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  1 / 1023 MEDLINE  
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[PMID]:28644952
[Au] Autor:Lombard DB; Zhao Y
[Ad] Endereço:Department of Pathology and Institute of Gerontology, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: davidlom@med.umich.edu.
[Ti] Título:ACSF3 and Mal(onate)-Adapted Mitochondria.
[So] Source:Cell Chem Biol;24(6):649-650, 2017 Jun 22.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue of Cell Chemical Biology, Bowman and colleagues show that the mitochondrial enzyme ACSF3 generates malonyl-CoA from malonate, in turn regulating metabolic flux and mitochondrial protein malonylation (Bowman et al., 2017). The study reveals a mechanism to generate mitochondrial malonyl-CoA and how this molecule impacts mitochondrial biology.
[Mh] Termos MeSH primário: Coenzima A Ligases/metabolismo
Malonatos/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Malonil Coenzima A/metabolismo
Camundongos
Proteínas Mitocondriais/metabolismo
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Malonates); 0 (Mitochondrial Proteins); 524-14-1 (Malonyl Coenzyme A); 9KX7ZMG0MK (malonic acid); EC 6.2.1.- (ACSF3 protein, human); EC 6.2.1.- (Coenzyme A Ligases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE


  2 / 1023 MEDLINE  
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[PMID]:28429315
[Au] Autor:Zimorski V; Rauch C; van Hellemond JJ; Tielens AGM; Martin WF
[Ad] Endereço:Institute of Molecular Evolution, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
[Ti] Título:The Mitochondrion of Euglena gracilis.
[So] Source:Adv Exp Med Biol;979:19-37, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the presence of oxygen, Euglena gracilis mitochondria function much like mammalian mitochondria. Under anaerobiosis, E. gracilis mitochondria perform a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. Some components (enzymes and cofactors) of Euglena's anaerobic energy metabolism are found among the anaerobic mitochondria of invertebrates, others are found among hydrogenosomes, the H -producing anaerobic mitochondria of protists.
[Mh] Termos MeSH primário: Euglena gracilis/metabolismo
Mitocôndrias/fisiologia
[Mh] Termos MeSH secundário: Anaerobiose/fisiologia
Ácidos Graxos/biossíntese
Glicólise/fisiologia
Malonil Coenzima A/metabolismo
Oxirredução
Ácido Pirúvico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Fatty Acids); 524-14-1 (Malonyl Coenzyme A); 8558G7RUTR (Pyruvic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-54910-1_2


  3 / 1023 MEDLINE  
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[PMID]:28385800
[Au] Autor:Cheung CYY; Tang CS; Xu A; Lee CH; Au KW; Xu L; Fong CHY; Kwok KHM; Chow WS; Woo YC; Yuen MMA; Cherny SS; Hai J; Cheung BMY; Tan KCB; Lam TH; Tse HF; Sham PC; Lam KSL
[Ad] Endereço:Department of Medicine, The University of Hong Kong, Hong Kong, China.
[Ti] Título:An Exome-Chip Association Analysis in Chinese Subjects Reveals a Functional Missense Variant of That Regulates FGF21 Levels.
[So] Source:Diabetes;66(6):1723-1728, 2017 Jun.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fibroblast growth factor 21 (FGF21) is increasingly recognized as an important metabolic regulator of glucose homeostasis. Here, we conducted an exome-chip association analysis by genotyping 5,169 Chinese individuals from a community-based cohort and two clinic-based cohorts. A custom Asian exome-chip was used to detect genetic determinants influencing circulating FGF21 levels. Single-variant association analysis interrogating 70,444 single nucleotide polymorphisms identified a novel locus, , significantly associated with circulating FGF21 levels at genome-wide significance. In the combined analysis, the common missense variant of , rs1260326 (p.Pro446Leu), showed an association with FGF21 levels after adjustment for age and sex ( = 1.61 × 10 ; ß [SE] = 0.14 [0.02]), which remained significant on further adjustment for BMI ( = 3.01 × 10 ; ß [SE] = 0.15 [0.02]). Leu446 may influence FGF21 expression via its ability to increase glucokinase (GCK) activity. This can lead to enhanced FGF21 expression via elevated fatty acid synthesis, consequent to the inhibition of carnitine/palmitoyl-transferase by malonyl-CoA, and via increased glucose-6-phosphate-mediated activation of the carbohydrate response element binding protein, known to regulate FGF21 gene expression. Our findings shed new light on the genetic regulation of FGF21 levels. Further investigations to dissect the relationship between GCKR and FGF21, with respect to the risk of metabolic diseases, are warranted.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Grupo com Ancestrais do Continente Asiático/genética
Fatores de Crescimento de Fibroblastos/genética
Regulação da Expressão Gênica/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/metabolismo
Carnitina O-Palmitoiltransferase
Exoma
Ácidos Graxos/biossíntese
Feminino
Glucoquinase/metabolismo
Glucose-6-Fosfato/metabolismo
Seres Humanos
Masculino
Malonil Coenzima A/metabolismo
Meia-Idade
Mutação de Sentido Incorreto
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (Fatty Acids); 0 (GCKR protein, human); 0 (MLXIPL protein, human); 0 (fibroblast growth factor 21); 524-14-1 (Malonyl Coenzyme A); 56-73-5 (Glucose-6-Phosphate); 62031-54-3 (Fibroblast Growth Factors); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.7.1.2 (Glucokinase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.2337/db16-1384


  4 / 1023 MEDLINE  
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[PMID]:28280244
[Au] Autor:Mugabo Y; Zhao S; Lamontagne J; Al-Mass A; Peyot ML; Corkey BE; Joly E; Madiraju SRM; Prentki M
[Ad] Endereço:From the Montreal Diabetes Research Center and Centre de Recherche du Centre Hospitalier de l'Université de Montréal, Montréal, Québec H2X 0A9, Canada.
[Ti] Título:Metabolic fate of glucose and candidate signaling and excess-fuel detoxification pathways in pancreatic ß-cells.
[So] Source:J Biol Chem;292(18):7407-7422, 2017 May 05.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucose metabolism promotes insulin secretion in ß-cells via metabolic coupling factors that are incompletely defined. Moreover, chronically elevated glucose causes ß-cell dysfunction, but little is known about how cells handle excess fuels to avoid toxicity. Here we sought to determine which among the candidate pathways and coupling factors best correlates with glucose-stimulated insulin secretion (GSIS), define the fate of glucose in the ß-cell, and identify pathways possibly involved in excess-fuel detoxification. We exposed isolated rat islets for 1 h to increasing glucose concentrations and measured various pathways and metabolites. Glucose oxidation, oxygen consumption, and ATP production correlated well with GSIS and saturated at 16 mm glucose. However, glucose utilization, glycerol release, triglyceride and glycogen contents, free fatty acid (FFA) content and release, and cholesterol and cholesterol esters increased linearly up to 25 mm glucose. Besides being oxidized, glucose was mainly metabolized via glycerol production and release and lipid synthesis (particularly FFA, triglycerides, and cholesterol), whereas glycogen production was comparatively low. Using targeted metabolomics in INS-1(832/13) cells, we found that several metabolites correlated well with GSIS, in particular some Krebs cycle intermediates, malonyl-CoA, and lower ADP levels. Glucose dose-dependently increased the dihydroxyacetone phosphate/glycerol 3-phosphate ratio in INS-1(832/13) cells, indicating a more oxidized state of NAD in the cytosol upon glucose stimulation. Overall, the data support a role for accelerated oxidative mitochondrial metabolism, anaplerosis, and malonyl-CoA/lipid signaling in ß-cell metabolic signaling and suggest that a decrease in ADP levels is important in GSIS. The results also suggest that excess-fuel detoxification pathways in ß-cells possibly comprise glycerol and FFA formation and release extracellularly and the diversion of glucose carbons to triglycerides and cholesterol esters.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Ácidos Graxos/metabolismo
Glucose/farmacologia
Células Secretoras de Insulina/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Ésteres do Colesterol/metabolismo
Fosfato de Di-Hidroxiacetona/metabolismo
Relação Dose-Resposta a Droga
Glucose/metabolismo
Glicerofosfatos/metabolismo
Glicogênio/metabolismo
Masculino
Malonil Coenzima A/metabolismo
Ratos
Ratos Wistar
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholesterol Esters); 0 (Fatty Acids); 0 (Glycerophosphates); 0 (Triglycerides); 524-14-1 (Malonyl Coenzyme A); 57-04-5 (Dihydroxyacetone Phosphate); 8L70Q75FXE (Adenosine Triphosphate); 9005-79-2 (Glycogen); 9NTI6P3O4X (alpha-glycerophosphoric acid); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.763060


  5 / 1023 MEDLINE  
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[PMID]:28222482
[Au] Autor:Bazet Lyonnet B; Diacovich L; Gago G; Spina L; Bardou F; Lemassu A; Quémard A; Gramajo H
[Ad] Endereço:Laboratory of Physiology and Genetics of Actinomycetes, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
[Ti] Título:Functional reconstitution of the Mycobacterium tuberculosis long-chain acyl-CoA carboxylase from multiple acyl-CoA subunits.
[So] Source:FEBS J;284(7):1110-1125, 2017 Apr.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycobacterium tuberculosis produces a large number of structurally diverse lipids that have been implicated in the pathogenicity, persistence and antibiotic resistance of this organism. Most building blocks involved in the biosynthesis of all these lipids are generated by acyl-CoA carboxylases whose subunit composition and physiological roles have not yet been clearly established. Inconclusive data in the literature refer to the exact protein composition and substrate specificity of the enzyme complex that produces the long-chain α-carboxy-acyl-CoAs, which are substrates involved in the last step of condensation mediated by the polyketide synthase 13 to synthesize mature mycolic acids. Here we have successfully reconstituted the long-chain acyl-CoA carboxylase (LCC) complex from its purified components, the α subunit (AccA3), the ε subunit (AccE5) and the two ß subunits (AccD4 and AccD5), and demonstrated that the four subunits are essential for its activity. Furthermore, we also showed by substrate competition experiments and the use of a specific inhibitor that the AccD5 subunit's role in the carboxylation of the long acyl-CoAs, as part of the LCC complex, was structural rather than catalytic. Moreover, AccD5 was also able to carboxylate its natural substrates, acetyl-CoA and propionyl-CoA, in the context of the LCC enzyme complex. Thus, the supercomplex formed by these four subunits has the potential to generate the main substrates, malonyl-CoA, methylmalonyl-CoA and α-carboxy-C -CoA, used as condensing units for the biosynthesis of all the lipids present in this pathogen.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Carbono-Carbono Ligases/metabolismo
Mycobacterium tuberculosis/metabolismo
Policetídeo Sintases/metabolismo
Subunidades Proteicas/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Acil Coenzima A/metabolismo
Proteínas de Bactérias/genética
Carbono-Carbono Ligases/genética
Clonagem Molecular
Ensaios Enzimáticos
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Malonil Coenzima A/metabolismo
Mycobacterium tuberculosis/genética
Ácidos Micólicos/metabolismo
Policetídeo Sintases/genética
Engenharia de Proteínas
Subunidades Proteicas/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Mycolic Acids); 0 (Protein Subunits); 0 (Recombinant Proteins); 1264-45-5 (methylmalonyl-coenzyme A); 317-66-8 (propionyl-coenzyme A); 524-14-1 (Malonyl Coenzyme A); 72-89-9 (Acetyl Coenzyme A); 79956-01-7 (Polyketide Synthases); EC 6.4.- (Carbon-Carbon Ligases); EC 6.4.1.- (acyl-CoA carboxylase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14046


  6 / 1023 MEDLINE  
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[PMID]:28197856
[Au] Autor:Yilmaz JL; Lim ZL; Beganovic M; Breazeale S; Andre C; Stymne S; Vrinten P; Senger T
[Ad] Endereço:Scandinavian Biotechnology Research (ScanBiRes) AB, 230 53, Alnarp, Sweden. Jenny.LindbergYilmaz@scanbires.com.
[Ti] Título:Determination of Substrate Preferences for Desaturases and Elongases for Production of Docosahexaenoic Acid from Oleic Acid in Engineered Canola.
[So] Source:Lipids;52(3):207-222, 2017 Mar.
[Is] ISSN:1558-9307
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in plant seed oils has been pursued to improve availability of these omega-3 fatty acids that provide important human health benefits. Canola (Brassica napus), through the introduction of 10 enzymes, can convert oleic acid (OLA) into EPA and ultimately DHA through a pathway consisting of two elongation and five desaturation steps. Herein we present an assessment of the substrate specificity of the seven desaturases and three elongases that were introduced into canola by expressing individual proteins in yeast. In vivo feeding experiments were conducted with 14 potential fatty acid intermediates in an OLA to DHA pathway to determine the fatty acid substrate profiles for each enzyme. Membrane fractions were prepared from yeast expression strains and shown to contain active enzymes. The elongases, as expected, extended acyl-CoA substrates in the presence of malonyl-CoA. To distinguish between enzymes that desaturate CoA- and phosphatidylcholine-linked fatty acid substrates, we developed a novel in vitro method. We show that a delta-12 desaturase from Phytophthora sojae, an omega-3 desaturase from Phytophthora infestans and a delta-4 desaturase from Thraustochytrium sp., all prefer phosphatidylcholine-linked acyl substrates with comparatively low use of acyl-CoA substrates. To further validate our method, a delta-9 desaturase from Saccharomyces cerevisiae was confirmed to use acyl-CoA as substrate, but could not use phosphatidylcholine-linked substrates. The results and the assay methods presented herein will be useful in efforts to improve modeling of fatty acid metabolism and production of EPA and DHA in plants.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Acil Coenzima A/metabolismo
Brassica napus/enzimologia
Ácidos Docosa-Hexaenoicos/metabolismo
Ácidos Graxos Dessaturases/metabolismo
Malonil Coenzima A/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Brassica napus/química
Brassica napus/genética
Ácido Eicosapentaenoico/metabolismo
Ácidos Graxos Dessaturases/genética
Engenharia Genética
Seres Humanos
Ácido Oleico/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Saccharomyces cerevisiae/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Plant Proteins); 25167-62-8 (Docosahexaenoic Acids); 2UMI9U37CP (Oleic Acid); 524-14-1 (Malonyl Coenzyme A); AAN7QOV9EA (Eicosapentaenoic Acid); EC 1.14.19.- (Fatty Acid Desaturases); EC 2.3.1.- (Acetyltransferases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170721
[Lr] Data última revisão:
170721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1007/s11745-017-4235-4


  7 / 1023 MEDLINE  
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[PMID]:28078904
[Au] Autor:Liu C; Ding Y; Xian M; Liu M; Liu H; Ma Q; Zhao G
[Ad] Endereço:a CAS Key Lab of Biobased Materials , Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences , Qingdao , China.
[Ti] Título:Malonyl-CoA pathway: a promising route for 3-hydroxypropionate biosynthesis.
[So] Source:Crit Rev Biotechnol;37(7):933-941, 2017 Nov.
[Is] ISSN:1549-7801
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:3-Hydroxypropionate (3HP) is an attractive platform chemical, serving as a precursor to a variety of commodity chemicals like acrylate and acrylamide, as well as a monomer of a biodegradable plastic. To establish a sustainable way to produce these commercially important chemicals and materials, fermentative production of 3HP is widely investigated in recent years. It is reported that 3HP can be produced from several intermediates, such as glycerol, malonyl-CoA, and ß-alanine. Among all these biosynthetic routes, the malonyl-CoA pathway has some distinct advantages, including a broad feedstock spectrum, thermodynamic feasibility, and redox neutrality. To date, this pathway has been successfully constructed in various species including Escherichia coli, yeast and cyanobacteria, and optimized through carbon flux redirection, enzyme screening and engineering, and an increasing supply of energy and cofactors, resulting in significantly enhanced 3HP titer up to 40 g/L. These results show the feasibility of commercial manufacturing of 3HP and its derivatives in the future.
[Mh] Termos MeSH primário: Malonil Coenzima A/metabolismo
[Mh] Termos MeSH secundário: Escherichia coli
Ácido Láctico
Oxirredução
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
33X04XA5AT (Lactic Acid); 524-14-1 (Malonyl Coenzyme A)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1080/07388551.2016.1272093


  8 / 1023 MEDLINE  
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[PMID]:28054946
[Au] Autor:Lehmann D; Motlagh L; Robaa D; Zierz S
[Ad] Endereço:Department of Neurology, Martin-Luther-University Halle-Wittenberg, Ernst-Grube-Str. 40, 06120 Halle/Saale, Germany. diana.lehmann@uk-halle.de.
[Ti] Título:Muscle Carnitine Palmitoyltransferase II Deficiency: A Review of Enzymatic Controversy and Clinical Features.
[So] Source:Int J Mol Sci;18(1), 2017 Jan 03.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:CPT (carnitine palmitoyltransferase) II muscle deficiency is the most common form of muscle fatty acid metabolism disorders. In contrast to carnitine deficiency, it is clinically characterized by attacks of myalgia and rhabdomyolysis without persistent muscle weakness and lipid accumulation in muscle fibers. The biochemical consequences of the disease-causing mutations are still discussed controversially. CPT activity in muscles of patients with CPT II deficiency ranged from not detectable to reduced to normal. Based on the observation that in patients, total CPT is completely inhibited by malony-CoA, a deficiency of malonyl-CoA-insensitive CPT II has been suggested. In contrast, it has also been shown that in muscle CPT II deficiency, CPT II protein is present in normal concentrations with normal enzymatic activity. However, CPT II in patients is abnormally sensitive to inhibition by malonyl-CoA, Triton X-100 and fatty acid metabolites. A recent study on human recombinant CPT II enzymes (His6- - CPT2 and His6- - CPT2/S113L) revealed that the wild-type and the S113L variants showed the same enzymatic activity. However, the mutated enzyme showed an abnormal thermal destabilization at 40 and 45 °C and an abnormal sensitivity to inhibition by malony-CoA. The thermolability of the mutant enzyme might explain why symptoms in muscle CPT II deficiency mainly occur during prolonged exercise, infections and exposure to cold. In addition, the abnormally regulated enzyme might be mostly inhibited when the fatty acid metabolism is stressed.
[Mh] Termos MeSH primário: Carnitina O-Palmitoiltransferase/deficiência
Carnitina O-Palmitoiltransferase/genética
Erros Inatos do Metabolismo/genética
Erros Inatos do Metabolismo/patologia
Músculos/patologia
Doenças Musculares/genética
Doenças Musculares/patologia
[Mh] Termos MeSH secundário: Animais
Carnitina O-Palmitoiltransferase/análise
Carnitina O-Palmitoiltransferase/metabolismo
Estabilidade Enzimática
Seres Humanos
Malonil Coenzima A/metabolismo
Erros Inatos do Metabolismo/complicações
Erros Inatos do Metabolismo/metabolismo
Modelos Moleculares
Músculos/enzimologia
Músculos/metabolismo
Doenças Musculares/complicações
Doenças Musculares/metabolismo
Mutação
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
524-14-1 (Malonyl Coenzyme A); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE


  9 / 1023 MEDLINE  
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[PMID]:27941154
[Au] Autor:Miotto PM; Steinberg GR; Holloway GP
[Ad] Endereço:Department of Human Health and Nutritional Sciences, University of Guelph, 50 Stone Rd East, Guelph, Ontario, Canada N1G 2W1 pmiotto@uoguelph.ca ghollowa@uoguelph.ca.
[Ti] Título:Controlling skeletal muscle CPT-I malonyl-CoA sensitivity: the importance of AMPK-independent regulation of intermediate filaments during exercise.
[So] Source:Biochem J;474(4):557-569, 2017 Feb 15.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The obligatory role of carnitine palmitoyltransferase-I (CPT-I) in mediating mitochondrial lipid transport is well established, a process attenuated by malonyl-CoA (M-CoA). However, the necessity of reducing M-CoA concentrations to promote lipid oxidation has recently been challenged, suggesting external regulation on CPT-I. Since previous work in hepatocytes suggests the involvement of the intermediate filament fraction of the cytoskeleton in regulating CPT-I, we investigated in skeletal muscle if CPT-I sensitivity for M-CoA inhibition could be regulated by the intermediate filaments, and whether AMP-activated protein kinase (AMPK) could be involved in this process. Chemical disruption (3,3'-iminodipropionitrile, IDPN) of the intermediate filaments did not alter mitochondrial respiration or sensitivity for numerous substrates (palmitoyl-CoA, ADP, palmitoyl carnitine and pyruvate). In contrast, IDPN reduced CPT-I sensitivity for M-CoA inhibition in permeabilized muscle fibers, identifying M-CoA kinetics as a specific target for intermediate filament regulation. Importantly, exercise mimicked the effect of IDPN on M-CoA sensitivity, suggesting that intermediate filament disruption in vivo is physiologically important for CPT-I regulation. To ascertain a potential mechanism, since AMPK is activated during exercise, AMPK ß1ß2-KO mice were utilized in an attempt to ablate the observed exercise response. Unexpectedly, these mice displayed drastic attenuation in resting M-CoA sensitivity, such that exercise and IDPN could not further alter M-CoA sensitivity. These data suggest that AMPK is not required for the regulation of the intermediate filament interaction with CPT-I. Altogether, these data highlight that M-CoA sensitivity is important for regulating mitochondrial lipid transport. Moreover, M-CoA sensitivity appears to be regulated by intermediate filament interaction with CPT-I, a process that is important when metabolic homeostasis is challenged.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por AMP/metabolismo
Carnitina O-Palmitoiltransferase/metabolismo
Filamentos Intermediários/metabolismo
Malonil Coenzima A/metabolismo
Mitocôndrias Musculares/metabolismo
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Difosfato de Adenosina/metabolismo
Animais
Carnitina O-Palmitoiltransferase/genética
Regulação da Expressão Gênica
Filamentos Intermediários/efeitos dos fármacos
Masculino
Camundongos
Camundongos Knockout
Mitocôndrias Musculares/genética
Músculo Esquelético/efeitos dos fármacos
Nitrilos/farmacologia
Oxirredução
Fosforilação Oxidativa
Palmitoil Coenzima A/metabolismo
Palmitoilcarnitina/metabolismo
Condicionamento Físico Animal
Ácido Pirúvico/metabolismo
Transdução de Sinais
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nitriles); 1763-10-6 (Palmitoyl Coenzyme A); 1935-18-8 (Palmitoylcarnitine); 3XP1CVU865 (3,3'-iminodipropionitrile); 524-14-1 (Malonyl Coenzyme A); 61D2G4IYVH (Adenosine Diphosphate); 8558G7RUTR (Pyruvic Acid); EC 2.3.1.21 (CPT1B protein, mouse); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160913


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[PMID]:27897367
[Au] Autor:Taguchi T; Awakawa T; Nishihara Y; Kawamura M; Ohnishi Y; Ichinose K
[Ad] Endereço:Research Institute of Pharmaceutical Sciences, Musashino University, Shinmachi, Nishitokyo-shi, Tokyo, 202-8585, Japan.
[Ti] Título:Bifunctionality of ActIV as a Cyclase-Thioesterase Revealed by in Vitro Reconstitution of Actinorhodin Biosynthesis in Streptomyces coelicolor A3(2).
[So] Source:Chembiochem;18(3):316-323, 2017 Feb 01.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Type II polyketide synthases iteratively generate a nascent polyketide thioester of the acyl carrier protein (ACP); this is structurally modified to produce an ACP-free intermediate towards the final metabolite. However, the timing of ACP off-loading is not well defined because of the lack of an apparent thioesterase (TE) among relevant biosynthetic enzymes. Here, ActIV, which had been assigned as a second ring cyclase (CYC) in actinorhodin (ACT) biosynthesis, was shown to possess TE activity in vitro with a model substrate, anthraquinone-2-carboxylic acid-N-acetylcysteamine. In order to investigate its function further, the ACT biosynthetic pathway in Streptomyces coelicolor A3(2) was reconstituted in vitro in a stepwise fashion up to (S)-DNPA, and the product of ActIV reaction was characterized as an ACP-free bicyclic intermediate. These findings indicate that ActIV is a bifunctional CYC-TE and provide clear evidence for the release timing of the intermediate from the ACP anchor.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Policetídeo Sintases/metabolismo
Streptomyces coelicolor/metabolismo
[Mh] Termos MeSH secundário: Antraquinonas/química
Antraquinonas/metabolismo
Proteínas de Bactérias/genética
Malonil Coenzima A/metabolismo
Oxirredutases/genética
Oxirredutases/metabolismo
Policetídeo Sintases/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/isolamento & purificação
Streptomyces coelicolor/genética
Tioléster Hidrolases/genética
Tioléster Hidrolases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthraquinones); 0 (Bacterial Proteins); 0 (Recombinant Proteins); 524-14-1 (Malonyl Coenzyme A); 79956-01-7 (Polyketide Synthases); EC 1.- (Oxidoreductases); EC 3.1.2.- (Thiolester Hydrolases); G4HH387T6Z (actinorhodin)
[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:161130
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600589



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