxybutyryl CoA and the like . TECHNICAL FIELD Several approaches of producing a useful substance by introducing a carbon dioxide fixation pathway to a micro The present invention relates to a microorganism having 15 organism that produces a useful compound have been pro a carbon dioxide fixation cycle introduced thereinto and a posed . For example , International Publication Nos. WO method of producing a substance using the microorganism . 2009 /094485 and WO 2010 / 071697 disclose approaches for producing acetyl- CoA from CO2 by using a microorganism BACKGROUND ART to which a pathway similar to the Wood - Ljungdahl pathway 20 of acetic acid bacteria has been introduced . WO 2009/ Acetyl- CoA is one of significantly important intermedi- 046929 discloses an approach for producing lactic acid from ates in metabolic pathways of microorganisms. Various CO2 by using a microorganism to which hydrogenase and metabolites are produced via acetyl- CoA . Well -known tetrahydrofolate lyase have been introduced . WO 2011/ examples of such substances produced via acetyl- CoA 099006 proposes a cycle in which CO , is fixed via a carbon include amino acids such as L - glutamic acid , L - glutamine, 25 dioxide fixation reaction into acetyl- CoA or a malonyl- CoA L - proline, L -arginine , L - leucine , and L - isoleucine ; organic reduction reaction . German Patent Application Laid -
Recommended publications
  • Comparison of the Effects on Mrna and Mirna Stability Arian Aryani and Bernd Denecke*

    Comparison of the Effects on Mrna and Mirna Stability Arian Aryani and Bernd Denecke*

    Aryani and Denecke BMC Research Notes (2015) 8:164 DOI 10.1186/s13104-015-1114-z RESEARCH ARTICLE Open Access In vitro application of ribonucleases: comparison of the effects on mRNA and miRNA stability Arian Aryani and Bernd Denecke* Abstract Background: MicroRNA has become important in a wide range of research interests. Due to the increasing number of known microRNAs, these molecules are likely to be increasingly seen as a new class of biomarkers. This is driven by the fact that microRNAs are relatively stable when circulating in the plasma. Despite extensive analysis of mechanisms involved in microRNA processing, relatively little is known about the in vitro decay of microRNAs under defined conditions or about the relative stabilities of mRNAs and microRNAs. Methods: In this in vitro study, equal amounts of total RNA of identical RNA pools were treated with different ribonucleases under defined conditions. Degradation of total RNA was assessed using microfluidic analysis mainly based on ribosomal RNA. To evaluate the influence of the specific RNases on the different classes of RNA (ribosomal RNA, mRNA, miRNA) ribosomal RNA as well as a pattern of specific mRNAs and miRNAs was quantified using RT-qPCR assays. By comparison to the untreated control sample the ribonuclease-specific degradation grade depending on the RNA class was determined. Results: In the present in vitro study we have investigated the stabilities of mRNA and microRNA with respect to the influence of ribonucleases used in laboratory practice. Total RNA was treated with specific ribonucleases and the decay of different kinds of RNA was analysed by RT-qPCR and miniaturized gel electrophoresis.
  • Enzymes Handling/Processing

    Enzymes Handling/Processing

    Enzymes Handling/Processing 1 Identification of Petitioned Substance 2 3 This Technical Report addresses enzymes used in used in food processing (handling), which are 4 traditionally derived from various biological sources that include microorganisms (i.e., fungi and 5 bacteria), plants, and animals. Approximately 19 enzyme types are used in organic food processing, from 6 at least 72 different sources (e.g., strains of bacteria) (ETA, 2004). In this Technical Report, information is 7 provided about animal, microbial, and plant-derived enzymes generally, and more detailed information 8 is presented for at least one model enzyme in each group. 9 10 Enzymes Derived from Animal Sources: 11 Commonly used animal-derived enzymes include animal lipase, bovine liver catalase, egg white 12 lysozyme, pancreatin, pepsin, rennet, and trypsin. The model enzyme is rennet. Additional details are 13 also provided for egg white lysozyme. 14 15 Chemical Name: Trade Name: 16 Rennet (animal-derived) Rennet 17 18 Other Names: CAS Number: 19 Bovine rennet 9001-98-3 20 Rennin 25 21 Chymosin 26 Other Codes: 22 Prorennin 27 Enzyme Commission number: 3.4.23.4 23 Rennase 28 24 29 30 31 Chemical Name: CAS Number: 32 Peptidoglycan N-acetylmuramoylhydrolase 9001-63-2 33 34 Other Name: Other Codes: 35 Muramidase Enzyme Commission number: 3.2.1.17 36 37 Trade Name: 38 Egg white lysozyme 39 40 Enzymes Derived from Plant Sources: 41 Commonly used plant-derived enzymes include bromelain, papain, chinitase, plant-derived phytases, and 42 ficin. The model enzyme is bromelain.
  • Glycine Transaminase 1. Identification of The

    Glycine Transaminase 1. Identification of The

    SAFETY DATA SHEET glycine transaminase Not for Private Therapeutic Use! 1. Identification of the Substance/preparation and of the company/undertaking 1.1 Identification of the Product: glycine transaminase (EXWM-2880) 1.2 Manufacture/Supplier Identification: Creative Enzymes 45-1 Ramsey Road Shirley, NY 11967, USA Tel: 1-631-562-8517 1-516-512-3133 Fax: 1-631-938-8127 E-mail: [email protected] Website: www.creative-enzymes.com 1.3 Relevant identified uses of the substance or mixture and uses advised against Identified uses: For research use only, not for human or veterinary use. 1.4 Emergency telephone number Emergency Phone #: +1-800-424-9300 (CHEMTREC Within USA and Canada) +1-703-527-3887 (CHEMTREC Outside USA and Canada) 2. Hazards Identification Physical/chemical hazards :n/a Human health hazards: Not specific hazard 3. EC No. / CAS No. EC No.:EC 2.6.1.4 CAS No.: 9032-99-9 4. First Aid Measures 4.1 Inhalation: If inhaled, remove to fresh air. If not breathing, give artificial respiration. If breathing is difficult, give oxygen. Get medical attention. 4.2 Ingestion: Do NOT induce vomiting unless directed to do so by medical personnel. Never give anything by mouth to an Unconscious person. If large quantities of this material are swallowed, call a physician immediately. Loosentight clothing such as a collar, tie, belt or waistband. Ingestion: Do NOT induce vomiting unless directed to do so by medical personnel. Never give anything by mouth to an Unconscious person. If large quantities of this material are swallowed, call a physician immediately.
  • The Coffee Protective Effect on Catalase System in the Preneoplastic Induced Rat Liver

    The Coffee Protective Effect on Catalase System in the Preneoplastic Induced Rat Liver

    Hindawi Publishing Corporation Journal of Chemistry Volume 2016, Article ID 8570321, 9 pages http://dx.doi.org/10.1155/2016/8570321 Research Article The Coffee Protective Effect on Catalase System in the Preneoplastic Induced Rat Liver Cristiana Schmidt de Magalhães,1 Jéssica Emi Takarada,1 Nathália Costa Carvalho,1 Dayene do C. Carvalho,2 Felipe Lopes de Andrade,1 Eric Batista Ferreira,1 Pedro Orival Luccas,2 and Luciana Azevedo3 1 Exact Sciences Institute, Federal University of Alfenas, Rua Gabriel Monteiro da Silva 700, Centro, 37130-000 Alfenas, MG, Brazil 2Chemistry Institute, Federal University of Alfenas, Rua Gabriel Monteiro da Silva 700, Centro, 37130-000 Alfenas, MG, Brazil 3Nutrition Faculty, Federal University of Alfenas, Rua Gabriel Monteiro da Silva 700, Centro, 37130-000 Alfenas, MG, Brazil Correspondence should be addressed to Cristiana Schmidt de Magalhaes;˜ [email protected] Received 15 October 2015; Revised 2 March 2016; Accepted 28 March 2016 Academic Editor: Philippe Jeandet Copyright © 2016 Cristiana Schmidt de Magalhaes˜ et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. This study aimed to evaluate the effect of organic/conventional coffee in liver tissues in the cancer process, taking into account the level and activities of catalase. The experiments were carried out with 8 groups of rats during 12 weeks. They received two injections of ethylenediaminetetraacetic acid solution 1.5% (v/v) prepared in 0.9% NaCl or 1,2-dimethylhydrazine (DMH) subcutaneous dose −1 −1 of 40 mg⋅kg ⋅bw for 2 weeks.
  • Como As Enzimas Agem?

    Como As Enzimas Agem?

    O que são enzimas? Catalizadores biológicos - Aceleram reações químicas específicas sem a formação de produtos colaterais PRODUTO SUBSTRATO COMPLEXO SITIO ATIVO ENZIMA SUBSTRATO Características das enzimas 1 - Grande maioria das enzimas são proteínas (algumas moléculas de RNA tem atividade catalítica) 2 - Funcionam em soluções aquosas diluídas, em condições muito suaves de temperatura e pH (mM, pH neutro, 25 a 37oC) Pepsina estômago – pH 2 Enzimas de organismos hipertermófilos (crescem em ambientes quentes) atuam a 95oC 3 - Apresentam alto grau de especificidade por seus reagentes (substratos) Molécula que se liga ao sítio ativo Região da enzima e que vai sofrer onde ocorre a a ação da reação = sítio ativo enzima = substrato 4 - Peso molecular: varia de 12.000 à 1 milhão daltons (Da), são portanto muito grandes quando comparadas ao substrato. 5 - A atividade catalítica das Enzimas depende da integridade de sua conformação protéica nativa – local de atividade catalítica (sitio ativo) Sítio ativo e toda a molécula proporciona um ambiente adequado para ocorrer a reação química desejada sobre o substrato A atividade de algumas enzimas podem depender de outros componentes não proteicos Enzima ativa = Holoenzimas Parte protéica das enzimas + cofator Apoenzima ou apoproteína •Íon inorgânico •Molécula complexa (coenzima) Covalentemente ligados à apoenzima GRUPO PROSTÉTICO COFATORES Elemento com ação complementar ao sitio ativo as enzimas que auxiliam na formação de um ambiente ideal para ocorrer a reação química ou participam diretamente dela
  • Genome Mining Reveals the Genus Xanthomonas to Be A

    Genome Mining Reveals the Genus Xanthomonas to Be A

    Royer et al. BMC Genomics 2013, 14:658 http://www.biomedcentral.com/1471-2164/14/658 RESEARCH ARTICLE Open Access Genome mining reveals the genus Xanthomonas to be a promising reservoir for new bioactive non-ribosomally synthesized peptides Monique Royer1, Ralf Koebnik2, Mélanie Marguerettaz1, Valérie Barbe3, Guillaume P Robin2, Chrystelle Brin4, Sébastien Carrere5, Camila Gomez1, Manuela Hügelland6, Ginka H Völler6, Julie Noëll1, Isabelle Pieretti1, Saskia Rausch6, Valérie Verdier2, Stéphane Poussier7, Philippe Rott1, Roderich D Süssmuth6 and Stéphane Cociancich1* Abstract Background: Various bacteria can use non-ribosomal peptide synthesis (NRPS) to produce peptides or other small molecules. Conserved features within the NRPS machinery allow the type, and sometimes even the structure, of the synthesized polypeptide to be predicted. Thus, bacterial genome mining via in silico analyses of NRPS genes offers an attractive opportunity to uncover new bioactive non-ribosomally synthesized peptides. Xanthomonas is a large genus of Gram-negative bacteria that cause disease in hundreds of plant species. To date, the only known small molecule synthesized by NRPS in this genus is albicidin produced by Xanthomonas albilineans. This study aims to estimate the biosynthetic potential of Xanthomonas spp. by in silico analyses of NRPS genes with unknown function recently identified in the sequenced genomes of X. albilineans and related species of Xanthomonas. Results: We performed in silico analyses of NRPS genes present in all published genome sequences of Xanthomonas spp., as well as in unpublished draft genome sequences of Xanthomonas oryzae pv. oryzae strain BAI3 and Xanthomonas spp. strain XaS3. These two latter strains, together with X. albilineans strain GPE PC73 and X.
  • „Transformation Von Phospholipiden Durch Phospholipasen A1 Und

    „Transformation Von Phospholipiden Durch Phospholipasen A1 Und

    „Transformation von Phospholipiden durch Phospholipasen A1 und Phospholipasen D“ Kumulative Dissertation zur Erlangung des akademischen Grades doctor rerum naturalium (Dr. rer. nat.) vorgelegt der Naturwissenschaftlichen Fakultät I Biowissenschaften der Martin-Luther-Universität Halle-Wittenberg von Martin Dippe geboren am 3. August 1981 in Wernigerode (Harz) Gutachter: 1. Prof. Renate Ulbrich-Hofmann (Martin-Luther-Universität Halle-Wittenberg) 2. Prof. Ingo Heilmann (Martin-Luther-Universität Halle-Wittenberg) 3. Prof. Uwe T. Bornscheuer (Ernst-Moritz-Arndt-Universität Greifswald) Halle (Saale), den 08. Dezember 2011 Inhaltsverzeichnis Inhaltsverzeichnis Inhaltsverzeichnis .............................................................................................................. 1 Abkürzungsverzeichnis ..................................................................................................... 2 1 Einleitung und Zielstellung .......................................................................................... 3 2 Theoretischer Teil ....................................................................................................... 5 2.1. Phospholipide – Molekularer Bau, Verwendung und chemische Synthese .... 6 2.2. Phospholipase-vermittelte Modifizierung von Phospholipiden ....................... 8 2.3. PLD-Enzyme............................................................................................... 10 2.3.1. Funktion und Mechanismus ............................................................ 10 2.3.2. Kopfgruppenaustausch
  • Morelloflavone and Its Semisynthetic Derivatives As Potential Novel Inhibitors of Cysteine and Serine Proteases

    Morelloflavone and Its Semisynthetic Derivatives As Potential Novel Inhibitors of Cysteine and Serine Proteases

    See discussions, stats, and author profiles for this publication at: http://www.researchgate.net/publication/276087209 Morelloflavone and its semisynthetic derivatives as potential novel inhibitors of cysteine and serine proteases ARTICLE in JOURNAL OF MEDICINAL PLANT RESEARCH · APRIL 2015 Impact Factor: 0.88 · DOI: 10.5897/JMPR2014.5641 DOWNLOADS VIEWS 2 17 8 AUTHORS, INCLUDING: Ihosvany Camps Claudio Viegas-jr Universidade Federal de Alfenas Universidade Federal de Alfenas 35 PUBLICATIONS 128 CITATIONS 6 PUBLICATIONS 22 CITATIONS SEE PROFILE SEE PROFILE Available from: Ihosvany Camps Retrieved on: 08 September 2015 Vol. 9(13), pp. 426-434, 3 April, 2015 DOI: 10.5897/JMPR2014.5641 Article Number: A42115152263 ISSN 1996-0875 Journal of Medicinal Plants Research Copyright © 2015 Author(s) retain the copyright of this article http://www.academicjournals.org/JMPR Full Length Research Paper Morelloflavone and its semisynthetic derivatives as potential novel inhibitors of cysteine and serine proteases Vanessa Silva Gontijo1, Jaqueline Pereira Januário1, Wagner Alves de Souza Júdice2, Alyne Alexandrino Antunes2, Ingridy Ribeiro Cabral1, Diego Magno Assis3, Maria Aparecida Juliano3, Ihosvany Camps4, Marcos José Marques4, Claudio Viegas Junior1 and Marcelo Henrique dos Santos1* 1Department of Exact Science, Laboratory of Phytochemistry and Medicinal Chemistry, Federal University of Alfenas, MG, Brazil. 2Interdisciplinary Center of Biochemical Investigation, Mogi das Cruzes University, Mogi das Cruzes, SP, Brazil. 3Department of Biophysics, Federal University of São Paulo, SP, Brazil. 4Department of Biological Sciences, Laboratory of Molecular Biology, Federal University of Alfenas, MG, Brazil. Received 9 October, 2014; Accepted 11 March, 2015 This article reports the three biflavonoids isolated from the fruit pericarp of Garcinia brasiliensis Mart.
  • Immobilization of Trypsin for Peptide Synthesis and Hydrolysis Reactions

    Immobilization of Trypsin for Peptide Synthesis and Hydrolysis Reactions

    IMMOBILIZATION OF TRYPSIN FOR PEPTIDE SYNTHESIS AND HYDROLYSIS REACTIONS zur Erlangung des akademischen Grades eines DOKTORS DER INGENIEURWISSENSCHAFTEN (Dr.-Ing.) der Fakultät für Chemieingenieurwesen und Verfahrenstechnik des Karlsruher Instituts für Technologie (KIT) vorgelegte genehmigte DISSERTATION von Dipl. Biol. (t.o.) Julia Andre geb. Stolarow aus Odessa, Ukraine Referent: Prof. Dr. rer. nat. Christoph Syldatk Korreferent: Prof. Dr.-Ing. Rudolf Hausmann Tag der mündlichen Prüfung: 19. November 2015 Maybe I will be something that you would be good at Für meine Eltern Acknowledgements I wish to express my sincere thanks to people who continuously supported and guided me throughout my work. Prof. Dr. rer. nat. Christoph Syldatk for giving me the opportunity to conduct my research work at his group, his guidance and his enormous scientific knowledge giving me a great opportunity to learn. Prof. Dr.-Ing. Rudolf Hausmann for his supervision, productive scientific discussions, his motivating personality and professional advice helping me to overcome many obstacles in my research work. Former and current members of the Technical Biology group for the great friendly and supporting atmosphere during my work and spare time: Dr.-Ing. Ines Schulze, Dr. rer. nat. Mareike Perzborn, Laura Krämer, Dr.-Ing. Berna Gerçe, Dr.-Ing. Martin Pöhnlein, Dipl.-Ing. Melanie Gerlitzki, Dipl.-Biotechnol. Johannes Kügler, Dr.-Ing. Marius Henkel, Dr. rer. nat. Markus Andre, Dr.-Ing. Ulrike Engel, M. Sc. Janina Beuker, Dipl.-Ing. Michaela Zwick, M. Sc. Judit Willenbacher, M. Sc. Sarah Dold, M. Sc. Christin Slomka, Sandra Baumann, Dr.-Ing. Katrin Ochsenreither, Dipl.-Ing. Florian Oswald, Desiree Westermann, Werner Mandel, Harald Gotzmann, Siegfried Almstedt, Katja Rupp, Susanne Warth, M.
  • Characterisation, Classification and Conformational Variability Of

    Characterisation, Classification and Conformational Variability Of

    Characterisation, Classification and Conformational Variability of Organic Enzyme Cofactors Julia D. Fischer European Bioinformatics Institute Clare Hall College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 11 April 2011 This dissertation is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation does not exceed the word limit of 60,000 words. Acknowledgements I would like to thank all the members of the Thornton research group for their constant interest in my work, their continuous willingness to answer my academic questions, and for their company during my time at the EBI. This includes Saumya Kumar, Sergio Martinez Cuesta, Matthias Ziehm, Dr. Daniela Wieser, Dr. Xun Li, Dr. Irene Pa- patheodorou, Dr. Pedro Ballester, Dr. Abdullah Kahraman, Dr. Rafael Najmanovich, Dr. Tjaart de Beer, Dr. Syed Asad Rahman, Dr. Nicholas Furnham, Dr. Roman Laskowski and Dr. Gemma Holli- day. Special thanks to Asad for allowing me to use early development versions of his SMSD software and for help and advice with the KEGG API installation, to Roman for knowing where to find all kinds of data, to Dani for help with R scripts, to Nick for letting me use his E.C. tree program, to Tjaart for python advice and especially to Gemma for her constant advice and feedback on my work in all aspects, in particular the chemistry side. Most importantly, I would like to thank Prof. Janet Thornton for giving me the chance to work on this project, for all the time she spent in meetings with me and reading my work, for sharing her seemingly limitless knowledge and enthusiasm about the fascinating world of enzymes, and for being such an experienced and motivational advisor.
  • Recent Progress in the Microbial Production of Pyruvic Acid

    Recent Progress in the Microbial Production of Pyruvic Acid

    fermentation Review Recent Progress in the Microbial Production of Pyruvic Acid Neda Maleki 1 and Mark A. Eiteman 2,* 1 Department of Food Science, Engineering and Technology, University of Tehran, Karaj 31587-77871, Iran; [email protected] 2 School of Chemical, Materials and Biomedical Engineering, University of Georgia, Athens, GA 30602, USA * Correspondence: [email protected]; Tel.: +1-706-542-0833 Academic Editor: Gunnar Lidén Received: 10 January 2017; Accepted: 6 February 2017; Published: 13 February 2017 Abstract: Pyruvic acid (pyruvate) is a cellular metabolite found at the biochemical junction of glycolysis and the tricarboxylic acid cycle. Pyruvate is used in food, cosmetics, pharmaceutical and agricultural applications. Microbial production of pyruvate from either yeast or bacteria relies on restricting the natural catabolism of pyruvate, while also limiting the accumulation of the numerous potential by-products. In this review we describe research to improve pyruvate formation which has targeted both strain development and process development. Strain development requires an understanding of carbohydrate metabolism and the many competing enzymes which use pyruvate as a substrate, and it often combines classical mutation/isolation approaches with modern metabolic engineering strategies. Process development requires an understanding of operational modes and their differing effects on microbial growth and product formation. Keywords: auxotrophy; Candida glabrata; Escherichia coli; fed-batch; metabolic engineering; pyruvate; pyruvate dehydrogenase 1. Introduction Pyruvic acid (pyruvate at neutral pH) is a three carbon oxo-monocarboxylic acid, also known as 2-oxopropanoic acid, 2-ketopropionic acid or acetylformic acid. Pyruvate is biochemically located at the end of glycolysis and entry into the tricarboxylic acid (TCA) cycle (Figure1).
  • Trehalose-Mediated Enhancement of Glycosaminoglycan Degradation in the Lysosomal Storage Disorder Mucopolysaccharidosis III

    Trehalose-Mediated Enhancement of Glycosaminoglycan Degradation in the Lysosomal Storage Disorder Mucopolysaccharidosis III

    Aus dem Institut für Humangenetik der Universität zu Köln Direktorin: Frau Universitätsprofessor Dr. rer. nat. B. Wirth Trehalose-mediated enhancement of glycosaminoglycan degradation in the lysosomal storage disorder Mucopolysaccharidosis III Trehalose vermittelte Steigerung des Glykosaminoglykan-Abbaus in der lysosomalen Speichererkrankung Mukopolysaccharidose III Inaugural-Dissertation zur Erlangung der Doktorwürde der Hohen Medizinischen Fakultät der Universität zu Köln vorgelegt von Victor Mauri aus Stuttgart promoviert am 29. Januar 2014 Gedruckt mit Genehmigung der Medizinischen Fakultät der Universität zu Köln, 2014 Dekan: Universitätsprofessor Dr. med. Dr. h.c. Th. Krieg 1. Berichterstatterin: Frau Universitätsprofessor Dr. rer. nat. B. Wirth 2. Berichterstatter: Professor Dr. rer. nat. F.-G. Hanisch Erklärung Ich erkläre hiermit, dass ich die vorliegende Dissertationsschrift ohne unzulässige Hilfe Dritter und ohne Benutzung anderer als der angegebenen Hilfsmittel angefertigt habe; die aus fremden Quellen direkt oder indirekt übernommenen Gedanken sind als solche kenntlich gemacht. Bei der Auswahl und Auswertung des Materials sowie bei der Herstellung des Manuskriptes habe ich Unterstützungsleistungen von folgenden Personen erhalten: Univ.-Prof. Dr. rer. nat. Brunhilde Wirth Marco Sardiello, PhD, Assistant Professor BCM Christian Schaaf, MD, PhD, Assistant Professor BCM Weitere Personen waren an der geistigen Herstellung der vorliegenden Arbeit nicht beteiligt. Insbesondere habe ich nicht die Hilfe einer Promotionsberaterin/eines