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Pesquisa : D08.811.520.241.300.250 [Categoria DeCS]
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[PMID]:28923398
[Au] Autor:Sun LN; Zhi Z; Chen LY; Zhou Q; Li XM; Gan WJ; Chen S; Yang M; Liu Y; Shen T; Xu Y; Li JM
[Ad] Endereço:Department of Pathology and Pathophysiology, Medical College of Soochow University, Soochow University, Suzhou 215123, People's Republic of China.
[Ti] Título:SIRT1 suppresses colorectal cancer metastasis by transcriptional repression of miR-15b-5p.
[So] Source:Cancer Lett;409:104-115, 2017 Nov 28.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The class III deacetylase sirtuin 1 (SIRT1), a member of the sirtuin family proteins, plays a key role in many types of cancers including colorectal cancer (CRC). Here we report that SIRT1 suppressed CRC metastasis in vitro and in vivo as a negative regulator for miR-15b-5p transcription. Mechanistically, SIRT1 impaired regulatory effects of activator protein (AP-1) on miR-15b-5p trans-activation through deacetylation of AP-1. Importantly, acyl-CoA oxidase 1 (ACOX1), a key enzyme of the fatty acid oxidation (FAO) pathway, was found as a direct target for miR-15b-5p. SIRT1 expression was positively correlated with ACOX1 expression in CRC cells and in xenografts. Moreover, ACOX1 overexpression attenuated the augmentation of migration and invasion of CRC cells by miR-15b-5p overexpression. In conclusion, our study demonstrated a functional role of the SIRT1/miR-15b-5p/ACOX1 axis in CRC metastasis and suggested a potential target for metastatic CRC therapy.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
MicroRNAs/genética
Sirtuína 1/genética
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Acetil-CoA C-Aciltransferase/metabolismo
Animais
Células CACO-2
Isomerases de Ligação Dupla Carbono-Carbono/metabolismo
Linhagem Celular Tumoral
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Enoil-CoA Hidratase/metabolismo
Células HCT116
Células HT29
Xenoenxertos
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
MicroRNAs/metabolismo
Metástase Neoplásica
Racemases e Epimerases/metabolismo
Transdução de Sinais
Sirtuína 1/metabolismo
Transcrição Genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN15 microRNA, human); 0 (MicroRNAs); 0 (fatty acid oxidation complex); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 3.5.1.- (SIRT1 protein, human); EC 3.5.1.- (Sirtuin 1); EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 5.1.- (Racemases and Epimerases); EC 5.3.3.- (Carbon-Carbon Double Bond Isomerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE


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[PMID]:28803779
[Au] Autor:Liu S; Yu H; Liu Y; Liu X; Zhang Y; Bu C; Yuan S; Chen Z; Xie G; Li W; Xu B; Yang J; He L; Jin T; Xiong Y; Sun L; Liu X; Han C; Cheng Z; Liang J; Shang Y
[Ad] Endereço:Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China; Department of Biochemistry and Molecular Biology, School of Basic M
[Ti] Título:Chromodomain Protein CDYL Acts as a Crotonyl-CoA Hydratase to Regulate Histone Crotonylation and Spermatogenesis.
[So] Source:Mol Cell;67(5):853-866.e5, 2017 Sep 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine crotonylation (Kcr) is a newly identified histone modification that is associated with active transcription in mammalian cells. Here we report that the chromodomain Y-like transcription corepressor CDYL negatively regulates histone Kcr by acting as a crotonyl-CoA hydratase to convert crotonyl-CoA to ß-hydroxybutyryl-CoA. We showed that the negative regulation of histone Kcr by CDYL is intrinsically linked to its transcription repression activity and functionally implemented in the reactivation of sex chromosome-linked genes in round spermatids and genome-wide histone replacement in elongating spermatids. Significantly, Cdyl transgenic mice manifest dysregulation of histone Kcr and reduction of male fertility with a decreased epididymal sperm count and sperm cell motility. Our study uncovers a biochemical pathway in the regulation of histone Kcr and implicates CDYL-regulated histone Kcr in spermatogenesis, adding to the understanding of the physiology of male reproduction and the mechanism of the spermatogenic failure in AZFc (Azoospermia Factor c)-deleted infertile men.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Proteínas Correpressoras/metabolismo
Enoil-CoA Hidratase/metabolismo
Histona Acetiltransferases/metabolismo
Histonas/metabolismo
Infertilidade Masculina/enzimologia
Processamento de Proteína Pós-Traducional
Proteínas/metabolismo
Espermatogênese
Espermatozoides/enzimologia
Testículo/enzimologia
[Mh] Termos MeSH secundário: Animais
Proteínas Correpressoras/genética
Enoil-CoA Hidratase/genética
Fertilidade
Predisposição Genética para Doença
Células HeLa
Histona Acetiltransferases/genética
Seres Humanos
Infertilidade Masculina/genética
Infertilidade Masculina/patologia
Infertilidade Masculina/fisiopatologia
Cinética
Lisina
Masculino
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Fenótipo
Domínios Proteicos
Proteínas/genética
Interferência de RNA
Células Sf9
Contagem de Espermatozoides
Motilidade Espermática
Espermatozoides/patologia
Testículo/patologia
Testículo/fisiopatologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (CDYL protein, human); 0 (Co-Repressor Proteins); 0 (Histones); 0 (Proteins); 2871-66-1 (3-hydroxybutyryl-coenzyme A); 992-67-6 (crotonyl-coenzyme A); EC 2.3.1.48 (Cdyl protein, mouse); EC 2.3.1.48 (Histone Acetyltransferases); EC 4.2.1.17 (Enoyl-CoA Hydratase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE


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[PMID]:28632406
[Au] Autor:Machaba KE; Mhlongo NN; Dokurugu YM; Soliman ME
[Ad] Endereço:Molecular Modelling & Drug Design Research Group, School of Health Sciences, University of KwaZulu-Natal, Westville, Durban 4001, South Africa.
[Ti] Título:Tailored-pharmacophore model to enhance virtual screening and drug discovery: a case study on the identification of potential inhibitors against drug-resistant Mycobacterium tuberculosis (3R)-hydroxyacyl-ACP dehydratases.
[So] Source:Future Med Chem;9(10):1055-1071, 2017 Jun.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: Virtual screening (VS) is powerful tool in discovering molecular inhibitors that are most likely to bind to drug targets of interest. Herein, we introduce a novel VS approach, so-called 'tailored-pharmacophore', in order to explore inhibitors that overcome drug resistance. Methodology & results: The emergence and spread of drug resistance strains of tuberculosis is one of the most critical issues in healthcare. A tailored-pharmacophore approach was found promising to identify in silico predicted hit with better binding affinities in case of the resistance mutations in MtbHadAB as compared with thiacetazone, a prodrug used in the clinical treatment of tuberculosis. CONCLUSION: This approach can potentially be enforced for the discovery and design of drugs against a wide range of resistance targets.
[Mh] Termos MeSH primário: Descoberta de Drogas
Enoil-CoA Hidratase/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Tuberculose Resistente a Múltiplos Medicamentos/tratamento farmacológico
[Mh] Termos MeSH secundário: Avaliação Pré-Clínica de Medicamentos
Enoil-CoA Hidratase/metabolismo
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Modelos Moleculares
Estrutura Molecular
Relação Estrutura-Atividade
Tuberculose Resistente a Múltiplos Medicamentos/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0020


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[PMID]:28629946
[Au] Autor:Mezzar S; De Schryver E; Asselberghs S; Meyhi E; Morvay PL; Baes M; Van Veldhoven PP
[Ad] Endereço:LIPIT, Department of Cellular and Molecular Medicine, KU Leuven, Belgium.
[Ti] Título:Phytol-induced pathology in 2-hydroxyacyl-CoA lyase (HACL1) deficient mice. Evidence for a second non-HACL1-related lyase.
[So] Source:Biochim Biophys Acta;1862(9):972-990, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:2-Hydroxyacyl-CoA lyase (HACL1) is a key enzyme of the peroxisomal α-oxidation of phytanic acid. To better understand its role in health and disease, a mouse model lacking HACL1 was investigated. Under normal conditions, these mice did not display a particular phenotype. However, upon dietary administration of phytol, phytanic acid accumulated in tissues, mainly in liver and serum of KO mice. As a consequence of phytanic acid (or a metabolite) toxicity, KO mice displayed a significant weight loss, absence of abdominal white adipose tissue, enlarged and mottled liver and reduced hepatic glycogen and triglycerides. In addition, hepatic PPARα was activated. The central nervous system of the phytol-treated mice was apparently not affected. In addition, 2OH-FA did not accumulate in the central nervous system of HACL1 deficient mice, likely due to the presence in the endoplasmic reticulum of an alternate HACL1-unrelated lyase. The latter may serve as a backup system in certain tissues and account for the formation of pristanic acid in the phytol-fed KO mice. As the degradation of pristanic acid is also impaired, both phytanoyl- and pristanoyl-CoA levels are increased in liver, and the ω-oxidized metabolites are excreted in urine. In conclusion, HACL1 deficiency is not associated with a severe phenotype, but in combination with phytanic acid intake, the normal situation in man, it might present with phytanic acid elevation and resemble a Refsum like disorder.
[Mh] Termos MeSH primário: Enoil-CoA Hidratase/deficiência
Enoil-CoA Hidratase/metabolismo
Liases/metabolismo
Fitol/farmacologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Retículo Endoplasmático/efeitos dos fármacos
Retículo Endoplasmático/metabolismo
Ácidos Graxos/farmacologia
Feminino
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Camundongos Knockout
Oxirredução
PPAR alfa/metabolismo
Ácido Fitânico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (PPAR alpha); 14721-66-5 (Phytanic Acid); 150-86-7 (Phytol); 5FMQ2908AP (pristanic acid); EC 4.- (Lyases); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


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[PMID]:28542493
[Au] Autor:Nickels JD; Chatterjee S; Stanley CB; Qian S; Cheng X; Myles DAA; Standaert RF; Elkins JG; Katsaras J
[Ad] Endereço:Shull Wollan Center-A Joint Institute for Neutron Sciences, Oak Ridge National Laboratory, Oak Ridge, Tennessee, United States of America.
[Ti] Título:The in vivo structure of biological membranes and evidence for lipid domains.
[So] Source:PLoS Biol;15(5):e2002214, 2017 May.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Examining the fundamental structure and processes of living cells at the nanoscale poses a unique analytical challenge, as cells are dynamic, chemically diverse, and fragile. A case in point is the cell membrane, which is too small to be seen directly with optical microscopy and provides little observational contrast for other methods. As a consequence, nanoscale characterization of the membrane has been performed ex vivo or in the presence of exogenous labels used to enhance contrast and impart specificity. Here, we introduce an isotopic labeling strategy in the gram-positive bacterium Bacillus subtilis to investigate the nanoscale structure and organization of its plasma membrane in vivo. Through genetic and chemical manipulation of the organism, we labeled the cell and its membrane independently with specific amounts of hydrogen (H) and deuterium (D). These isotopes have different neutron scattering properties without altering the chemical composition of the cells. From neutron scattering spectra, we confirmed that the B. subtilis cell membrane is lamellar and determined that its average hydrophobic thickness is 24.3 ± 0.9 Ångstroms (Å). Furthermore, by creating neutron contrast within the plane of the membrane using a mixture of H- and D-fatty acids, we detected lateral features smaller than 40 nm that are consistent with the notion of lipid rafts. These experiments-performed under biologically relevant conditions-answer long-standing questions in membrane biology and illustrate a fundamentally new approach for systematic in vivo investigations of cell membrane structure.
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Membrana Celular/metabolismo
Ácidos Graxos/metabolismo
Bicamadas Lipídicas/metabolismo
Microdomínios da Membrana/metabolismo
Modelos Biológicos
[Mh] Termos MeSH secundário: Algoritmos
Bacillus subtilis/química
Bacillus subtilis/efeitos dos fármacos
Bacillus subtilis/crescimento & desenvolvimento
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Membrana Celular/química
Membrana Celular/efeitos dos fármacos
Cerulenina/farmacologia
Deutério
Enoil-CoA Hidratase/genética
Enoil-CoA Hidratase/metabolismo
Inibidores da Síntese de Ácidos Graxos/farmacologia
Ácidos Graxos/química
Deleção de Genes
Interações Hidrofóbicas e Hidrofílicas
Bicamadas Lipídicas/química
Microdomínios da Membrana/química
Microdomínios da Membrana/efeitos dos fármacos
Viabilidade Microbiana/efeitos dos fármacos
Difração de Nêutrons
Ácidos Palmíticos/química
Ácidos Palmíticos/metabolismo
Espalhamento a Baixo Ângulo
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acid Synthesis Inhibitors); 0 (Fatty Acids); 0 (Lipid Bilayers); 0 (Palmitic Acids); 17397-89-6 (Cerulenin); 5502-94-3 (aseanostatin P5); AR09D82C7G (Deuterium); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[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:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2002214


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[PMID]:28532241
[Au] Autor:Kihara T; Hiroe A; Ishii-Hyakutake M; Mizuno K; Tsuge T
[Ad] Endereço:a Department of Materials Science and Engineering, Tokyo Institute of Technology , Midori-ku, Yokohama , Japan.
[Ti] Título:Bacillus cereus-type polyhydroxyalkanoate biosynthetic gene cluster contains R-specific enoyl-CoA hydratase gene.
[So] Source:Biosci Biotechnol Biochem;81(8):1627-1635, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bacillus cereus and Bacillus megaterium both accumulate polyhydroxyalkanoate (PHA) but their PHA biosynthetic gene (pha) clusters that code for proteins involved in PHA biosynthesis are different. Namely, a gene encoding MaoC-like protein exists in the B. cereus-type pha cluster but not in the B. megaterium-type pha cluster. MaoC-like protein has an R-specific enoyl-CoA hydratase (R-hydratase) activity and is referred to as PhaJ when involved in PHA metabolism. In this study, the pha cluster of B. cereus YB-4 was characterized in terms of PhaJ's function. In an in vitro assay, PhaJ from B. cereus YB-4 (PhaJ ) exhibited hydration activity toward crotonyl-CoA. In an in vivo assay using Escherichia coli as a host for PHA accumulation, the recombinant strain expressing PhaJ and PHA synthase led to increased PHA accumulation, suggesting that PhaJ functioned as a monomer supplier. The monomer composition of the accumulated PHA reflected the substrate specificity of PhaJ , which appeared to prefer short chain-length substrates. The pha cluster from B. cereus YB-4 functioned to accumulate PHA in E. coli; however, it did not function when the phaJ gene was deleted. The B. cereus-type pha cluster represents a new example of a pha cluster that contains the gene encoding PhaJ.
[Mh] Termos MeSH primário: Família Multigênica
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Aciltransferases/genética
Aciltransferases/metabolismo
Bacillus cereus/enzimologia
Bacillus cereus/genética
Bacillus megaterium/enzimologia
Bacillus megaterium/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Ácido Butírico/metabolismo
Caproatos/metabolismo
Clonagem Molecular
Enoil-CoA Hidratase/genética
Enoil-CoA Hidratase/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucose/metabolismo
Ácidos Pentanoicos/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Poli-Hidroxialcanoatos/biossíntese
Proteínas Recombinantes
Especificidade da Espécie
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Caproates); 0 (Pentanoic Acids); 0 (Polyhydroxyalkanoates); 0 (Recombinant Proteins); 107-92-6 (Butyric Acid); 1F8SN134MX (hexanoic acid); 992-67-6 (crotonyl-coenzyme A); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 4.2.1.17 (Enoyl-CoA Hydratase); GZK92PJM7B (n-pentanoic acid); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1325314


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[PMID]:28372908
[Au] Autor:Desai V; Desai S; Gaonkar SN; Palyekar U; Joshi SD; Dixit SK
[Ad] Endereço:Dnyanprassarak Mandal's College and Research Centre, Assagao, Mapusa-Bardez, Goa 403507, India. Electronic address: desai_vidya@ymail.com.
[Ti] Título:Novel quinoxalinyl chalcone hybrid scaffolds as enoyl ACP reductase inhibitors: Synthesis, molecular docking and biological evaluation.
[So] Source:Bioorg Med Chem Lett;27(10):2174-2180, 2017 05 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We report herein, first ever synthesis of series of novel differently substituted quinoxalinyl chalcones using Claisen Schmidt condensation, its molecular docking studies, and potential to be good anti-microbial, anti-tubercular and anti-cancer agents. The antimicrobial studies were carried out against Staphylococcus aureus, Escherichia coli and Candida albicans using disc diffusion procedure. The selected chalcones were tested for anti-cancer and cytotoxicity activity against MCF-7 cancer cell line using MTT assay method. All the synthesized compounds were screened for in vitro anti-tubercular screening against MtbH37RV strains by Alamar blue dye method. These results were compared with molecular docking studies carried out on Mycobacterium tuberculosis enzyme enoyl ACP reductase using Surflex-Dock program that is interfaced with Sybyl-X 2.0. SAR analysis for antimicrobial and antitubercular activity has also been proposed.
[Mh] Termos MeSH primário: Anti-Infecciosos/síntese química
Chalconas/química
Enoil-CoA Hidratase/antagonistas & inibidores
Inibidores Enzimáticos/síntese química
[Mh] Termos MeSH secundário: Anti-Infecciosos/química
Anti-Infecciosos/farmacologia
Antineoplásicos/síntese química
Antineoplásicos/química
Antineoplásicos/toxicidade
Sítios de Ligação
Candida albicans/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Chalconas/síntese química
Chalconas/farmacologia
Testes de Sensibilidade a Antimicrobianos por Disco-Difusão
Desenho de Drogas
Enoil-CoA Hidratase/metabolismo
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Escherichia coli/efeitos dos fármacos
Seres Humanos
Células MCF-7
Simulação de Acoplamento Molecular
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/enzimologia
Estrutura Terciária de Proteína
Staphylococcus aureus/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antineoplastic Agents); 0 (Chalcones); 0 (Enzyme Inhibitors); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


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[PMID]:28202214
[Au] Autor:Bedoyan JK; Yang SP; Ferdinandusse S; Jack RM; Miron A; Grahame G; DeBrosse SD; Hoppel CL; Kerr DS; Wanders RJ
[Ad] Endereço:Center for Human Genetics, University Hospitals Cleveland Medical Center, Cleveland, OH, USA; Department of Genetics and Genome Sciences, Case Western Reserve University, Cleveland, OH, USA; Center for Inherited Disorders of Energy Metabolism (CIDEM), University Hospitals Cleveland Medical Center, C
[Ti] Título:Lethal neonatal case and review of primary short-chain enoyl-CoA hydratase (SCEH) deficiency associated with secondary lymphocyte pyruvate dehydrogenase complex (PDC) deficiency.
[So] Source:Mol Genet Metab;120(4):342-349, 2017 Apr.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in ECHS1 result in short-chain enoyl-CoA hydratase (SCEH) deficiency which mainly affects the catabolism of various amino acids, particularly valine. We describe a case compound heterozygous for ECHS1 mutations c.836T>C (novel) and c.8C>A identified by whole exome sequencing of proband and parents. SCEH deficiency was confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient had a severe neonatal course with elevated blood and cerebrospinal fluid lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid was markedly elevated as were metabolites of the three branched-chain α-ketoacids on urine organic acids analysis. These urine metabolites notably decreased when lactic acidosis decreased in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity was deficient, but PDC and α-ketoglutarate dehydrogenase complex activities in cultured fibroblasts were normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts was suggestive of slightly reduced PDC activity relative to control range in mitochondria. We reviewed 16 other cases with mutations in ECHS1 where PDC activity was also assayed in order to determine how common and generalized secondary PDC deficiency is associated with primary SCEH deficiency. For reasons that remain unexplained, we find that about half of cases with primary SCEH deficiency also exhibit secondary PDC deficiency. The patient died on day-of-life 39, prior to establishing his diagnosis, highlighting the importance of early and rapid neonatal diagnosis because of possible adverse effects of certain therapeutic interventions, such as administration of ketogenic diet, in this disorder. There is a need for better understanding of the pathogenic mechanisms and phenotypic variability in this relatively recently discovered disorder.
[Mh] Termos MeSH primário: Enoil-CoA Hidratase/deficiência
Doença da Deficiência do Complexo de Piruvato Desidrogenase/mortalidade
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Enoil-CoA Hidratase/genética
Exoma
Seres Humanos
Recém-Nascido
Masculino
Polimorfismo de Nucleotídeo Único
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 4.2.1.17 (enoyl CoA hydratase, short chain, 1, mitochondrial, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE


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[PMID]:28126742
[Au] Autor:Blaise M; Van Wyk N; Banères-Roquet F; Guérardel Y; Kremer L
[Ad] Endereço:Centre d'étude d'agents Pathogènes et Biotechnologies pour la Santé (CPBS), Université de Montpellier, CNRS, FRE 3689, 34293 Montpellier, France mickael.blaise@cpbs.cnrs.fr laurent.kremer@cpbs.cnrs.fr.
[Ti] Título:Binding of NADP triggers an open-to-closed transition in a mycobacterial FabG ß-ketoacyl-ACP reductase.
[So] Source:Biochem J;474(6):907-921, 2017 Mar 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The ketoacyl-acyl carrier protein (ACP) reductase FabG catalyzes the NADPH/NADH dependent reduction of ß-ketoacyl-ACP substrates to ß-hydroxyacyl-ACP products, the first reductive step in the fatty acid biosynthesis elongation cycle. FabG proteins are ubiquitous in bacteria and are part of the type II fatty acid synthase system. Mining the genome uncovered several putative FabG-like proteins. Among them, we identified MSMEG_6753 whose gene was found adjacent to , encoding a recently characterized enoyl-CoA dehydratase, and to , encoding another potential reductase. Recombinantly expressed and purified MSMEG_6753 exhibits ketoacyl reductase activity in the presence of acetoacetyl-CoA and NADPH. This activity was subsequently confirmed by functional complementation studies in a thermosensitive mutant. Furthermore, comparison of the and the NADP -bound MSMEG_6753 crystal structures showed that cofactor binding induces a closed conformation of the protein. A Δ deletion mutant could be generated in , indicating that this gene is dispensable for mycobacterial growth. Overall, these results showcase the diversity of FabG-like proteins in mycobacteria and new structural features regarding the catalytic mechanism of this important family of enzymes that may be of importance for the rational design of specific FabG inhibitors.
[Mh] Termos MeSH primário: Acil Coenzima A/química
Oxirredutases do Álcool/química
Proteínas de Bactérias/química
Mycobacterium smegmatis/química
Mycobacterium tuberculosis/química
NADP/química
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Enoil-CoA Hidratase/química
Enoil-CoA Hidratase/genética
Enoil-CoA Hidratase/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Teste de Complementação Genética
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Modelos Moleculares
Mycobacterium smegmatis/enzimologia
Mycobacterium tuberculosis/enzimologia
NADP/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Isoenzymes); 0 (Recombinant Proteins); 1420-36-6 (acetoacetyl CoA); 53-59-8 (NADP); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.36 (acetoacetyl-CoA reductase); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20161052


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[PMID]:28089378
[Au] Autor:Kataoka N; Vangnai AS; Pongtharangkul T; Yakushi T; Matsushita K
[Ad] Endereço:Division of Agricultural Sciences, Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8515, Japan; Research Center for Thermotolerant Microbial Resources, Yamaguchi University, Yamaguchi 753-8515, Japan. Electronic address: nkataoka@yamaguchi-u.ac.jp.
[Ti] Título:Butyrate production under aerobic growth conditions by engineered Escherichia coli.
[So] Source:J Biosci Bioeng;123(5):562-568, 2017 May.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Butyrate is an important industrial platform chemical. Although several groups have reported butyrate production under oxygen-limited conditions by a native producer, Clostridium tyrobutylicum, and by a metabolically engineered Escherichia coli, efforts to produce butyrate under aerobic growth conditions have met limited success. Here, we constructed a novel butyrate synthetic pathway that functions under aerobic growth conditions in E. coli, by modifying the 1-butanol synthetic pathway reported previously. The pathway consists of phaA (acetyltransferase) and phaB (NADPH-dependent acetoacetyl-CoA reductase) from Ralstonia eutropha, phaJ ((R)-specific enoyl-CoA hydratase) from Aeromonas caviae, ter (trans-enoyl-CoA reductase) from Treponema denticola, and endogenous thioesterase(s) of E. coli. To evaluate the potential of this pathway for butyrate production, culture conditions, including pH, oxygen supply, and concentration of inorganic nitrogen sources, were optimized in a mini-jar fermentor. Under the optimal conditions, butyrate was produced at a concentration of up to 140 mM (12.3 g/L in terms of butyric acid) after 54 h of fed-batch culture.
[Mh] Termos MeSH primário: Reatores Biológicos
Vias Biossintéticas/genética
Ácido Butírico/metabolismo
Escherichia coli/metabolismo
Engenharia Metabólica
[Mh] Termos MeSH secundário: 1-Butanol/metabolismo
Acetiltransferases/genética
Acetiltransferases/metabolismo
Aerobiose
Aeromonas caviae/enzimologia
Aeromonas caviae/genética
Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Técnicas de Cultura Celular por Lotes
Clostridium/metabolismo
Cupriavidus necator/enzimologia
Cupriavidus necator/genética
Enoil-CoA Hidratase/genética
Enoil-CoA Hidratase/metabolismo
Escherichia coli/enzimologia
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Concentração de Íons de Hidrogênio
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo
Oxigênio/metabolismo
Oxigênio/farmacologia
Tioléster Hidrolases/genética
Tioléster Hidrolases/metabolismo
Treponema denticola/enzimologia
Treponema denticola/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
107-92-6 (Butyric Acid); 8PJ61P6TS3 (1-Butanol); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.36 (acetoacetyl-CoA reductase); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.1.38 (trans-2-enoyl-CoA reductase (NADPH)); EC 2.3.1.- (Acetyltransferases); EC 3.1.2.- (Thiolester Hydrolases); EC 4.2.1.- (R-specific trans-2,3-enoylacyl-CoA hydratase); EC 4.2.1.17 (Enoyl-CoA Hydratase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE



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