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Pesquisa : D08.811.913.050.170 [Categoria DeCS]
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[PMID]:27598417
[Au] Autor:Ishikawa F; Sugimoto H; Kakeya H
[Ad] Endereço:Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto, 606-8501, Japan.
[Ti] Título:In Vitro Investigation of Crosstalk between Fatty Acid and Polyketide Synthases in the Andrimid Biosynthetic Assembly Line.
[So] Source:Chembiochem;17(22):2137-2142, 2016 Nov 17.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Andrimid (Adm) synthase, which belongs to the type II system of enzymes, produces Adm in Pantoea agglomerans. The adm biosynthetic gene cluster lacks canonical acyltransferases (ATs) to load the malonyl group to acyl carrier proteins (ACPs), thus suggesting that a malonyl-CoA ACP transacylase (MCAT) from the fatty acid synthase (FAS) complex provides the essential AT activity in Adm biosynthesis. Here we report that an MCAT is essential for catalysis of the transacylation of malonate from malonyl-CoA to AdmA polyketide synthase (PKS) ACP in vitro. Catalytic self-malonylation of AdmA (PKS ACP) was not observed in reactions without MCAT, although many type II PKS ACPs are capable of catalyzing self-acylation. This lack of self-malonylation was explained by amino acid sequence analysis of the AdmA PKS ACP and the type II PKS ACPs. The results show that MCAT from the organism's FAS complex can provide the missing AT activity in trans, thus suggesting a protein-protein interaction between the fatty acid and polyketide synthases in the Adm assembly line.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Proteínas de Bactérias/metabolismo
Ácido Graxo Sintases/metabolismo
Policetídeo Sintases/metabolismo
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Maloniltransferase/genética
Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Antibacterianos/análise
Antibacterianos/química
Proteínas de Bactérias/genética
Escherichia coli/enzimologia
Escherichia coli/genética
Ácido Graxo Sintases/genética
Família Multigênica
Pantoea/enzimologia
Pantoea/genética
Polienos/análise
Polienos/química
Polienos/metabolismo
Policetídeo Sintases/genética
Domínios e Motivos de Interação entre Proteínas
Pirróis/análise
Pirróis/química
Pirróis/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Polyenes); 0 (Pyrroles); 0 (Recombinant Proteins); 108868-95-7 (andrimid); 79956-01-7 (Polyketide Synthases); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.85 (Fatty Acid Synthases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160907
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600410


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[PMID]:27116968
[Au] Autor:Liang JL; Guo LQ; Lin JF; He ZQ; Cai FJ; Chen JF
[Ad] Endereço:Department of Bioengineering, College of Food Science and Institute of Food Biotechnology, South China Agricultural University, 483 Wushan Road, Tianhe District, Guangzhou, 510640, China.
[Ti] Título:A novel process for obtaining pinosylvin using combinatorial bioengineering in Escherichia coli.
[So] Source:World J Microbiol Biotechnol;32(6):102, 2016 Jun.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Pinosylvin as a bioactive stilbene is of great interest for food supplements and pharmaceuticals development. In comparison to conventional extraction of pinosylvin from plant sources, biosynthesis engineering of microbial cell factories is a sustainable and flexible alternative method. Current synthetic strategies often require expensive phenylpropanoic precursor and inducer, which are not available for large-scale fermentation process. In this study, three bioengineering strategies were described to the development of a simple and economical process for pinosylvin biosynthesis in Escherichia coli. Firstly, we evaluated different construct environments to give a highly efficient constitutive system for enzymes of pinosylvin pathway expression: 4-coumarate: coenzyme A ligase (4CL) and stilbene synthase (STS). Secondly, malonyl coenzyme A (malonyl-CoA) is a key precursor of pinosylvin bioproduction and at low level in E. coli cell. Thus clustered regularly interspaced short palindromic repeats interference (CRISPRi) was explored to inactivate malonyl-CoA consumption pathway to increase its availability. The resulting pinosylvin content in engineered E. coli was obtained a 1.9-fold increase depending on the repression of fabD (encoding malonyl-CoA-ACP transacylase) gene. Eventually, a phenylalanine over-producing E. coli consisting phenylalanine ammonia lyase was introduced to produce the precursor of pinosylvin, trans-cinnamic acid, the crude extraction of cultural medium was used as supplementation for pinosylvin bioproduction. Using these combinatorial processes, 47.49 mg/L pinosylvin was produced from glycerol.
[Mh] Termos MeSH primário: Bioengenharia/métodos
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Estilbenos/metabolismo
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Maloniltransferase/biossíntese
Proteína de Transporte de Acila S-Maloniltransferase/genética
Aciltransferases/metabolismo
Cinamatos/química
Coenzima A Ligases/metabolismo
Ácidos Cumáricos/metabolismo
Escherichia coli/enzimologia
Proteínas de Escherichia coli/biossíntese
Proteínas de Escherichia coli/química
Ácido Graxo Sintase Tipo II/biossíntese
Ácido Graxo Sintase Tipo II/genética
Ácidos Graxos/biossíntese
Glicerol/metabolismo
Malonil Coenzima A/metabolismo
Fenilalanina/metabolismo
Estilbenos/química
Estilbenos/economia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cinnamates); 0 (Coumaric Acids); 0 (Escherichia coli Proteins); 0 (Fatty Acids); 0 (Stilbenes); 47E5O17Y3R (Phenylalanine); 524-14-1 (Malonyl Coenzyme A); 881R434AIB (pinosylvin); EC 2.3.- (Acyltransferases); EC 2.3.1.- (stilbene synthase); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.39 (fabD protein, E coli); EC 6.- (Fatty Acid Synthase, Type II); EC 6.2.1.- (Coenzyme A Ligases); PDC6A3C0OX (Glycerol); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160428
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-016-2062-z


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[PMID]:26008118
[Au] Autor:Marcella AM; Jing F; Barb AW
[Ad] Endereço:Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, United States.
[Ti] Título:Preparation of holo- and malonyl-[acyl-carrier-protein] in a manner suitable for analog development.
[So] Source:Protein Expr Purif;115:39-45, 2015 Nov.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The fatty acid biosynthetic pathway generates highly reduced carbon based molecules. For this reason fatty acid synthesis is a target of pathway engineering to produce novel specialty or commodity chemicals using renewable techniques to supplant molecules currently derived from petroleum. Malonyl-[acyl carrier protein] (malonyl-ACP) is a key metabolite in the fatty acid pathway and donates two carbon units to the growing fatty acid chain during each step of biosynthesis. Attempts to test engineered fatty acid biosynthesis enzymes in vitro will require malonyl-ACP or malonyl-ACP analogs. Malonyl-ACP is challenging to prepare due to the instability of the carboxylate leaving group and the multiple steps of post-translational modification required to activate ACP. Here we report the expression and purification of holo- and malonyl-ACP from Escherichia coli with high yields (>15 mg per L of expression). The malonyl-ACP is efficiently recognized by the E. coli keto-acyl synthase enzyme, FabH. A FabH assay using malonyl-ACP and a coumarin-based fluorescent reagent is described that provides a high throughput alternative to reported radioactive assays.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Proteína de Transporte de Acila/química
Proteína de Transporte de Acila/metabolismo
Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Proteínas de Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Proteína de Transporte de Acila S-Maloniltransferase/genética
Escherichia coli
Proteínas de Escherichia coli/genética
Ácido Graxo Sintase Tipo II/genética
Ácido Graxo Sintase Tipo II/metabolismo
Redes e Vias Metabólicas
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Escherichia coli Proteins); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.180 (fabH protein, E coli); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.39 (fabD protein, E coli); EC 6.- (Fatty Acid Synthase, Type II)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150919
[Lr] Data última revisão:
150919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE


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[PMID]:25863265
[Au] Autor:Yang Y; Lin Y; Li L; Linhardt RJ; Yan Y
[Ad] Endereço:College of Engineering, University of Georgia, Athens, GA 30602, USA.
[Ti] Título:Regulating malonyl-CoA metabolism via synthetic antisense RNAs for enhanced biosynthesis of natural products.
[So] Source:Metab Eng;29:217-26, 2015 May.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:Malonyl-CoA is the building block for fatty acid biosynthesis and also a precursor to various pharmaceutically and industrially valuable molecules, such as polyketides and biopolymers. However, intracellular malonyl-CoA is usually maintained at low levels, which poses great challenges to efficient microbial production of malonyl-CoA derived molecules. Inactivation of the malonyl-CoA consumption pathway to increase its intracellular availability is not applicable, since it is usually lethal to microorganisms. In this work, we employ synthetic antisense RNAs (asRNAs) to conditionally down-regulate fatty acid biosynthesis and achieve malonyl-CoA enrichment in Escherichia coli. The optimized asRNA constructs with a loop-stem structure exhibit high interference efficiency up to 80%, leading to a 4.5-fold increase in intracellular malonyl-CoA concentration when fabD gene expression is inhibited. Strikingly, this strategy allows the improved production of natural products 4-hydroxycoumarin, resveratrol, and naringenin by 2.53-, 1.70-, and 1.53-fold in E. coli, respectively. In addition, down-regulation of other fab genes including fabH, fabB, and fabF also leads to remarkable increases in 4-hydroxycoumarin production. This study demonstrates a novel strategy to enhance intracellular malonyl-CoA and indicates the effectiveness of asRNA as a powerful tool for use in metabolic engineering.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/biossíntese
Proteínas de Escherichia coli/biossíntese
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Malonil Coenzima A
RNA Antissenso
[Mh] Termos MeSH secundário: Ácido Graxo Sintase Tipo II/biossíntese
Malonil Coenzima A/genética
Malonil Coenzima A/metabolismo
RNA Antissenso/biossíntese
RNA Antissenso/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (RNA, Antisense); 524-14-1 (Malonyl Coenzyme A); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.39 (fabD protein, E coli); EC 6.- (Fatty Acid Synthase, Type II)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150513
[Lr] Data última revisão:
150513
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150412
[St] Status:MEDLINE


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[PMID]:25582772
[Au] Autor:Liu Y; Feng Y; Wang Y; Li X; Cao X; Xue S
[Ad] Endereço:Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
[Ti] Título:Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism.
[So] Source:Biochem Biophys Res Commun;457(3):398-403, 2015 Feb 13.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Malonyl-coenzyme A: acyl-carrier protein transacylase (MCAT) catalyzes the transfer of malonyl group from malonyl-CoA to the holo-acyl carrier protein (Holo-ACP), yielding malonyl-ACP. The overall reaction has been extensively studied in heterotrophic microorganisms, while its mechanism in photosynthetic autotrophs as well as the stepwise reaction information remains unclear. Here the 2.42 Å crystal structure of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 is presented. It demonstrates that Arg113, Ser88 and His188 constitute catalytic triad. The second step involved ACP-MCAT-malonyl intermediate is speed-limited instead of the malonyl-CoA-MCAT intermediate in the first step. Therefore His87, Arg113 and Ser88 render different contributions for the two intermediates. Additionally, S88T mutant initializes the reaction by H87 deprotonating S88T which is different from the wild type.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/química
Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Synechocystis/enzimologia
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Maloniltransferase/genética
Sequência de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/genética
Catálise
Domínio Catalítico
Sequência Conservada
Cristalografia por Raios X
Modelos Moleculares
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Conformação Proteica
Homologia de Sequência de Aminoácidos
Synechocystis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:150216
[Lr] Data última revisão:
150216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150114
[St] Status:MEDLINE


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[PMID]:25360565
[Au] Autor:Beld J; Lee DJ; Burkart MD
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA. mburkart@ucsd.edu.
[Ti] Título:Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.
[So] Source:Mol Biosyst;11(1):38-59, 2015 Jan.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fatty acids are primary metabolites synthesized by complex, elegant, and essential biosynthetic machinery. Fatty acid synthases resemble an iterative assembly line, with an acyl carrier protein conveying the growing fatty acid to necessary enzymatic domains for modification. Each catalytic domain is a unique enzyme spanning a wide range of folds and structures. Although they harbor the same enzymatic activities, two different types of fatty acid synthase architectures are observed in nature. During recent years, strained petroleum supplies have driven interest in engineering organisms to either produce more fatty acids or specific high value products. Such efforts require a fundamental understanding of the enzymatic activities and regulation of fatty acid synthases. Despite more than one hundred years of research, we continue to learn new lessons about fatty acid synthases' many intricate structural and regulatory elements. In this review, we summarize each enzymatic domain and discuss efforts to engineer fatty acid synthases, providing some clues to important challenges and opportunities in the field.
[Mh] Termos MeSH primário: Vias Biossintéticas
Ácidos Graxos/metabolismo
Engenharia Metabólica
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/química
Proteína de Transporte de Acila/metabolismo
Proteína de Transporte de Acila S-Maloniltransferase/química
Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Aciltransferases/química
Aciltransferases/metabolismo
Enoil-(Proteína de Transporte de Acila) Redutase (NADH)/química
Enoil-(Proteína de Transporte de Acila) Redutase (NADH)/metabolismo
Ácido Graxo Sintases/química
Ácido Graxo Sintases/metabolismo
Ácidos Graxos/biossíntese
Ácidos Graxos/química
Hidroliases/química
Hidroliases/metabolismo
Engenharia Metabólica/métodos
Tioléster Hidrolases/química
Tioléster Hidrolases/metabolismo
[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.; REVIEW
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Fatty Acids); EC 1.3.1.9 (Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)); EC 2.3.- (Acyltransferases); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.85 (Fatty Acid Synthases); EC 3.1.2.- (Thiolester Hydrolases); EC 4.2.1.- (Hydro-Lyases)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141101
[St] Status:MEDLINE
[do] DOI:10.1039/c4mb00443d


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[PMID]:24192363
[Au] Autor:Liu Y; Zhang Y; Cao X; Xue S
[Ad] Endereço:Marine Bioproducts Engineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, People's Republic of China.
[Ti] Título:Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Synechocystis sp. PCC 6803.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;69(Pt 11):1256-9, 2013 Nov.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Malonyl-coenzymeA:acyl-carrier protein transacylase (MCAT), which catalyzes the transfer of the malonyl group from malonyl-CoA to acyl-carrier protein (ACP), is an essential enzyme in type II fatty-acid synthesis. The enzyme MCAT from Synechocystis sp. PCC 6803 (spMCAT), the first MCAT counterpart from a cyanobacterium, was cloned, purified and crystallized in order to determine its three-dimensional crystal structure. A higher-quality crystal with better diffraction was obtained by crystallization optimization. The crystal diffracted to 1.8 Šresolution and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 43.22, b = 149.21, c = 40.59 Å. Matthews coefficient calculations indicated that the crystal contained one spMCAT molecule in the asymmetric unit with a Matthews coefficient of 2.18 Å(3) Da(-1) and a solvent content of 43.65%.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/química
Proteína de Transporte de Acila S-Maloniltransferase/isolamento & purificação
Synechocystis/enzimologia
[Mh] Termos MeSH secundário: Clonagem Molecular
Cristalização
Cristalografia por Raios X
Eletroforese em Gel de Poliacrilamida
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:151101
[Lr] Data última revisão:
151101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131107
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309113026274


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[PMID]:23954257
[Au] Autor:Tian J; Zheng M; Yang G; Zheng L; Chen J; Yang B
[Ad] Endereço:College of Food, Shihezi University, Shihezi 832000, China; Research Center for Marine Ecology, The First Institute of Oceanography, State Oceanic Administration of China, Qingdao 266061, China.
[Ti] Título:Cloning and stress-responding expression analysis of malonyl CoA-acyl carrier protein transacylase gene of Nannochloropsis gaditana.
[So] Source:Gene;530(1):33-8, 2013 Nov 01.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Malonyl CoA-acyl carrier protein transacylase (MCAT, E2.3.1.39) is closely associated with the FASII pathway of fatty acid biosynthesis. However, the information about microalgal MCAT is scarce. In this study, a MCAT gene was isolated from Nannochloropsis gaditana with its deduced protein (NgMCAT) characterized with bioinformatic tools. The abundance of the NgMCAT transcript under different environmental conditions was determined with real-time quantitative PCR. Results showed that the open reading frame (ORF) of NgMCAT was 1059 bp in length, which encoded 352 amino acid residues. The abundance of NgMCAT transcript reached the maximum (5.17-fold) at 6h when sodium nitrate was limited, and reached the maximum (4.25-fold) at 12h at low temperature (15°C). The abundance of NgMCAT transcript fluctuated at high temperature (35°C) when the concentration of nitrate and sodium chloride exceeded 150 mg/L and 62 g/L, respectively. In addition, some components of fatty acid that changed with the expression of NgMCAT were also observed.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/genética
Clonagem Molecular
Ácidos Graxos/genética
Estramenópilas/genética
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Maloniltransferase/isolamento & purificação
Sequência de Aminoácidos
Biologia Computacional
Bases de Dados de Proteínas
Ácidos Graxos/biossíntese
Mutagênese Sítio-Dirigida
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:130923
[Lr] Data última revisão:
130923
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130820
[St] Status:MEDLINE


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[PMID]:23180244
[Au] Autor:Kumari R; Saxena R; Tiwari S; Tripathi DK; Srivastava KK
[Ad] Endereço:Department of Microbiology, CSIR-Central Drug Research Institute, Lucknow, 226001, India.
[Ti] Título:Rv3080c regulates the rate of inhibition of mycobacteria by isoniazid through FabD.
[So] Source:Mol Cell Biochem;374(1-2):149-55, 2013 Feb.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The mycobacterial FASII multi-enzyme complex has been identified to be a target of Ser/Thr protein kinases (STPKs) of Mycobacterium tuberculosis (MTB), with substrates, including the malonyl-CoA:ACP transacylase (FabD) and the ß-ketoacyl-ACP synthases KasA and KasB. These proteins are phosphorylated by various kinases in vitro. The present study links the correlation of FASII pathway with serine threonine protein kinase of MTB. In the preliminary finding, we have shown that mycobacterial protein Rv3080c (PknK) phosphorylates FabD and the knockdown of PknK protein in mycobacteria down regulates FabD expression. This event leads to the differential inhibition of mycobacteria in the presence of isoniazid (INH), as the inhibition of growth of mycobacteria in the presence of INH is enhanced in PknK deficient mycobacteria.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Escherichia coli/metabolismo
Ácido Graxo Sintase Tipo II/metabolismo
Isoniazida/farmacologia
Mycobacterium tuberculosis/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Antituberculosos/farmacologia
Proteínas de Bactérias/genética
Escherichia coli
Mycobacterium tuberculosis/efeitos dos fármacos
Ácidos Micólicos/metabolismo
Proteínas Serina-Treonina Quinases/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Mycolic Acids); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.39 (fabD protein, E coli); EC 2.7.11.1 (Pknk protein, Mycobacterium tuberculosis); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 6.- (Fatty Acid Synthase, Type II); V83O1VOZ8L (Isoniazid)
[Em] Mês de entrada:1306
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121127
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-012-1514-5


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[PMID]:23077570
[Au] Autor:Smith S; Witkowski A; Moghul A; Yoshinaga Y; Nefedov M; de Jong P; Feng D; Fong L; Tu Y; Hu Y; Young SG; Pham T; Cheung C; Katzman SM; Brand MD; Quinlan CL; Fens M; Kuypers F; Misquitta S; Griffey SM; Tran S; Gharib A; Knudsen J; Hannibal-Bach HK; Wang G; Larkin S; Thweatt J; Pasta S
[Ad] Endereço:Children's Hospital Oakland Research Institute, Oakland, California, USA. ssmith@chori.org
[Ti] Título:Compromised mitochondrial fatty acid synthesis in transgenic mice results in defective protein lipoylation and energy disequilibrium.
[So] Source:PLoS One;7(10):e47196, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A mouse model with compromised mitochondrial fatty acid synthesis has been engineered in order to assess the role of this pathway in mitochondrial function and overall health. Reduction in the expression of mitochondrial malonyl CoA-acyl carrier protein transacylase, a key enzyme in the pathway encoded by the nuclear Mcat gene, was achieved to varying extents in all examined tissues employing tamoxifen-inducible Cre-lox technology. Although affected mice consumed more food than control animals, they failed to gain weight, were less physically active, suffered from loss of white adipose tissue, reduced muscle strength, kyphosis, alopecia, hypothermia and shortened lifespan. The Mcat-deficient phenotype is attributed primarily to reduced synthesis, in several tissues, of the octanoyl precursors required for the posttranslational lipoylation of pyruvate and α-ketoglutarate dehydrogenase complexes, resulting in diminished capacity of the citric acid cycle and disruption of energy metabolism. The presence of an alternative lipoylation pathway that utilizes exogenous free lipoate appears restricted to liver and alone is insufficient for preservation of normal energy metabolism. Thus, de novo synthesis of precursors for the protein lipoylation pathway plays a vital role in maintenance of mitochondrial function and overall vigor.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Maloniltransferase/genética
Ácidos Graxos/metabolismo
Técnicas de Inativação de Genes
Lipoilação
Mitocôndrias/metabolismo
Proteínas Mitocondriais/genética
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Maloniltransferase/metabolismo
Tecido Adiposo Branco/metabolismo
Tecido Adiposo Branco/ultraestrutura
Anemia/genética
Animais
Respiração Celular
Ácidos Graxos/genética
Feminino
Corpos Cetônicos/sangue
Ácido Láctico/sangue
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Mitocôndrias/genética
Proteínas Mitocondriais/metabolismo
Miocárdio/metabolismo
Prolapso Retal/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Ketone Bodies); 0 (Mitochondrial Proteins); 33X04XA5AT (Lactic Acid); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0047196



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