Base de dados : MEDLINE
Pesquisa : D08.811.277.352.897.700 [Categoria DeCS]
Referências encontradas : 381 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 39 ir para página                         

  1 / 381 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28322575
[Au] Autor:Ek WE; Ahsan M; Rask-Andersen M; Liang L; Moffatt MF; Gyllensten U; Johansson Å
[Ad] Endereço:Department of Immunology, Genetics & Pathology, Science for Life Laboratory, Uppsala University, Box 815 75108 Uppsala, Sweden.
[Ti] Título:Epigenome-wide DNA methylation study of IgE concentration in relation to self-reported allergies.
[So] Source:Epigenomics;9(4):407-418, 2017 Apr.
[Is] ISSN:1750-192X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: Epigenetic mechanisms are critical for normal immune development and epigenetic alterations might therefore be possible contributors to immune diseases. To investigate if DNA methylation in whole blood is associated with total and allergen-specific IgE levels. METHODS: We performed an epigenome-wide association study to investigate the association between DNA methylation and IgE level, allergen-specific IgE and self-reported immune diseases and allergies in 728 individuals. RESULTS: We identified and replicated 15 CpG sites associated with IgE, mapping to biologically relevant genes, including ACOT7, ILR5A, KCNH2, PRG2 and EPX. A total of 331 loci were associated with allergen-specific IgE, but none of these CpG sites were associated with self-reported allergies and immune diseases. CONCLUSION: This study shows that IgE levels are associated with DNA methylation levels at numerous CpG sites, which might provide new leads for investigating the links between IgE and allergic inflammation.
[Mh] Termos MeSH primário: Metilação de DNA
Epigenômica/métodos
Estudo de Associação Genômica Ampla/métodos
Hipersensibilidade/genética
Imunoglobulina E/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Criança
Pré-Escolar
Ilhas de CpG
Canal de Potássio ERG1/genética
Proteína Básica Maior de Eosinófilos/genética
Feminino
Seres Humanos
Hipersensibilidade/imunologia
Masculino
Meia-Idade
Palmitoil-CoA Hidrolase/genética
Proteoglicanas/genética
Autorrelato
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ERG1 Potassium Channel); 0 (KCNH2 protein, human); 0 (Proteoglycans); 147016-17-9 (PRG2 protein, human); 37341-29-0 (Immunoglobulin E); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); EC 3.1.27.- (Eosinophil Major Basic Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.2217/epi-2016-0158


  2 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28156101
[Au] Autor:Swarbrick CM; Bythrow GV; Aragao D; Germain GA; Quadri LE; Forwood JK
[Ad] Endereço:School of Biomedical Sciences, Charles Sturt University , Wagga Wagga, New South Wales 2678, Australia.
[Ti] Título:Mycobacteria Encode Active and Inactive Classes of TesB Fatty-Acyl CoA Thioesterases Revealed through Structural and Functional Analysis.
[So] Source:Biochemistry;56(10):1460-1472, 2017 Mar 14.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycobacteria contain a large number of highly divergent species and exhibit unusual lipid metabolism profiles, believed to play important roles in immune invasion. Thioesterases modulate lipid metabolism through the hydrolysis of activated fatty-acyl CoAs; multiple copies are present in mycobacteria, yet many remain uncharacterized. Here, we undertake a comprehensive structural and functional analysis of a TesB thioesterase from Mycobacterium avium (MaTesB). Structural superposition with other TesB thioesterases reveals that the Asp active site residue, highly conserved across a wide range of TesB thioesterases, is mutated to Ala. Consistent with these structural data, the wild-type enzyme failed to hydrolyze an extensive range of acyl-CoA substrates. Mutation of this residue to an active Asp residue restored activity against a range of medium-chain length fatty-acyl CoA substrates. Interestingly, this Ala mutation is highly conserved across a wide range of Mycobacterium species but not found in any other bacteria or organism. Our structural homology analysis revealed that at least one other TesB acyl-CoA thioesterase also contains an Ala residue at the active site, while two other Mycobacterium TesB thioesterases harbor an Asp residue at the active site. The inactive TesBs display a common quaternary structure that is distinct from that of the active TesB thioesterases. Investigation of the effect of expression of either the catalytically active or inactive MaTesB in Mycobacterium smegmatis exposed, to the best of our knowledge, the first genotype-phenotype association implicating a mycobacterial tesB gene. This is the first report that mycobacteria encode active and inactive forms of thioesterases, the latter of which appear to be unique to mycobacteria.
[Mh] Termos MeSH primário: Acil Coenzima A/química
Proteínas de Bactérias/química
Mycobacterium avium/enzimologia
Mycobacterium smegmatis/enzimologia
Palmitoil-CoA Hidrolase/química
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Alanina/química
Alanina/metabolismo
Sequência de Aminoácidos
Substituição de Aminoácidos
Ácido Aspártico/química
Ácido Aspártico/metabolismo
Proteínas de Bactérias/classificação
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Escherichia coli/enzimologia
Escherichia coli/genética
Expressão Gênica
Estudos de Associação Genética
Hidrólise
Isoenzimas/química
Isoenzimas/classificação
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Mutação
Mycobacterium avium/genética
Mycobacterium smegmatis/genética
Palmitoil-CoA Hidrolase/classificação
Palmitoil-CoA Hidrolase/genética
Palmitoil-CoA Hidrolase/metabolismo
Domínios Proteicos
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/classificação
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Isoenzymes); 0 (Recombinant Proteins); 30KYC7MIAI (Aspartic Acid); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01049


  3 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27653630
[Au] Autor:Luo HD; Jin MY; Wu H; Jiang H
[Ti] Título:Functions of Type II Thioesterases in Bacterial Polyketide Biosynthesis.
[So] Source:Protein Pept Lett;23(11):1032-1037, 2016.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Many polyketides show biological activities and have thus been applied in clinics, as food additives, and in agriculture. Type II thioesterases (TEIIs) play an important role in polyketide biosynthesis. Most TEIIs belong to α/ß-hydrolase family and usually contain a catalytic triad Ser-His-Asp. In polyketide biosynthesis, TEIIs can play an editing role by removal of aberrant non-extendable acyl units in elongation steps, a starter unit selection role by removal of unfavored starter acyl units in initiation steps, and a releasing role by removal of final product in termination steps. Complementation of TEIIs has been observed and applied.
[Mh] Termos MeSH primário: Ácido Graxo Sintases/metabolismo
Policetídeos/metabolismo
Streptomyces/metabolismo
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Palmitoil-CoA Hidrolase/metabolismo
Policetídeo Sintases/metabolismo
Streptomyces/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyketides); 79956-01-7 (Polyketide Synthases); EC 2.3.1.85 (Fatty Acid Synthases); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.- (thioesterase II); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE


  4 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26927806
[Au] Autor:Serena M; Giorgetti A; Busato M; Gasparini F; Diani E; Romanelli MG; Zipeto D
[Ad] Endereço:Department of Neurosciences, Biomedicine and Movement Sciences, University of Verona, Strada le Grazie 8, 37134 Verona, Italy.
[Ti] Título:Molecular characterization of HIV-1 Nef and ACOT8 interaction: insights from in silico structural predictions and in vitro functional assays.
[So] Source:Sci Rep;6:22319, 2016 Mar 01.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:HIV-1 Nef interacts with several cellular proteins, among which the human peroxisomal thioesterase 8 (ACOT8). This interaction may be involved in the endocytosis regulation of membrane proteins and might modulate lipid composition in membrane rafts. Nef regions involved in the interaction have been experimentally characterized, whereas structural details of the ACOT8 protein are unknown. The lack of structural information hampers the comprehension of the functional consequences of the complex formation during HIV-1 infection. We modelled, through in silico predictions, the ACOT8 structure and we observed a high charge complementarity between Nef and ACOT8 surfaces, which allowed the identification of the ACOT8 putative contact points involved in the interaction. The predictions were validated by in vitro assays through the development of ACOT8 deletion mutants. Coimmunoprecipitation and immunofluorescence analyses showed that ACOT8 Arg(45)-Phe(55) and Arg(86)-Pro(93) regions are involved in Nef association. In addition, K91S mutation abrogated the interaction with Nef, indicating that Lys(91) plays a key role in the interaction. Finally, when associated with ACOT8, Nef may be preserved from degradation. These findings improve the comprehension of the association between HIV-1 Nef and ACOT8, helping elucidating the biological effect of their interaction.
[Mh] Termos MeSH primário: HIV-1/fisiologia
Modelos Moleculares
Palmitoil-CoA Hidrolase/metabolismo
Produtos do Gene nef do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Seres Humanos
Lisina/genética
Palmitoil-CoA Hidrolase/genética
Ligação Proteica/genética
Conformação Proteica
Engenharia de Proteínas
Domínios e Motivos de Interação entre Proteínas/genética
Deleção de Sequência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (nef Gene Products, Human Immunodeficiency Virus); 0 (nef protein, Human immunodeficiency virus 1); EC 3.1.2.2 (ACOT8 protein, human); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE
[do] DOI:10.1038/srep22319


  5 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26861785
[Au] Autor:Martinez-Sanchez A; Pullen TJ; Chabosseau P; Zhang Q; Haythorne E; Cane MC; Nguyen-Tu MS; Sayers SR; Rutter GA
[Ad] Endereço:Section of Cell Biology and Functional Genomics, Division of Diabetes, Endocrinology and Metabolism, Imperial Centre for Translational and Experimental Medicine, Imperial College London, London, U.K.
[Ti] Título:Disallowance of Acot7 in ß-Cells Is Required for Normal Glucose Tolerance and Insulin Secretion.
[So] Source:Diabetes;65(5):1268-82, 2016 May.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Encoding acyl-CoA thioesterase-7 (Acot7) is one of ∼60 genes expressed ubiquitously across tissues but relatively silenced, or disallowed, in pancreatic ß-cells. The capacity of ACOT7 to hydrolyze long-chain acyl-CoA esters suggests potential roles in ß-oxidation, lipid biosynthesis, signal transduction, or insulin exocytosis. We explored the physiological relevance of ß-cell-specific Acot7 silencing by re-expressing ACOT7 in these cells. ACOT7 overexpression in clonal MIN6 and INS1(832/13) ß-cells impaired insulin secretion in response to glucose plus fatty acids. Furthermore, in a panel of transgenic mouse lines, we demonstrate that overexpression of mitochondrial ACOT7 selectively in the adult ß-cell reduces glucose tolerance dose dependently and impairs glucose-stimulated insulin secretion. By contrast, depolarization-induced secretion was unaffected, arguing against a direct action on the exocytotic machinery. Acyl-CoA levels, ATP/ADP increases, membrane depolarization, and Ca(2+) fluxes were all markedly reduced in transgenic mouse islets, whereas glucose-induced oxygen consumption was unchanged. Although glucose-induced increases in ATP/ADP ratio were similarly lowered after ACOT7 overexpression in INS1(832/13) cells, changes in mitochondrial membrane potential were unaffected, consistent with an action of Acot7 to increase cellular ATP consumption. Because Acot7 mRNA levels are increased in human islets in type 2 diabetes, inhibition of the enzyme might provide a novel therapeutic strategy.
[Mh] Termos MeSH primário: Regulação para Baixo
Ácidos Graxos não Esterificados/metabolismo
Regulação Enzimológica da Expressão Gênica
Glucose/metabolismo
Células Secretoras de Insulina/metabolismo
Insulina/secreção
Palmitoil-CoA Hidrolase/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Linhagem Celular Tumoral
Células Clonais
Feminino
Intolerância à Glucose/enzimologia
Intolerância à Glucose/metabolismo
Intolerância à Glucose/patologia
Células Secretoras de Insulina/citologia
Células Secretoras de Insulina/patologia
Células Secretoras de Insulina/secreção
Ilhotas Pancreáticas/citologia
Ilhotas Pancreáticas/metabolismo
Ilhotas Pancreáticas/patologia
Ilhotas Pancreáticas/secreção
Masculino
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Especificidade de Órgãos
Palmitoil-CoA Hidrolase/genética
Ratos
Proteínas Recombinantes/metabolismo
Caracteres Sexuais
Técnicas de Cultura de Tecidos
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids, Nonesterified); 0 (Insulin); 0 (Recombinant Proteins); EC 3.1.2.2 (Acot7 protein, mouse); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.2337/db15-1240


  6 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26553755
[Au] Autor:Ray L; Yamanaka K; Moore BS
[Ad] Endereço:Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92037 (USA) http://scrippsscholars.ucsd.edu/bsmoore.
[Ti] Título:A Peptidyl-Transesterifying Type I Thioesterase in Salinamide Biosynthesis.
[So] Source:Angew Chem Int Ed Engl;55(1):364-7, 2016 Jan 04.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Salinamide A belongs to a rare class of bicyclic depsipeptide antibiotics in which the installation of a (4-methylhexa-2,4-dienoyl)glycine handle across a hexadepsipeptide core contributes to its chemical complexity and biological properties. Herein, we report the genetic and biochemical basis for salinamide construction in the marine bacterium Streptomyces sp. CNB-091, which involves a novel intermolecular transesterification reaction catalyzed by a type I thioesterase. Heterologous expression studies revealed the central role of the nonribosomal peptide synthetase Sln9 in constructing and installing the distinctive acylglycine "basket handle" of salinamide. Biochemical characterization of the Sln9 thioesterase domain established that transesterification of the serine residue of desmethylsalinamide E with acylated glycyl thioesters yields desmethylsalinamide C.
[Mh] Termos MeSH primário: Depsipeptídeos/biossíntese
Palmitoil-CoA Hidrolase/metabolismo
[Mh] Termos MeSH secundário: Depsipeptídeos/química
Conformação Molecular
Palmitoil-CoA Hidrolase/química
Estereoisomerismo
Streptomyces/química
Streptomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Depsipeptides); 0 (salinamide A); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170104
[Lr] Data última revisão:
170104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151111
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201508576


  7 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26388428
[Au] Autor:Leber C; Choi JW; Polson B; Da Silva NA
[Ad] Endereço:Department of Chemical Engineering and Materials Science, University of California, Irvine, 92697-2575, California.
[Ti] Título:Disrupted short chain specific ß-oxidation and improved synthase expression increase synthesis of short chain fatty acids in Saccharomyces cerevisiae.
[So] Source:Biotechnol Bioeng;113(4):895-900, 2016 Apr.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biologically derived fatty acids have gained tremendous interest as an alternative to petroleum-derived fuels and chemical precursors. We previously demonstrated the synthesis of short chain fatty acids in Saccharomyces cerevisiae by introduction of the Homo sapiens fatty acid synthase (hFAS) with heterologous phosphopantetheine transferases and heterologous thioesterases. In this study, short chain fatty acid production was improved by combining a variety of novel enzyme and metabolic engineering strategies. The use of a H. sapiens-derived thioesterase and phosphopantetheine transferase were evaluated. In addition, strains were engineered to disrupt either the full ß-oxidation (by deleting FAA2, PXA1, and POX1) or short chain-specific ß-oxidation (by deleting FAA2, ANT1, and PEX11) pathways. Prohibiting full ß-oxidation increased hexanoic and octanoic acid levels by 8- and 79-fold relative to the parent strain expressing hFAS. However, by targeting only short chain ß-oxidation, hexanoic and octanoic acid levels increased further to 31- and 140-fold over the parent. In addition, an optimized hFAS gene increased hexanoic, octanoic, decanoic and total short chain fatty acid levels by 2.9-, 2.0-, 2.3-, and 2.2-fold, respectively, relative to the non-optimized counterpart. By combining these unique enzyme and metabolic engineering strategies, octanoic acid was increased more than 181-fold over the parent strain expressing hFAS.
[Mh] Termos MeSH primário: Ácidos Graxos Voláteis/metabolismo
Engenharia Metabólica/métodos
Redes e Vias Metabólicas/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Deleção de Genes
Seres Humanos
Oxirredução
Palmitoil-CoA Hidrolase/genética
Palmitoil-CoA Hidrolase/metabolismo
Transferases (Outros Grupos de Fosfato Substituídos)/genética
Transferases (Outros Grupos de Fosfato Substituídos)/metabolismo
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids, Volatile); 0 (phosphopantetheinyl transferase); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150922
[St] Status:MEDLINE
[do] DOI:10.1002/bit.25839


  8 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25642666
[Au] Autor:Horsman ME; Hari TP; Boddy CN
[Ad] Endereço:Department of chemistry, Centre for Catalysis Research and Innovation, University of Ottawa, Canada. cboddy@uottawa.ca.
[Ti] Título:Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?
[So] Source:Nat Prod Rep;33(2):183-202, 2016 Feb.
[Is] ISSN:1460-4752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Type 1, α/ß hydrolase-like thioesterase (TE) domains are essential offloading enzymes, releasing covalently bound products from fatty acid, polyketide, and non-ribosomal peptide biosynthetic complexes. The release step can occur by attack of an exogenous nucleophile effecting hydrolysis or transesterification or by an intramolecular O-, N-, or C-nucleophile, effecting macrolactonization, macrolactamization or Claisen-like condensation of the product. Thus in addition to ensuring turnover of the pathway, TEs provide access to increased chemical diversity. We review the diversity, structure, and mechanism of PKS and NRPS TEs and discuss recent works that highlight the role of TEs as potential arbitrators in offloading. In particular, we examine cases where TEs act as logic gates that ask a particular question about the substrate and use this information to determine the substrate's fate. As the TE mechanism occurs via two steps, we analyze both the loading and release steps independently as logic gates. The use of logic gates provides an important perspective when evaluating the evolution of TEs within a pathway, as well as highlighting work towards the goal of predicting TE function in unknown and engineered pathways.
[Mh] Termos MeSH primário: Produtos Biológicos/metabolismo
Palmitoil-CoA Hidrolase/metabolismo
Peptídeo Sintases/metabolismo
[Mh] Termos MeSH secundário: Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biological Products); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160204
[Lr] Data última revisão:
160204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150203
[St] Status:MEDLINE
[do] DOI:10.1039/c4np00148f


  9 / 381 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26129951
[Au] Autor:Rutter CD; Zhang S; Rao CV
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, University of Illinois-Urbana Champaign, 600 S. Mathews Ave, Urbana, IL, 61801, USA.
[Ti] Título:Engineering Yarrowia lipolytica for production of medium-chain fatty acids.
[So] Source:Appl Microbiol Biotechnol;99(17):7359-68, 2015 Sep.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Lipids are naturally derived products that offer an attractive, renewable alternative to petroleum-based hydrocarbons. While naturally produced long-chain fatty acids can replace some petroleum analogs, medium-chain fatty acid would more closely match the desired physical and chemical properties of currently employed petroleum products. In this study, we engineered Yarrowia lipolytica, an oleaginous yeast that naturally produces lipids at high titers, to produce medium-chain fatty acids. Five different acyl-acyl carrier protein (ACP) thioesterases with specificity for medium-chain acyl-ACP molecules were expressed in Y. lipolytica, resulting in formation of either decanoic or octanoic acid. These novel fatty acid products were found to comprise up to 40 % of the total cell lipids. Furthermore, the reduction in chain length resulted in a twofold increase in specific lipid productivity in these engineered strains. The medium-chain fatty acids were found to be incorporated into all lipid classes.
[Mh] Termos MeSH primário: Vias Biossintéticas/genética
Ácidos Graxos/biossíntese
Engenharia Metabólica
Yarrowia/genética
Yarrowia/metabolismo
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/metabolismo
Caprilatos/metabolismo
Ácidos Decanoicos/metabolismo
Expressão Gênica
Palmitoil-CoA Hidrolase/genética
Palmitoil-CoA Hidrolase/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Caprylates); 0 (Decanoic Acids); 0 (Fatty Acids); 0 (Recombinant Proteins); 4G9EDB6V73 (decanoic acid); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); OBL58JN025 (octanoic acid)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150702
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-015-6764-1


  10 / 381 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26067557
[Au] Autor:Yu S; Li H; Gao F; Zhou Y
[Ad] Endereço:Non-coding RNA Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China.
[Ti] Título:Crystal structure and potential physiological role of zebra fish thioesterase superfamily member 2 (fTHEM2).
[So] Source:Biochem Biophys Res Commun;463(4):912-6, 2015 Aug 07.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thioesterase superfamily member 2 (THEM2) is an essential protein for mammalian cell proliferation. It belongs to the hotdog-fold thioesterase superfamily and catalyzes hydrolysis of thioester bonds of acyl-CoA in vitro, while its in vivo function remains unrevealed. In this study, Zebra fish was selected as a model organism to facilitate the investigations on THEM2. First, we solved the crystal structure of recombinant fTHEM2 at the resolution of 1.80 Å, which displayed a similar scaffolding as hTHEM2. Second, functional studies demonstrated that fTHEM2 is capable of hydrolyzing palmitoyl-CoA in vitro. In addition, injection of morpholino against fTHEM2 at one-cell stage resulted in distorted early embryo development, including delayed cell division, retarded development and increased death rate. The above findings validated our hypothesis that fTHEM2 could serve as an ideal surrogate for studying the physiological functions of THEM2.
[Mh] Termos MeSH primário: Palmitoil-CoA Hidrolase/química
Palmitoil-CoA Hidrolase/fisiologia
Proteínas de Peixe-Zebra/química
Proteínas de Peixe-Zebra/fisiologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Domínio Catalítico
Cristalografia por Raios X
Primers do DNA
Técnicas de Silenciamento de Genes
Palmitoil-CoA Hidrolase/genética
Reação em Cadeia da Polimerase
Conformação Proteica
Peixe-Zebra/embriologia
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Zebrafish Proteins); EC 3.1.2.2 (Palmitoyl-CoA Hydrolase); EC 3.1.2.2 (THEM2 protein, zebrafish)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150708
[Lr] Data última revisão:
150708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150613
[St] Status:MEDLINE



página 1 de 39 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde