ABBREVIATION REACTION NAME REACTION Reactions That Occur
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Proteínas De Superfície De Paracoccidioides Brasiliensis
UNIVERSIDADE DE BRASÍLIA FACULDADE DE MEDICINA PROGRAMA DE PÓS-GRADUAÇÃO EM PATOLOGIA MOLECULAR Proteínas de superfície de Paracoccidioides brasiliensis CANDIDATA: NADYA DA SILVA CASTRO ORIENTADORA: DRA. CÉLIA MARIA DE ALMEIDA SOARES TESE APRESENTADA AO PROGRAMA DE PÓS-GRADUAÇÃO EM PATOLOGIA MOLECULAR, DA FACULDADE DE MEDICINA, DA UNIVERSIDADE DE BRASÍLIA COMO REQUISITO PARCIAL À OBTENÇÃO DO TÍTULO DE DOUTOR EM PATOLOGIA MOLECULAR. BRASÍLIA – DF MAIO 2008 TRABALHO REALIZADO NO LABORATÓRIO DE BIOLOGIA MOLECULAR, DEPARTAMENTO DE BIOQUÍMICA E BIOLOGIA MOLECULAR, INSTITUTO DE CIÊNCIAS BIOLÓGICAS, DA UNIVERSIDADE FEDERAL DE GOIÁS. APOIO FINANCEIRO: CAPES/ CNPQ/ FINEP/ FAPEG/ SECTEC-GO. II BANCA EXAMINADORA TITULARES Profa. Dra. Célia Maria de Almeida Soares, Instituto de Ciências Biológicas, Universidade Federal de Goiás. Prof. Dr. Augusto Schrank Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul Prof. Dr. Ivan Torres Nicolau de Campos Instituto de Ciências Biológicas, Universidade Federal de Goiás. Prof. Dr. Bergmann Morais Ribeiro Instituto de Ciências Biológicas, Universidade de Brasília. Prof. Dra. Anamélia Lorenzetti Bocca Instituto de Ciências Biológicas, Universidade de Brasília. SUPLENTE Prof. Dr. Fernando Araripe Gonçalves Torres Instituto de Ciências Biológicas, Universidade de Brasília. III ´- Os homens do seu planeta ² disse o pequeno Príncipe ² cultivam cinco mil rosas num jardim... e não encontram o que procuram... - É verdade ² respondi. - E, no entanto, o que eles procuram poderia ser encontrado numa só rosa, ou num pouco de água... - É verdade. E o principezinho acrescentou: Mas os olhos são cegos. eSUHFLVRYHUFRPRFRUDomRµ ³O pequeno príncipe´ de Antonie de Saint-Exupéry IV Dedico esta tese aos meus queridos pais, Nadson e Genialda, que foram e são exemplos de dedicação e de perseverança e cujos incentivos, apoio e amor contribuíram em muito para a realização deste trabalho. -
HEAT INACTIVATION of THIAMINASE in WHOLE FISH by R
August 1966 COMMERCIAL FISHERIES REVIEW 11 HEAT INACTIVATION OF THIAMINASE IN WHOLE FISH By R. H. Gnaedinger and R. A. Krzeczkowskil,c ABSTRACT The time required at various temperatures to inactivate all of the thiam inase in several species of whole fish was studied. Some effects of pH and enzyme concentra tion on the time-temperature inactivation were also determined. Whole raw fish were ground! sealed in spec~ally-constructed m etal cans, heated a t various tempera tures .for. varIOUS length.s <;>f tune! and analyzed for residual thiaminase a ct ivity. Re sul~ md.lcate that a m~un .um tune -tempe.rature of 5 minutes a t 1800 F. is required t<;> mac.tlvate all the .thl~mma s e of who.le hsh. Enzyme concentrations, pH, a nd pos slbly 011 c ontent of flsh mfluence the tune required to destroy thiaminase. INTRODUCTION The heating conditions employed b y commercial mink-food producers and mink ranchers ;0 destroy thiaminase in whole fish are empiri cal. The conditions are not based on predeter nined time-temperature relations for the thermal inactivation of this antimetabolite. A com mon practice, for example, is to cook the fish at 1800 -2000 F. for 15 minutes (Bor gstrom 1962). Most of the specific data available on the time -temperature r e la tion is found in various research publications dealing with the occurrence of thiamina s e in fish , or with studies on the chemistry of the enzyme. Deutsch and Hasler (1943) used 15 m i nutes at 100 0 C . -
Control Engineering Perspective on Genome-Scale Metabolic Modeling
Control Engineering Perspective on Genome-Scale Metabolic Modeling by Andrew Louis Damiani A dissertation submitted to the Graduate Faculty of Auburn University in partial fulfillment of the requirements for the Degree of Doctor of Philosophy Auburn, Alabama December 12, 2015 Key words: Scheffersomyces stipitis, Flux Balance Analysis, Genome-scale metabolic models, System Identification Framework, Model Validation, Phenotype Phase Plane Analysis Copyright 2015 by Andrew Damiani Approved by Jin Wang, Chair, Associate Professor of Chemical Engineering Q. Peter He, Associate Professor of Chemical Engineering, Tuskegee University Thomas W. Jeffries, Professor of Bacteriology, Emeritus; University of Wisconsin-Madison Allan E. David, Assistant Professor of Chemical Engineering Yoon Y. Lee, Professor of Chemical Engineering Abstract Fossil fuels impart major problems on the global economy and have detrimental effects to the environment, which has caused a world-wide initiative of producing renewable fuels. Lignocellulosic bioethanol for renewable energy has recently gained attention, because it can overcome the limitations that first generation biofuels impose. Nonetheless, in order to have this process commercialized, the biological conversion of pentose sugars, mainly xylose, needs to be improved. Scheffersomyces stipitis has a physiology that makes it a valuable candidate for lignocellulosic bioethanol production, and lately has provided genes for designing recombinant Saccharomyces cerevisiae. In this study, a system biology approach was taken to understand the relationship of the genotype to phenotype, whereby genome-scale metabolic models (GSMMs) are used in conjunction with constraint-based modeling. The major restriction of GSMMs is having an accurate methodology for validation and evaluation. This is due to the size and complexity of the models. -
Generated by SRI International Pathway Tools Version 25.0, Authors S
An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000238675-HmpCyc: Bacillus smithii 7_3_47FAA Cellular Overview Connections between pathways are omitted for legibility. -
| Hai Lui a Un Acutul Luniit Moonhiti
|HAI LUI AUN ACUTULUS010006055B2 LUNIIT MOONHITI (12 ) United States Patent (10 ) Patent No. : US 10 , 006 , 055 B2 Burk et al. (45 ) Date of Patent: Jun . 26 , 2018 ( 54 ) MICROORGANISMS FOR PRODUCING 2002/ 0168654 A1 11/ 2002 Maranas et al. 2003 / 0059792 Al 3 /2003 Palsson et al . BUTADIENE AND METHODS RELATED 2003 /0087381 A1 5 / 2003 Gokarn THERETO 2003 / 0224363 Al 12 /2003 Park et al . 2003 / 0233218 Al 12 /2003 Schilling (71 ) Applicant: Genomatica , Inc. , San Diego , CA (US ) 2004 / 0009466 AL 1 /2004 Maranas et al. 2004 / 0029149 Al 2 /2004 Palsson et al. ( 72 ) Inventors : Mark J . Burk , San Diego , CA (US ) ; 2004 / 0072723 A1 4 /2004 Palsson et al. Anthony P . Burgard , Bellefonte , PA 2004 / 0152159 Al 8 / 2004 Causey et al . 2005 /0042736 A1 2 / 2005 San et al . (US ) ; Robin E . Osterhout , San Diego , 2005 / 0079482 A1 4 / 2005 Maranas et al . CA (US ) ; Jun Sun , San Diego , CA 2006 / 0046288 Al 3 / 2006 Ka - Yiu et al. ( US ) ; Priti Pharkya , San Diego , CA 2006 / 0073577 A1 4 / 2006 Ka - Yiu et al . (US ) 2007 /0184539 Al 8 / 2007 San et al . 2009 / 0047718 Al 2 / 2009 Blaschek et al . 2009 / 0047719 Al 2 / 2009 Burgard et al . (73 ) Assignee : Genomatica , Inc ., San Diego , CA (US ) 2009 /0191593 A1 7 / 2009 Burk et al . 2010 / 0003716 A1 1 / 2010 Cervin et al. ( * ) Notice : Subject to any disclaimer , the term of this 2010 /0184171 Al 7 /2010 Jantama et al. patent is extended or adjusted under 35 2010 /0304453 Al 12 / 2010 Trawick et al . -
Effects of Dietary Thiaminase on Reproductive Traits in Three Populations of Atlantic Salmon Targeted for Reintroduction Into Lake Ontario
Western University Scholarship@Western Electronic Thesis and Dissertation Repository 1-22-2020 1:00 PM Effects of dietary thiaminase on reproductive traits in three populations of Atlantic salmon targeted for reintroduction into Lake Ontario Kimberly T. Mitchell The University of Western Ontario Supervisor Neff, Bryan D. The University of Western Ontario Graduate Program in Biology A thesis submitted in partial fulfillment of the equirr ements for the degree in Master of Science © Kimberly T. Mitchell 2020 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Aquaculture and Fisheries Commons, Biodiversity Commons, and the Terrestrial and Aquatic Ecology Commons Recommended Citation Mitchell, Kimberly T., "Effects of dietary thiaminase on reproductive traits in three populations of Atlantic salmon targeted for reintroduction into Lake Ontario" (2020). Electronic Thesis and Dissertation Repository. 6826. https://ir.lib.uwo.ca/etd/6826 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. Abstract The fitness of reintroduced salmonids in Lake Ontario can be reduced by high levels of thiaminase in exotic prey consumed at the adult stage. If sensitivity to dietary thiaminase differs among the three Atlantic salmon populations targeted for reintroduction into Lake Ontario, this could significantly influence their performance. I quantified the effects of experimental diets that contained high or low (control) levels of thiaminase on thiamine concentrations, survival, growth rate, and reproductive traits (sperm and egg quality) in Atlantic salmon from the three candidate source populations. -
(12) Patent Application Publication (10) Pub. No.: US 2014/0155567 A1 Burk Et Al
US 2014O155567A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2014/0155567 A1 Burk et al. (43) Pub. Date: Jun. 5, 2014 (54) MICROORGANISMS AND METHODS FOR (60) Provisional application No. 61/331,812, filed on May THE BIOSYNTHESIS OF BUTADENE 5, 2010. (71) Applicant: Genomatica, Inc., San Diego, CA (US) Publication Classification (72) Inventors: Mark J. Burk, San Diego, CA (US); (51) Int. Cl. Anthony P. Burgard, Bellefonte, PA CI2P 5/02 (2006.01) (US); Jun Sun, San Diego, CA (US); CSF 36/06 (2006.01) Robin E. Osterhout, San Diego, CA CD7C II/6 (2006.01) (US); Priti Pharkya, San Diego, CA (52) U.S. Cl. (US) CPC ................. CI2P5/026 (2013.01); C07C II/I6 (2013.01); C08F 136/06 (2013.01) (73) Assignee: Genomatica, Inc., San Diego, CA (US) USPC ... 526/335; 435/252.3:435/167; 435/254.2: (21) Appl. No.: 14/059,131 435/254.11: 435/252.33: 435/254.21:585/16 (22) Filed: Oct. 21, 2013 (57) ABSTRACT O O The invention provides non-naturally occurring microbial Related U.S. Application Data organisms having a butadiene pathway. The invention addi (63) Continuation of application No. 13/101,046, filed on tionally provides methods of using Such organisms to produce May 4, 2011, now Pat. No. 8,580,543. butadiene. Patent Application Publication Jun. 5, 2014 Sheet 1 of 4 US 2014/O155567 A1 ?ueudos!SMS |?un61– Patent Application Publication Jun. 5, 2014 Sheet 2 of 4 US 2014/O155567 A1 VOJ OO O Z?un61– Patent Application Publication US 2014/O155567 A1 {}}} Hººso Patent Application Publication Jun. -
Generate Metabolic Map Poster
Authors: Peter D. Karp Suzanne Paley Julio Collado-Vides John L Ingraham Ingrid Keseler Markus Krummenacker Cesar Bonavides-Martinez Robert Gunsalus An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Carol Fulcher Ian Paulsen Socorro Gama-Castro Robert LaRossa Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. EcoCyc: Escherichia coli K-12 substr. MG1655 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari Amanda Mackie Alberto Santos-Zavaleta succinate phosphate succinate N-acetyl-DL-methionine + L-ornithine glutathione + L-methionine S-oxide D-fructofuranose γ Ag+ molybdate ferroheme b L,L-homocystine asp lys cys L-alanyl- -D- D-mannopyranose 6-phosphate 2+ 2+ H D-methionine 2-deoxy-D-glucose succinate formate formate succinate D-tartrate putrescine agmatine cadaverine L-tartrate D-fructofuranose 6-phosphate + nitrate nitrate Cu thiosulfate deoxycholate L,L-homocystine D-cystine D-cycloserine methyl β-D-glucoside putrescine asp spermidine (S)-2-hydroxybutanoate (S)-2-hydroxybutanoate arg L-homoserine lactone magnesium hydrogenphosphate magnesium hydrogenphosphate antimonous acid glutamyl-meso- Co2+ Cd2+ lactulose poly-β-1,6- met cob(I)inamide 2,3-dioxo- -
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 -
Supplementary Table 16 Components of the Secretory Pathway
Supplementary Table 16 Components of the secretory pathway Aspergillus niger Description of putative Aspergillus niger gene Best homolog to putative A.niger gene A.niger orf A.niger A.nidulans A.fumigatus A.oryzae N.crassa S.cerevisiae Mammal gene Entry into ER Signal recognition YKL122c An01g02800 strong similarity to signal recognition particle 68K protein SRP68 - AN4043.2 Afu1g03940 AO090003000956 NCU10927.2 YPL243w Canis lupus An04g06890 similarity to 72-kD protein of the signal recognition particle SRP72 -AN2014.2 Afu4g10180 AO090003001205 NCU01455.2 YPL210c Canis lupus An01g10070 strong similarity to signal recognition particle chain Sec65 - AN0643.2 Afu1g16820 NCU03485.2 YML105c Saccharomyces cerevisiae AN0642.2 An15g06470 similarity to signal sequence receptor alpha chain - Canis lupus AN2140.2 Afu2g16120 AO090012000186 NCU01146.2 familiaris An07g05800 similarity to signal recognition particle protein srp14 - Canis lupus AN4580.2 Afu2g01990 AO090011000469 YDL092w An09g06320 similarity to signal recognition particle 54K protein SRP54 - AN8246.2 Afu5g03880 AO090102000593 NCU09696.2 YPR088c Saccharomyces cerevisiae Signal peptidase An01g00560 strong similarity to signal peptidase subunit Sec11 - AN3126.2 Afu3g12840 AO090012000838 NCU04519.2 YIR022w Saccharomyces cerevisiae An17g02095 similarity to signal peptidase subunit Spc1 - Saccharomyces Afu5g05800 YJR010c-a cerevisiae An16g07390 strong similarity to signal peptidase subunit Spc2 - AN1525.2 Afu8g05340 AO090005000615 NCU00965.2 YML055w Saccharomyces cerevisiae An09g05420 similarity -
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 -
Open Matthew R Moreau Ph.D. Dissertation Finalfinal.Pdf
The Pennsylvania State University The Graduate School Department of Veterinary and Biomedical Sciences Pathobiology Program PATHOGENOMICS AND SOURCE DYNAMICS OF SALMONELLA ENTERICA SEROVAR ENTERITIDIS A Dissertation in Pathobiology by Matthew Raymond Moreau 2015 Matthew R. Moreau Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy May 2015 The Dissertation of Matthew R. Moreau was reviewed and approved* by the following: Subhashinie Kariyawasam Associate Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Bhushan M. Jayarao Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Mary J. Kennett Professor, Veterinary and Biomedical Sciences Vijay Kumar Assistant Professor, Department of Nutritional Sciences Anthony Schmitt Associate Professor, Veterinary and Biomedical Sciences Head of the Pathobiology Graduate Program *Signatures are on file in the Graduate School iii ABSTRACT Salmonella enterica serovar Enteritidis (SE) is one of the most frequent common causes of morbidity and mortality in humans due to consumption of contaminated eggs and egg products. The association between egg contamination and foodborne outbreaks of SE suggests egg derived SE might be more adept to cause human illness than SE from other sources. Therefore, there is a need to understand the molecular mechanisms underlying the ability of egg- derived SE to colonize the chicken intestinal and reproductive tracts and cause disease in the human host. To this end, the present study was carried out in three objectives. The first objective was to sequence two egg-derived SE isolates belonging to the PFGE type JEGX01.0004 to identify the genes that might be involved in SE colonization and/or pathogenesis.