Base de dados : MEDLINE
Pesquisa : D08.811.464.267 [Categoria DeCS]
Referências encontradas : 55 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 6 ir para página                

  1 / 55 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27704180
[Au] Autor:Kojima K; Keta S; Uesaka K; Kato A; Takatani N; Ihara K; Omata T; Aichi M
[Ad] Endereço:Department of Biological Chemistry, Chubu University, Kasugai, 487-8501, Japan.
[Ti] Título:A simple method for isolation and construction of markerless cyanobacterial mutants defective in acyl-acyl carrier protein synthetase.
[So] Source:Appl Microbiol Biotechnol;100(23):10107-10113, 2016 Dec.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Cyanobacterial mutants defective in acyl-acyl carrier protein synthetase (Aas) secrete free fatty acids (FFAs) into the external medium and hence have been used for the studies aimed at photosynthetic production of biofuels. While the wild-type strain of Synechocystis sp. PCC 6803 is highly sensitive to exogenously added linolenic acid, mutants defective in the aas gene are known to be resistant to the externally provided fatty acid. In this study, the wild-type Synechocystis cells were shown to be sensitive to lauric, oleic, and linoleic acids as well, and the resistance to these fatty acids was shown to be enhanced by inactivation of the aas gene. On the basis of these observations, we developed an efficient method to isolate aas-deficient mutants from cultures of Synechocystis cells by counter selection using linoleic acid or linolenic acid as the selective agent. A variety of aas mutations were found in about 70 % of the FFA-resistant mutants thus selected. Various aas mutants were isolated also from Synechococcus sp. PCC 7002, using lauric acid as a selective agent. Selection using FFAs was useful also for construction of markerless aas knockout mutants from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Thus, genetic engineering of FFA-producing cyanobacterial strains would be greatly facilitated by the use of the FFAs for counter selection.
[Mh] Termos MeSH primário: Carbono-Enxofre Ligases/deficiência
Deleção de Genes
Synechococcus/enzimologia
Synechocystis/enzimologia
[Mh] Termos MeSH secundário: Farmacorresistência Bacteriana
Ácidos Láuricos/toxicidade
Ácido Linoleico/toxicidade
Mutação
Seleção Genética
Synechococcus/efeitos dos fármacos
Synechococcus/genética
Synechocystis/efeitos dos fármacos
Synechocystis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lauric Acids); 1160N9NU9U (lauric acid); 9KJL21T0QJ (Linoleic Acid); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


  2 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26900152
[Au] Autor:Guillet V; Galandrin S; Maveyraud L; Ladevèze S; Mariaule V; Bon C; Eynard N; Daffé M; Marrakchi H; Mourey L
[Ad] Endereço:From the Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, 31077 Toulouse, France valerie.guillet@ipbs.fr.
[Ti] Título:Insight into Structure-Function Relationships and Inhibition of the Fatty Acyl-AMP Ligase (FadD32) Orthologs from Mycobacteria.
[So] Source:J Biol Chem;291(15):7973-89, 2016 Apr 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycolic acids are essential components of the mycobacterial cell envelope, and their biosynthetic pathway is one of the targets of first-line antituberculous drugs. This pathway contains a number of potential targets, including some that have been identified only recently and have yet to be explored. One such target, FadD32, is required for activation of the long meromycolic chain and is essential for mycobacterial growth. We report here an in-depth biochemical, biophysical, and structural characterization of four FadD32 orthologs, including the very homologous enzymes fromMycobacterium tuberculosisandMycobacterium marinum Determination of the structures of two complexes with alkyl adenylate inhibitors has provided direct information, with unprecedented detail, about the active site of the enzyme and the associated hydrophobic tunnel, shedding new light on structure-function relationships and inhibition mechanisms by alkyl adenylates and diarylated coumarins. This work should pave the way for the rational design of inhibitors of FadD32, a highly promising drug target.
[Mh] Termos MeSH primário: Antituberculosos/farmacologia
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Desenho de Drogas
Ligases/química
Ligases/metabolismo
Mycobacterium tuberculosis/enzimologia
Mycobacterium/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/antagonistas & inibidores
Carbono-Enxofre Ligases
Cristalografia por Raios X
Ligases/antagonistas & inibidores
Modelos Moleculares
Dados de Sequência Molecular
Mycobacterium/química
Mycobacterium/efeitos dos fármacos
Infecções por Mycobacterium/tratamento farmacológico
Infecções por Mycobacterium/microbiologia
Mycobacterium tuberculosis/química
Mycobacterium tuberculosis/efeitos dos fármacos
Ácidos Micólicos/metabolismo
Conformação Proteica
Tuberculose/tratamento farmacológico
Tuberculose/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (Mycolic Acids); EC 6.- (Ligases); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170408
[Lr] Data última revisão:
170408
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160223
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.712612


  3 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26675168
[Au] Autor:Hopkinson RJ; Leung IK; Smart TJ; Rose NR; Henry L; Claridge TD; Schofield CJ
[Ad] Endereço:Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom.
[Ti] Título:Studies on the Glutathione-Dependent Formaldehyde-Activating Enzyme from Paracoccus denitrificans.
[So] Source:PLoS One;10(12):e0145085, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Formaldehyde is a toxin and carcinogen that is both an environmental pollutant and an endogenous metabolite. Formaldehyde metabolism, which is probably essential for all aerobic cells, likely proceeds via multiple mechanisms, including via a glutathione-dependent pathway that is widely conserved in bacteria, plants and animals. However, it is unclear whether the first step in the glutathione-dependent pathway (i.e. formation of S-hydroxymethylglutathione (HMG)) is enzyme-catalysed. We report studies on glutathione-dependent formaldehyde-activating enzyme (GFA) from Paracoccus denitrificans, which has been proposed to catalyse HMG formation from glutathione and formaldehyde on the basis of studies using NMR exchange spectroscopy (EXSY). Although we were able to replicate the EXSY results, time course experiments unexpectedly imply that GFA does not catalyse HMG formation under standard conditions. However, GFA was observed to bind glutathione using NMR and mass spectrometry. Overall, the results reveal that GFA binds glutathione but does not directly catalyse HMG formation under standard conditions. Thus, it is possible that GFA acts as a glutathione carrier that acts to co-localise glutathione and formaldehyde in a cellular context.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Carbono-Enxofre Ligases/química
Paracoccus denitrificans/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/metabolismo
Glutationa/análogos & derivados
Glutationa/metabolismo
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 32260-87-0 (S-hydroxymethylglutathione); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.- (glutathione-dependent formaldehyde-activating enzyme); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151218
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0145085


  4 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26195634
[Au] Autor:Yao J; Dodson VJ; Frank MW; Rock CO
[Ad] Endereço:From the Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
[Ti] Título:Chlamydia trachomatis Scavenges Host Fatty Acids for Phospholipid Synthesis via an Acyl-Acyl Carrier Protein Synthetase.
[So] Source:J Biol Chem;290(36):22163-73, 2015 Sep 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The obligate intracellular parasite Chlamydia trachomatis has a reduced genome but relies on de novo fatty acid and phospholipid biosynthesis to produce its membrane phospholipids. Lipidomic analyses showed that 8% of the phospholipid molecular species synthesized by C. trachomatis contained oleic acid, an abundant host fatty acid that cannot be made by the bacterium. Mass tracing experiments showed that isotopically labeled palmitic, myristic, and lauric acids added to the medium were incorporated into C. trachomatis-derived phospholipid molecular species. HeLa cells did not elongate lauric acid, but infected HeLa cell cultures elongated laurate to myristate and palmitate. The elongated fatty acids were incorporated exclusively into C. trachomatis-produced phospholipid molecular species. C. trachomatis has adjacent genes encoding the separate domains of the bifunctional acyl-acyl carrier protein (ACP) synthetase/2-acylglycerolphosphoethanolamine acyltransferase gene (aas) of Escherichia coli. The CT775 gene encodes an acyltransferase (LpaT) that selectively transfers fatty acids from acyl-ACP to the 1-position of 2-acyl-glycerophospholipids. The CT776 gene encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic acid in vitro. Exogenous fatty acids were elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo. These data point to an AasC-dependent pathway in C. trachomatis that selectively scavenges host saturated fatty acids to be used for the de novo synthesis of its membrane constituents.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/metabolismo
Chlamydia trachomatis/metabolismo
Ácidos Graxos/metabolismo
Fosfolipídeos/biossíntese
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Carbono-Enxofre Ligases/genética
Chlamydia trachomatis/genética
Chlamydia trachomatis/fisiologia
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Cinética
Ácido Oleico/metabolismo
Ácido Palmítico/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids); 0 (Phospholipids); 2UMI9U37CP (Oleic Acid); 2V16EO95H1 (Palmitic Acid); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150722
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.671008


  5 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26063393
[Au] Autor:Takatani N; Use K; Kato A; Ikeda K; Kojima K; Aichi M; Maeda S; Omata T
[Ad] Endereço:Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan Japan Science and Technology Agency, CREST.
[Ti] Título:Essential Role of Acyl-ACP Synthetase in Acclimation of the Cyanobacterium Synechococcus elongatus Strain PCC 7942 to High-Light Conditions.
[So] Source:Plant Cell Physiol;56(8):1608-15, 2015 Aug.
[Is] ISSN:1471-9053
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Most organisms capable of oxygenic photosynthesis have an aas gene encoding an acyl-acyl carrier protein synthetase (Aas), which activates free fatty acids (FFAs) via esterification to acyl carrier protein. Cyanobacterial aas mutants are often used for studies aimed at photosynthetic production of biofuels because the mutation leads to intracellular accumulation of FFAs and their secretion into the external medium, but the physiological significance of the production of FFAs and their recycling involving Aas has remained unclear. Using an aas-deficient mutant of Synechococcus elongatus strain PCC 7942, we show here that remodeling of membrane lipids is activated by high-intensity light and that the recycling of FFAs is essential for acclimation to high-light conditions. Unlike wild-type cells, the mutant cells could not increase their growth rate as the light intensity was increased from 50 to 400 µmol photons m(-2) s(-1), and the high-light-grown mutant cells accumulated FFAs and the lysolipids derived from all the four major classes of membrane lipids, revealing high-light-induced lipid deacylation. The high-light-grown mutant cells showed much lower PSII activity and Chl contents as compared with the wild-type cells or low-light-grown mutant cells. The loss of Aas accelerated photodamage of PSII but did not affect the repair process of PSII, indicating that PSII is destabilized in the mutant. Thus, Aas is essential for acclimation of the cyanobacterium to high-light conditions. The relevance of the present finding s to biofuel production using cyanobacteria is discussed.
[Mh] Termos MeSH primário: Carbono-Enxofre Ligases/metabolismo
Synechococcus/enzimologia
[Mh] Termos MeSH secundário: Aclimatação
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/genética
Ácidos Graxos não Esterificados/metabolismo
Luz
Lipídeos de Membrana/metabolismo
Mutação
Fotossíntese/fisiologia
Fotossíntese/efeitos da radiação
Complexo de Proteína do Fotossistema II/fisiologia
Complexo de Proteína do Fotossistema II/efeitos da radiação
Synechococcus/genética
Synechococcus/fisiologia
Synechococcus/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids, Nonesterified); 0 (Membrane Lipids); 0 (Photosystem II Protein Complex); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:150805
[Lr] Data última revisão:
150805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150612
[St] Status:MEDLINE
[do] DOI:10.1093/pcp/pcv086


  6 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25373341
[Au] Autor:Campopiano DJ
[Ad] Endereço:EaStChem School of Chemistry, Joseph Black Building, University of Edinburgh, David Brewster Road, King's Buildings, Edinburgh EH9 3FJ, Scotland. Electronic address: dominic.campopiano@ed.ac.uk.
[Ti] Título:ACP-AasS you like it.
[So] Source:Chem Biol;21(10):1257-1259, 2014 Oct 23.
[Is] ISSN:1879-1301
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl carrier proteins (ACPs) are promiscuous small proteins that play essential roles in the biosynthesis of many natural products, but our understanding of how they interact with various enzymes within larger protein complexes is lacking. In this issue of Chemistry and Biology, Beld and coworkers describe an enzymatic labeling method that will allow tracking of ACPs as they interact with their partners both in vitro and vivo.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/metabolismo
Vibrio/enzimologia
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 6.2.- (Carbon-Sulfur Ligases)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141107
[St] Status:MEDLINE


  7 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25308274
[Au] Autor:Beld J; Finzel K; Burkart MD
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA.
[Ti] Título:Versatility of acyl-acyl carrier protein synthetases.
[So] Source:Chem Biol;21(10):1293-1299, 2014 Oct 23.
[Is] ISSN:1879-1301
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The acyl carrier protein (ACP) requires posttranslational modification with a 4'-phosphopantetheine arm for activity, and this thiol-terminated modification carries cargo between enzymes in ACP-dependent metabolic pathways. We show that acyl-ACP synthetases (AasSs) from different organisms are able to load even, odd, and unnatural fatty acids onto E. coli ACP in vitro. Vibrio harveyi AasS not only shows promiscuity for the acid substrate, but also is active upon various alternate carrier proteins. AasS activity also extends to functional activation in living organisms. We show that exogenously supplied carboxylic acids are loaded onto ACP and extended by the E. coli fatty acid synthase, including unnatural fatty acid analogs. These analogs are further integrated into cellular lipids. In vitro characterization of four different adenylate-forming enzymes allowed us to disambiguate CoA-ligases and AasSs, and further in vivo studies show the potential for functional application in other organisms.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/metabolismo
Vibrio/enzimologia
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Proteínas de Bactérias/genética
Carbono-Enxofre Ligases/genética
Coenzima A Ligases/metabolismo
Escherichia coli/metabolismo
Ácidos Graxos/química
Ácidos Graxos/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Especificidade por Substrato
Synechocystis/enzimologia
Thermus thermophilus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids); 0 (Recombinant Proteins); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141014
[St] Status:MEDLINE


  8 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24866092
[Au] Autor:Bi H; Yu Y; Dong H; Wang H; Cronan JE
[Ad] Endereço:Department of Microbiology, B103 Chemical and Life Sciences Laboratory, University of Illinois, 601 S. Goodwin Ave, Urbana, IL, 61801, USA.
[Ti] Título:Xanthomonas campestris RpfB is a fatty Acyl-CoA ligase required to counteract the thioesterase activity of the RpfF diffusible signal factor (DSF) synthase.
[So] Source:Mol Microbiol;93(2):262-75, 2014 Jul.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In Xanthomonas campestris pv. campestris (Xcc), the proteins encoded by the rpf (regulator of pathogenicity factor) gene cluster produce and sense a fatty acid signal molecule called diffusible signalling factor (DSF, 2(Z)-11-methyldodecenoic acid). RpfB was reported to be involved in DSF processing and was predicted to encode an acyl-CoA ligase. We report that RpfB activates a wide range of fatty acids to their CoA esters in vitro. Moreover, RpfB can functionally replace the paradigm bacterial acyl-CoA ligase, Escherichia coli FadD, in the E. coli ß-oxidation pathway and deletion of RpfB from the Xcc genome results in a strain unable to utilize fatty acids as carbon sources. An essential RpfB function in the pathogenicity factor pathway was demonstrated by the properties of a strain deleted for both the rpfB and rpfC genes. The ΔrpfB ΔrpfC strain grew poorly and lysed upon entering stationary phase. Deletion of rpfF, the gene encoding the DSF synthetic enzyme, restored normal growth to this strain. RpfF is a dual function enzyme that synthesizes DSF by dehydration of a 3-hydroxyacyl-acyl carrier protein (ACP) fatty acid synthetic intermediate and also cleaves the thioester bond linking DSF to ACP. However, the RpfF thioesterase activity is of broad specificity and upon elimination of its RpfC inhibitor RpfF attains maximal activity and its thioesterase activity proceeds to block membrane lipid synthesis by cleavage of acyl-ACP intermediates. This resulted in release of the nascent acyl chains to the medium as free fatty acids. This lack of acyl chains for phospholipid synthesis results in cell lysis unless RpfB is present to counteract the RpfF thioesterase activity by catalysing uptake and activation of the free fatty acids to give acyl-CoAs that can be utilized to restore membrane lipid synthesis. Heterologous expression of a different fatty acid activating enzyme, the Vibrio harveyi acyl-ACP synthetase, replaced RpfB in counteracting the effects of high level RpfF thioesterase activity indicating that the essential role of RpfB is uptake and activation of free fatty acids.
[Mh] Termos MeSH primário: Coenzima A Ligases/metabolismo
Ácidos Graxos/metabolismo
Xanthomonas campestris/enzimologia
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Proteínas de Bactérias/metabolismo
Carbono-Enxofre Ligases/metabolismo
Coenzima A Ligases/genética
Coenzima A Ligases/isolamento & purificação
Difusão
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Proteínas de Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Genes Bacterianos
Teste de Complementação Genética
Enzimas Multifuncionais/metabolismo
Família Multigênica
Mutação
Oxirredução
Doenças das Plantas/microbiologia
Transdução de Sinais/genética
Especificidade por Substrato
Tioléster Hidrolases/metabolismo
Xanthomonas campestris/genética
Xanthomonas campestris/crescimento & desenvolvimento
Xanthomonas campestris/patogenicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Fatty Acids); 0 (Multifunctional Enzymes); EC 3.1.2.- (Thiolester Hydrolases); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (acyl-coenzyme A synthetase, E coli); EC 6.2.1.20 (long-chain-fatty-acid-(acyl-carrier-protein) ligase)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140529
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.12657


  9 / 55 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24831705
[Au] Autor:Menendez-Bravo S; Comba S; Sabatini M; Arabolaza A; Gramajo H
[Ad] Endereço:Microbiology Division, IBR (Instituto de Biología Molecular y Celular de Rosario), Consejo Nacional deInvestigaciones Científicas y Técnicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Ocampo y Esmeralda, 2000 Rosario, Argentina.
[Ti] Título:Expanding the chemical diversity of natural esters by engineering a polyketide-derived pathway into Escherichia coli.
[So] Source:Metab Eng;24:97-106, 2014 Jul.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:Microbial fatty acid (FA)-derived molecules have emerged as promising alternatives to petroleum-based chemicals for reducing dependence on fossil hydrocarbons. However, native FA biosynthetic pathways often yield limited structural diversity, and therefore restricted physicochemical properties, of the end products by providing only a limited variety of usually linear hydrocarbons. Here we have engineered into Escherichia coli a mycocerosic polyketide synthase-based biosynthetic pathway from Mycobacterium tuberculosis and redefined its biological role towards the production of multi-methyl-branched-esters (MBEs) with novel chemical structures. Expression of FadD28, Mas and PapA5 enzymes enabled the biosynthesis of multi-methyl-branched-FA and their further esterification to an alcohol. The high substrate tolerance of these enzymes towards different FA and alcohol moieties resulted in the biosynthesis of a broad range of MBE. Further metabolic engineering of the MBE producer strain coupled this system to long-chain-alcohol biosynthetic pathways resulting in de novo production of branched wax esters following addition of only propionate.
[Mh] Termos MeSH primário: Ésteres/metabolismo
Ácidos Graxos/metabolismo
Engenharia Metabólica
Mycobacterium tuberculosis
Policetídeos/metabolismo
[Mh] Termos MeSH secundário: Aciltransferases/biossíntese
Aciltransferases/genética
Carbono-Enxofre Ligases/biossíntese
Carbono-Enxofre Ligases/genética
Escherichia coli/enzimologia
Escherichia coli/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Esters); 0 (Fatty Acids); 0 (Polyketides); EC 2.3.- (Acyltransferases); EC 2.3.- (PapA5 protein, Mycobacterium tuberculosis); EC 6.2.- (Carbon-Sulfur Ligases); EC 6.2.1.- (FadD28 protein, Mycobacterium tuberculosis)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140707
[Lr] Data última revisão:
140707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140517
[St] Status:MEDLINE


  10 / 55 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24016264
[Au] Autor:Song H; Leninger M; Lee N; Liu P
[Ad] Endereço:Department of Chemistry, Boston University , Boston, Massachusetts 02215, United States.
[Ti] Título:Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses.
[So] Source:Org Lett;15(18):4854-7, 2013 Sep 20.
[Is] ISSN:1523-7052
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ergothioneine (5) and ovothiol (8) are two novel thiol-containing natural products. Their C-S bonds are formed by oxidative coupling reactions catalyzed by EgtB and OvoA enzymes, respectively. In this work, it was discovered that in addition to catalyzing the oxidative coupling between histidine and cysteine (1 → 6 conversion), OvoA can also catalyze a direct oxidative coupling between hercynine (2) and cysteine (2 → 4 conversion), which can shorten the ergothioneine biosynthetic pathway by two steps.
[Mh] Termos MeSH primário: Carbono-Enxofre Ligases/metabolismo
Ergotioneína/biossíntese
Metilistidinas/síntese química
[Mh] Termos MeSH secundário: Betaína/análogos & derivados
Betaína/química
Catálise
Cisteína/química
Ergotioneína/química
Ergotioneína/metabolismo
Histidina/análogos & derivados
Histidina/biossíntese
Histidina/química
Histidina/metabolismo
Metilistidinas/química
Metilistidinas/metabolismo
Estrutura Molecular
Oxirredução
Estereoisomerismo
Compostos de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Methylhistidines); 0 (Sulfhydryl Compounds); 105496-34-2 (ovothiol C); 3SCV180C9W (Betaine); 4QD397987E (Histidine); BDZ3DQM98W (Ergothioneine); EC 6.2.- (Carbon-Sulfur Ligases); K848JZ4886 (Cysteine); M8MWM6K25V (hercynine)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130911
[St] Status:MEDLINE
[do] DOI:10.1021/ol402275t



página 1 de 6 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