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Pesquisa : D08.811.913.817.200 [Categoria DeCS]
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[PMID]:29311546
[Au] Autor:Yang JE; Park SJ; Kim WJ; Kim HJ; Kim BJ; Lee H; Shin J; Lee SY
[Ad] Endereço:Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering (BK21 Plus Program), Center for Systems and Synthetic Biotechnology, Institute for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Repu
[Ti] Título:One-step fermentative production of aromatic polyesters from glucose by metabolically engineered Escherichia coli strains.
[So] Source:Nat Commun;9(1):79, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aromatic polyesters are widely used plastics currently produced from petroleum. Here we engineer Escherichia coli strains for the production of aromatic polyesters from glucose by one-step fermentation. When the Clostridium difficile isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase (HadA) and evolved polyhydroxyalkanoate (PHA) synthase genes are overexpressed in a D-phenyllactate-producing strain, poly(52.3 mol% 3-hydroxybutyrate (3HB)-co-47.7 mol% D-phenyllactate) can be produced from glucose and sodium 3HB. Also, various poly(3HB-co-D-phenyllactate) polymers having 11.0, 15.8, 20.0, 70.8, and 84.5 mol% of D-phenyllactate are produced from glucose as a sole carbon source by additional expression of Ralstonia eutropha ß-ketothiolase (phaA) and reductase (phaB) genes. Fed-batch culture of this engineered strain produces 13.9 g l of poly(61.9 mol% 3HB-co-38.1 mol% D-phenyllactate). Furthermore, different aromatic polyesters containing D-mandelate and D-3-hydroxy-3-phenylpropionate are produced from glucose when feeding the corresponding monomers. The engineered bacterial system will be useful for one-step fermentative production of aromatic polyesters from renewable resources.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Fermentação
Glucose/metabolismo
Engenharia Metabólica/métodos
Poliésteres/metabolismo
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/metabolismo
Acetil-CoA C-Aciltransferase/genética
Acetil-CoA C-Aciltransferase/metabolismo
Aciltransferases/genética
Aciltransferases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clostridium difficile/enzimologia
Clostridium difficile/genética
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Cupriavidus necator/enzimologia
Cupriavidus necator/genética
Escherichia coli/genética
Lactatos/metabolismo
Oxirredutases/genética
Oxirredutases/metabolismo
Polietilenotereftalatos/metabolismo
Polímeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lactates); 0 (Polyesters); 0 (Polyethylene Terephthalates); 0 (Polymers); 156-05-8 (3-phenyllactic acid); EC 1.- (Oxidoreductases); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.8.3.- (Coenzyme A-Transferases); IY9XDZ35W2 (Glucose); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02498-w


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[PMID]:28684065
[Au] Autor:Zhang S; Xie C
[Ad] Endereço:School of Life Sciences, Nanchang University, Nanchang, Jiangxi, PR China; Institute of Translational Medicine, Nanchang University, Nanchang, Jiangxi 330031, PR China.
[Ti] Título:The role of OXCT1 in the pathogenesis of cancer as a rate-limiting enzyme of ketone body metabolism.
[So] Source:Life Sci;183:110-115, 2017 Aug 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cancer cells are well documented to reprogram their metabolism in order to support the maintenance and reproduction. 3-oxoacid CoA-transferase 1 (OXCT1) is a key enzyme in ketone body metabolism that catalyzes the first and rate-determining step of ketolysis. The product of OXCT1 converts to acetyl-CoA and finally fed into the tricarboxylic acid cycle for oxidation and ATP production. However, little is known of its regulation right now. Recently, some studies suggested that OXCT1 participates in tumorigenesis and signaling in cancer cells. Furthermore, our recent work showed that a marked elevation of OXCT1 expression in different categories of cancer cells. Here we review the metabolic functions of OXCT1 and its surprising roles in supporting the biological hallmarks of malignancy. We also review recent efforts in exploring the mechanism responsible for the tumor promoting effect of OXCT1 and suggest a novel therapeutic target for cancer therapy.
[Mh] Termos MeSH primário: Coenzima A-Transferases/metabolismo
Cetonas/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Coenzima A-Transferases/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias/genética
Neoplasias/patologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ketones); 72-89-9 (Acetyl Coenzyme A); 8L70Q75FXE (Adenosine Triphosphate); EC 2.8.3.- (Coenzyme A-Transferases); EC 2.8.3.5 (3-ketoacid CoA-transferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


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[PMID]:28683918
[Au] Autor:Dey M
[Ad] Endereço:The University of Iowa, Iowa City, IA, United States. Electronic address: mishtu-dey@uiowa.edu.
[Ti] Título:Enzymology of Microbial Dimethylsulfoniopropionate Catabolism.
[So] Source:Adv Protein Chem Struct Biol;109:195-222, 2017.
[Is] ISSN:1876-1623
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The biochemistry of dimethylsulfoniopropionate (DMSP) catabolism is reviewed. The microbes that catalyze the reactions central to DMSP catabolic pathways are described, and the focus is on the enzymology of the process. Approximately 10 tons of DMSP is released annually by marine eukaryotes as an osmolyte. A vast majority of DMSP is assimilated by bacteria through either a demethylation or lyase pathways, producing either the methane thiol or the volatile dimethylsulfide (DMS), respectively. Enzymatic breakdown of DMSP generates ~10 tons of DMS annually, which may have impact on global climate. DMS also acts as a chemoattractant for zooplanktons and seabirds. Both DMSP and DMS play a key role in the global sulfur cycle and are key nutrients for marine microbial growth. Important enzymes in the biochemical pathways of DMSP catabolism are covered in this review, with a focus on the latest developments in their mechanism.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Compostos de Sulfônio/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bactérias/química
Bactérias/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Coenzima A-Transferases/química
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Regulação Bacteriana da Expressão Gênica
Liases/química
Liases/genética
Liases/metabolismo
Redes e Vias Metabólicas
Modelos Moleculares
Conformação Proteica
Proteobactérias/química
Proteobactérias/enzimologia
Proteobactérias/genética
Proteobactérias/metabolismo
Compostos de Sulfônio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Sulfonium Compounds); C884XA7QGG (dimethylpropiothetin); EC 2.8.3.- (Coenzyme A-Transferases); EC 4.- (Lyases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


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[PMID]:27392087
[Au] Autor:Ebenau-Jehle C; Mergelsberg M; Fischer S; Brüls T; Jehmlich N; von Bergen M; Boll M
[Ad] Endereço:University of Freiburg, Institute for Biology II, Freiburg, Germany.
[Ti] Título:An unusual strategy for the anoxic biodegradation of phthalate.
[So] Source:ISME J;11(1):224-236, 2017 Jan.
[Is] ISSN:1751-7370
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the past two decades, the study of oxygen-independent degradation of widely abundant aromatic compounds in anaerobic bacteria has revealed numerous unprecedented enzymatic principles. Surprisingly, the organisms, metabolites and enzymes involved in the degradation of o-phthalate (1,2-dicarboxybenzene), mainly derived from phthalate esters that are annually produced at the million ton scale, are sparsely known. Here, we demonstrate a previously unknown capacity of complete phthalate degradation in established aromatic compound-degrading, denitrifying model organisms of the genera Thauera, Azoarcus and 'Aromatoleum'. Differential proteome analyses revealed phthalate-induced gene clusters involved in uptake and conversion of phthalate to the central intermediate benzoyl-CoA. Enzyme assays provided in vitro evidence for the formation of phthaloyl-CoA by a succinyl-CoA- and phthalate-specific CoA transferase, which is essential for the subsequent oxygen-sensitive decarboxylation to benzoyl-CoA. The extreme instability of the phthaloyl-CoA intermediate requires highly balanced CoA transferase and decarboxylase activities to avoid its cellular accumulation. Phylogenetic analysis revealed phthaloyl-CoA decarboxylase as a novel member of the UbiD-like, (de)carboxylase enzyme family. Homologs of the encoding gene form a phylogenetic cluster and are found in soil, freshwater and marine bacteria; an ongoing global distribution of a possibly only recently evolved degradation pathway is suggested.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Ácidos Ftálicos/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/genética
Acil Coenzima A/metabolismo
Anaerobiose
Bactérias/classificação
Bactérias/genética
Bactérias/isolamento & purificação
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biodegradação Ambiental
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Família Multigênica
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Phthalic Acids); 604-98-8 (succinyl-coenzyme A); 6756-74-7 (benzoyl-coenzyme A); 6O7F7IX66E (phthalic acid); EC 2.8.3.- (Coenzyme A-Transferases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1038/ismej.2016.91


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[PMID]:27707801
[Au] Autor:Zeman I; Nebohácová M; Gérecová G; Katonová K; Jánosíková E; Jakúbková M; Centárová I; Duncková I; Tomáska L; Pryszcz LP; Gabaldón T; Nosek J
[Ad] Endereço:Department of Biochemistry, Comenius University in Bratislava, Faculty of Natural Sciences, 842 15, Slovak Republic nosek@fns.uniba.sk.
[Ti] Título:Mitochondrial Carriers Link the Catabolism of Hydroxyaromatic Compounds to the Central Metabolism in Candida parapsilosis.
[So] Source:G3 (Bethesda);6(12):4047-4058, 2016 Dec 07.
[Is] ISSN:2160-1836
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pathogenic yeast Candida parapsilosis metabolizes hydroxyderivatives of benzene and benzoic acid to compounds channeled into central metabolism, including the mitochondrially localized tricarboxylic acid cycle, via the 3-oxoadipate and gentisate pathways. The orchestration of both catabolic pathways with mitochondrial metabolism as well as their evolutionary origin is not fully understood. Our results show that the enzymes involved in these two pathways operate in the cytoplasm with the exception of the mitochondrially targeted 3-oxoadipate CoA-transferase (Osc1p) and 3-oxoadipyl-CoA thiolase (Oct1p) catalyzing the last two reactions of the 3-oxoadipate pathway. The cellular localization of the enzymes indicates that degradation of hydroxyaromatic compounds requires a shuttling of intermediates, cofactors, and products of the corresponding biochemical reactions between cytosol and mitochondria. Indeed, we found that yeast cells assimilating hydroxybenzoates increase the expression of genes SFC1, LEU5, YHM2, and MPC1 coding for succinate/fumarate carrier, coenzyme A carrier, oxoglutarate/citrate carrier, and the subunit of pyruvate carrier, respectively. A phylogenetic analysis uncovered distinct evolutionary trajectories for sparsely distributed gene clusters coding for enzymes of both pathways. Whereas the 3-oxoadipate pathway appears to have evolved by vertical descent combined with multiple losses, the gentisate pathway shows a striking pattern suggestive of horizontal gene transfer to the evolutionarily distant Mucorales.
[Mh] Termos MeSH primário: Ascomicetos/metabolismo
Hidrocarbonetos Aromáticos/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/genética
Acetil-CoA C-Aciltransferase/metabolismo
Ascomicetos/classificação
Ascomicetos/genética
Evolução Biológica
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Regulação Fúngica da Expressão Gênica
Redes e Vias Metabólicas
Mitocôndrias/genética
Mutação
Filogenia
Transporte Proteico
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Hydrocarbons, Aromatic); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.174 (3-oxoadipyl-coenzyme A thiolase); EC 2.8.3.- (Coenzyme A-Transferases); EC 2.8.3.6 (3-oxoadipate CoA-transferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161007
[St] Status:MEDLINE
[do] DOI:10.1534/g3.116.034389


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[PMID]:27613689
[Au] Autor:Trachsel J; Bayles DO; Looft T; Levine UY; Allen HK
[Ad] Endereço:Food Safety and Enteric Pathogens Research Unit, National Animal Disease Center, Agricultural Research Service, Ames, Iowa, USA Interdepartmental Microbiology Graduate Program, Iowa State University, Ames, Iowa, USA.
[Ti] Título:Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate Transferases and Their Diversity in the Proximal Colon of Swine.
[So] Source:Appl Environ Microbiol;82(22):6788-6798, 2016 Nov 15.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Studying the host-associated butyrate-producing bacterial community is important, because butyrate is essential for colonic homeostasis and gut health. Previous research has identified the butyryl coenzyme A (CoA):acetate-CoA transferase (EC 2.3.8.3) as a gene of primary importance for butyrate production in intestinal ecosystems; however, this gene family (but) remains poorly defined. We developed tools for the analysis of butyrate-producing bacteria based on 12 putative but genes identified in the genomes of nine butyrate-producing bacteria obtained from the swine intestinal tract. Functional analyses revealed that eight of these genes had strong But enzyme activity. When but paralogues were found within a genome, only one gene per genome encoded strong activity, with the exception of one strain in which no gene encoded strong But activity. Degenerate primers were designed to amplify the functional but genes and were tested by amplifying environmental but sequences from DNA and RNA extracted from swine colonic contents. The results show diverse but sequences from swine-associated butyrate-producing bacteria, most of which clustered near functionally confirmed sequences. Here, we describe tools and a framework that allow the bacterial butyrate-producing community to be profiled in the context of animal health and disease. IMPORTANCE: Butyrate is a compound produced by the microbiota in the intestinal tracts of animals. This compound is of critical importance for intestinal health, and yet studying its production by diverse intestinal bacteria is technically challenging. Here, we present an additional way to study the butyrate-producing community of bacteria using one degenerate primer set that selectively targets genes experimentally demonstrated to encode butyrate production. This work will enable researchers to more easily study this very important bacterial function that has implications for host health and resistance to disease.
[Mh] Termos MeSH primário: Acil Coenzima A/genética
Bactérias/enzimologia
Butiratos/metabolismo
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Colo/microbiologia
Suínos/microbiologia
[Mh] Termos MeSH secundário: Acetatos/metabolismo
Acil Coenzima A/classificação
Acil Coenzima A/metabolismo
Animais
Bactérias/genética
Bactérias/isolamento & purificação
Coenzima A-Transferases/classificação
Primers do DNA
Fezes/microbiologia
Genes Bacterianos
Genoma Bacteriano
Microbiota/genética
Microbiota/fisiologia
Filogenia
RNA Ribossômico 16S
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Acyl Coenzyme A); 0 (Butyrates); 0 (DNA Primers); 0 (RNA, Ribosomal, 16S); 2140-48-9 (butyryl-coenzyme A); EC 2.8.3.- (Coenzyme A-Transferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE


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[PMID]:27342638
[Au] Autor:Tajima K; Han X; Hashimoto Y; Satoh Y; Satoh T; Taguchi S
[Ad] Endereço:Division of Applied Chemistry, Faculty of Engineering, Hokkaido University, N13W8, Kita-ku, Sapporo 060-8628, Japan. Electronic address: ktajima@eng.hokudai.ac.jp.
[Ti] Título:In vitro synthesis of polyhydroxyalkanoates using thermostable acetyl-CoA synthetase, CoA transferase, and PHA synthase from thermotorelant bacteria.
[So] Source:J Biosci Bioeng;122(6):660-665, 2016 Dec.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Thermostable enzymes are required for the rapid and sustainable production of polyhydroxyalkanoate (PHA) in vitro. The in vitro synthesis of PHA using the engineered thermostable synthase PhaC1 (STQK) has been reported; however, the non-thermostable enzymes acetyl-CoA synthetase (ACS) and CoA transferase (CT) from mesophilic strains were used as monomer-supplying enzymes in this system. In the present study, acs and ct were cloned from the thermophilic bacteria Pelotomaculum thermopropionicum JCM10971 and Thermus thermophilus JCM10941 to construct an in vitro PHA synthesis system using only thermostable enzymes. ACS from P. thermopropionicum (ACS ) and CT from T. thermophilus (CT ) were confirmed to have high thermostability, and their optimal temperatures were around 60°C and 75°C, respectively. The in vitro PHA synthesis was successfully performed by ACS , CT , PhaC1 (STQK), and poly(3-hydroxybutyrate) [P(3HB)] was synthesized at 45°C. Furthermore, the yields of P(3HB) and P(lactate-co-3HB) at 37°C were 1.4-fold higher than those of the in vitro synthesis system with non-thermostable ACS and CT from mesophilic strains. Overall, the thermostable ACS and CT were demonstrated to be useful for the efficient in vitro PHA synthesis at relatively high temperatures.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Aciltransferases/metabolismo
Coenzima A-Transferases/metabolismo
Peptococcaceae/enzimologia
Poli-Hidroxialcanoatos/biossíntese
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/metabolismo
Acetato-CoA Ligase/isolamento & purificação
Acetilcoenzima A/metabolismo
Aciltransferases/isolamento & purificação
Coenzima A-Transferases/isolamento & purificação
Estabilidade Enzimática
Hidroxibutiratos/metabolismo
Ácido Láctico/metabolismo
Peptococcaceae/metabolismo
Poliésteres/metabolismo
Temperatura Ambiente
Thermus thermophilus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydroxybutyrates); 0 (Polyesters); 0 (Polyhydroxyalkanoates); 26063-00-3 (poly-beta-hydroxybutyrate); 33X04XA5AT (Lactic Acid); 72-89-9 (Acetyl Coenzyme A); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 2.8.3.- (Coenzyme A-Transferases); EC 6.2.1.1 (Acetate-CoA Ligase); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160626
[St] Status:MEDLINE


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[PMID]:27216458
[Au] Autor:Nagao M; Toh R; Irino Y; Mori T; Nakajima H; Hara T; Honjo T; Satomi-Kobayashi S; Shinke T; Tanaka H; Ishida T; Hirata K
[Ad] Endereço:Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University, Graduate School of Medicine, Japan.
[Ti] Título:ß-Hydroxybutyrate elevation as a compensatory response against oxidative stress in cardiomyocytes.
[So] Source:Biochem Biophys Res Commun;475(4):322-8, 2016 07 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown that the ketone body ß-hydroxybutyrate (ßOHB) acts not only as a carrier of energy but also as a signaling molecule that has a role in diverse cellular functions. Circulating levels of ketone bodies have been previously reported to be increased in patients with congestive heart failure (HF). In this study, we investigated regulatory mechanism and pathophysiological role of ßOHB in HF. First, we revealed that ßOHB level was elevated in failing hearts, but not in blood, using pressure-overloaded mice. We also measured cellular ßOHB levels in both cardiomyocytes and non-cardiomyocytes stimulated with or without H2O2 and revealed that increased myocardial ßOHB was derived from cardiomyocytes but not non-cardiomyocytes under pathological states. Next, we sought to elucidate the mechanisms of myocardial ßOHB elevation and its implication under pathological states. The gene and protein expression levels of CoA transferase (SCOT), a key enzyme involved in ketone body oxidation, was decreased in failing hearts. In cardiomyocytes, H2O2 stimulation caused ßOHB accumulation concomitantly with SCOT downregulation, implying that the accumulation of myocardial ßOHB occurs because of the decline in its utilization. Finally, we checked the effects of ßOHB on cardiomyocytes under oxidative stress. We found that ßOHB induced FOXO3a, an oxidative stress resistance gene, and its target enzyme, SOD2 and catalase. Consequently, ßOHB attenuated reactive oxygen species production and alleviated apoptosis induced by oxidative stress. It has been reported that hyperadrenergic state in HF boost lipolysis and result in elevation of circulating free fatty acids, which can lead hepatic ketogenesis for energy metabolism alteration. The present findings suggest that the accumulation of ßOHB also occurs as a compensatory response against oxidative stress in failing hearts.
[Mh] Termos MeSH primário: Ácido 3-Hidroxibutírico/metabolismo
Miócitos Cardíacos/metabolismo
Miócitos Cardíacos/patologia
Estresse Oxidativo
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/análise
Animais
Células Cultivadas
Coenzima A-Transferases/metabolismo
Peróxido de Hidrogênio/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Miocárdio/metabolismo
Miocárdio/patologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
BBX060AN9V (Hydrogen Peroxide); EC 2.8.3.- (Coenzyme A-Transferases); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160525
[St] Status:MEDLINE


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[PMID]:27102732
[Au] Autor:Schühle K; Nies J; Heider J
[Ad] Endereço:Laboratory for Microbiology, Philipps-Universität Marburg, Karl-von-Frisch-Straße 8, 35043, Marburg, Germany.
[Ti] Título:An indoleacetate-CoA ligase and a phenylsuccinyl-CoA transferase involved in anaerobic metabolism of auxin.
[So] Source:Environ Microbiol;18(9):3120-32, 2016 Sep.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The plant hormone auxin (indoleacetate) is anaerobically degraded by the Betaproteobacterium Aromatoleum aromaticum. We report here on a CoA ligase (IaaB) and a CoA-transferase (IaaL) which are encoded in the apparent substrate-induced iaa operon containing genes for indoleacetate degradation. IaaB is a highly specific indoleacetate-CoA ligase which activates indoleacetate to the CoA-thioester immediately after uptake into the cytoplasm. This enzyme only activates indoleacetate and some closely related compounds such as naphthylacetate, phenylacetate and indolepropionate, and is inhibited by high concentrations of substrates, and by the synthetic auxin compound 2,4-dichlorophenoxyacetate, which does not serve as substrate. IaaL is a CoA-transferase recognizing several C4-dicarboxylic acids, such as succinate, phenylsuccinate or benzylsuccinate and their CoA-thioesters, but only few monocarboxylic acids and no C3-dicarboxylic acids such as benzylmalonate. The enzyme shows no stereospecific discrimation of the benzylsuccinate enantiomers. Moreover, benzylsuccinate is regiospecifically activated to 2-benzylsuccinyl-CoA, whereas phenylsuccinate is converted to an equal mixture of both regioisomers (2- and 3-phenylsuccinyl-CoA). The identification of these two enzymes allows us to set up a modified version of the metabolic pathway of anaerobic indoleacetate degradation and to investigate the sequences databases for the occurrence and distribution of this pathway in other microorgansisms.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Coenzima A-Transferases/metabolismo
Ácidos Indolacéticos/metabolismo
Ligases/metabolismo
Rhodocyclaceae/enzimologia
Succinatos/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Proteínas de Bactérias/genética
Coenzima A-Transferases/genética
Ácidos Dicarboxílicos/metabolismo
Ligases/genética
Redes e Vias Metabólicas
Rhodocyclaceae/genética
Rhodocyclaceae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Dicarboxylic Acids); 0 (Indoleacetic Acids); 0 (Succinates); 103-40-2 (benzylsuccinate); 635-51-8 (2-phenylsuccinate); 6U1S09C61L (indoleacetic acid); EC 2.8.3.- (Coenzyme A-Transferases); EC 6.- (Ligases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160423
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13347


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[PMID]:27102125
[Au] Autor:Chen M; Huang X; Zhong C; Li J; Lu X
[Ad] Endereço:Key Laboratory of Biofuels, Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.
[Ti] Título:Identification of an itaconic acid degrading pathway in itaconic acid producing Aspergillus terreus.
[So] Source:Appl Microbiol Biotechnol;100(17):7541-8, 2016 Sep.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Itaconic acid, one of the most promising and flexible bio-based chemicals, is mainly produced by Aspergillus terreus. Previous studies to improve itaconic acid production in A. terreus through metabolic engineering were mainly focused on its biosynthesis pathway, while the itaconic acid-degrading pathway has largely been ignored. In this study, we used transcriptomic, proteomic, bioinformatic, and in vitro enzymatic analyses to identify three key enzymes, itaconyl-CoA transferase (IctA), itaconyl-CoA hydratase (IchA), and citramalyl-CoA lyase (CclA), that are involved in the catabolic pathway of itaconic acid in A. terreus. In the itaconic acid catabolic pathway in A. terreus, itaconic acid is first converted by IctA into itaconyl-CoA with succinyl-CoA as the CoA donor, and then itaconyl-CoA is hydrated into citramalyl-CoA by IchA. Finally, citramalyl-CoA is cleaved into acetyl-CoA and pyruvate by CclA. Moreover, IctA can also catalyze the reaction between citramalyl-CoA and succinate to generate succinyl-CoA and citramalate. These results, for the first time, identify the three key enzymes, IctA, IchA, and CclA, involved in the itaconic acid degrading pathway in itaconic acid producing A. terreus. The results will facilitate the improvement of itaconic acid production by metabolically engineering the catabolic pathway of itaconic acid in A. terreus.
[Mh] Termos MeSH primário: Aspergillus/metabolismo
Vias Biossintéticas/fisiologia
Carbono-Carbono Liases/metabolismo
Coenzima A-Transferases/metabolismo
Proteínas Fúngicas/metabolismo
Hidroliases/metabolismo
Succinatos/metabolismo
[Mh] Termos MeSH secundário: Engenharia Metabólica
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Succinates); EC 2.8.3.- (Coenzyme A-Transferases); EC 4.1.- (Carbon-Carbon Lyases); EC 4.2.1.- (Hydro-Lyases); Q4516562YH (itaconic acid)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160423
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7554-0



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