Base de dados : MEDLINE
Pesquisa : D08.811.682.657.350.825 [Categoria DeCS]
Referências encontradas : 6 [refinar]
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  1 / 6 MEDLINE  
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[PMID]:25958347
[Au] Autor:Song C; Li H; Sheng L; Zhang X
[Ad] Endereço:Key Laboratory of Conservation Biology for Endangered Wildlife of Ministry of Education and College of Life Sciences, Zhejiang University, Hangzhou 310058, People's Republic of China; School of Chemistry and Material Engineering, Fuyang Teachers College, Fuyang 236037, People's Republic of China.
[Ti] Título:Characterization of the interaction between superoxide dismutase and 2-oxoisovalerate dehydrogenase.
[So] Source:Gene;568(1):1-7, 2015 Aug 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Thermophiles are attractive microorganisms to study the adaptation of life in high temperature environment. It is revealed that superoxide dismutase (SOD) is essential for thermoadaptation of thermophiles. However, the SOD-mediated pathway of thermoadaptation remains unclear. To address this issue, the proteins interacted with SOD were characterized in Thermus thermophilus in this study. Based on co-immunoprecipitation and Western blot analyses, the results showed that 2-oxoisovalerate dehydrogenase α subunit was bound to SOD. The isothermal titration calorimetry analysis showed the existence of the interaction between SOD and 2-oxoisovalerate dehydrogenase α subunit. The bacterial two-hybrid data indicated that SOD was directly interacted with 2-oxoisovalerate dehydrogenase α subunit. Gene site-directed mutagenesis analysis revealed that the intracellular interaction between SOD and 2-oxoisovalerate dehydrogenase α subunit was dependent on their whole molecules. Therefore our study presented a novel aspect of SOD in the thermoadaptation of thermophiles by interaction with dehydrogenase, a key enzyme of tricarboxylic acid cycle.
[Mh] Termos MeSH primário: 2-Oxoisovalerato Desidrogenase (Acilante)/metabolismo
Proteínas de Bactérias/metabolismo
Superóxido Dismutase/metabolismo
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)/química
Adaptação Fisiológica
Sequência de Aminoácidos
Proteínas de Bactérias/química
Dados de Sequência Molecular
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Mapeamento de Interação de Proteínas
Superóxido Dismutase/química
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.15.1.1 (Superoxide Dismutase); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating))
[Em] Mês de entrada:1508
[Cu] Atualização por classe:150616
[Lr] Data última revisão:
150616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150511
[St] Status:MEDLINE


  2 / 6 MEDLINE  
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[PMID]:25157082
[Au] Autor:Nohara K; Orita I; Nakamura S; Imanaka T; Fukui T
[Ad] Endereço:Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan.
[Ti] Título:Genetic examination and mass balance analysis of pyruvate/amino acid oxidation pathways in the hyperthermophilic archaeon Thermococcus kodakarensis.
[So] Source:J Bacteriol;196(22):3831-9, 2014 Nov.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The present study investigated the simultaneous oxidation of pyruvate and amino acids during H2-evolving growth of the hyperthermophilic archaeon Thermococcus kodakarensis. The comparison of mass balance between a cytosolic hydrogenase (HYH)-deficient strain (the ΔhyhBGSL strain) and the parent strain indicated that NADPH generated via H2 uptake by HYH was consumed by reductive amination of 2-oxoglutarate catalyzed by glutamate dehydrogenase. Further examinations were done to elucidate functions of three enzymes potentially involved in pyruvate oxidation: pyruvate formate-lyase (PFL), pyruvate:ferredoxin oxidoreductase (POR), and 2-oxoisovalerate:ferredoxin oxidoreductase (VOR) under the HYH-deficient background in T. kodakarensis. No significant change was observed by deletion of pflDA, suggesting that PFL had no critical role in pyruvate oxidation. The growth properties and mass balances of ΔporDAB and ΔvorDAB strains indicated that POR and VOR specifically functioned in oxidation of pyruvate and branched-chain amino acids, respectively, and the lack of POR or VOR was compensated for by promoting the oxidation of another substrate driven by the remaining oxidoreductase. The H2 yields from the consumed pyruvate and amino acids were increased from 31% by the parent strain to 67% and 82% by the deletion of hyhBGSL and double deletion of hyhBGSL and vorDAB, respectively. Significant discrepancies in the mass balances were observed in excess formation of acetate and NH3, suggesting the presence of unknown metabolisms in T. kodakarensis grown in the rich medium containing pyruvate.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Proteínas Arqueais/metabolismo
Regulação da Expressão Gênica em Archaea/fisiologia
Ácido Pirúvico/metabolismo
Thermococcus/genética
Thermococcus/metabolismo
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)/genética
2-Oxoisovalerato Desidrogenase (Acilante)/metabolismo
Acetiltransferases/genética
Acetiltransferases/metabolismo
Proteínas Arqueais/genética
Deleção de Genes
Hidrogênio/metabolismo
Hidrogenase/genética
Hidrogenase/metabolismo
Oxirredução
Piruvato Sintase/genética
Piruvato Sintase/metabolismo
Thermococcus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Archaeal Proteins); 7YNJ3PO35Z (Hydrogen); 8558G7RUTR (Pyruvic Acid); EC 1.12.7.2 (Hydrogenase); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating)); EC 1.2.7.1 (Pyruvate Synthase); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.54 (formate C-acetyltransferase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140827
[St] Status:MEDLINE
[do] DOI:10.1128/JB.02021-14


  3 / 6 MEDLINE  
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[PMID]:7585357
[Au] Autor:Lounès A; Lebrihi A; Benslimane C; Lefebvre G; Germain P
[Ad] Endereço:Laboratoire de microbiologie industrielle et alimentaire, ENSAIA, Institut national polytechnique de Lorraine, Vandoeuvre, France.
[Ti] Título:Regulation of valine catabolism by ammonium in Streptomyces ambofaciens, producer of spiramycin.
[So] Source:Can J Microbiol;41(9):800-8, 1995 Sep.
[Is] ISSN:0008-4166
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:In Streptomyces ambofaciens, valine favored spiramycin biosynthesis by supplying aglycone precursors. The kinetics of valine consumption and isobutyrate production showed that isobutyrate accumulated in the cell during the growth phase, was excreted in the stationary phase, and then was reassimilated during spiramycin production. When valine was in excess, its deamination led to high ammonium excretion and to a significant drop in spiramycin production. We demonstrated that ammonium ions were the cause of the negative effect. Addition of a chelator agent, Ca3(PO4)2, improved spiramycin production by sixfold. In contrast, addition of ammonium, between 0 and 48 h, severely reduced spiramycin production. The negative effect of ammonium was reversed by addition of a catabolic intermediate of valine, isobutyrate. In addition to stimulating the specific growth rate, ammonium ions slowed down valine catabolism: the specific valine uptake rate, excretion, and reassimilation of isobutyrate were lowered by the pulse of ammonium. Our study showed that in addition to valine dehydrogenase, which provided the nitrogen necessary to the cell, ammonium ions repressed ketoisovalerate dehydrogenase, which introduced valine as carbon, energy, and aglycone precursor sources. However, valine dehydrogenase and ketoisovalerate dehydrogenase did not constitute the principal enzymatic targets of the negative effect of ammonium in spiramycin production.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Compostos de Amônio Quaternário/farmacologia
Espiramicina/biossíntese
Streptomyces/metabolismo
Valina/metabolismo
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)
Acetatos/metabolismo
Aminoácido Oxirredutases/biossíntese
Butiratos/metabolismo
Butiratos/farmacologia
Fosfatos de Cálcio/farmacologia
Divisão Celular/efeitos dos fármacos
Meios de Cultura
Dextrinas/metabolismo
Glicerol/metabolismo
Isobutiratos
Cetona Oxirredutases/biossíntese
Cinética
Oxirredutases/antagonistas & inibidores
Oxirredutases/metabolismo
Compostos de Amônio Quaternário/metabolismo
Streptomyces/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Anti-Bacterial Agents); 0 (Butyrates); 0 (Calcium Phosphates); 0 (Culture Media); 0 (Dextrins); 0 (Isobutyrates); 0 (Quaternary Ammonium Compounds); 0 (alpha-tricalcium phosphate); 0 (tetracalcium phosphate); 701EKV9RMN (calcium phosphate, monobasic, anhydrous); 8025-81-8 (Spiramycin); 8LL210O1U0 (isobutyric acid); 97Z1WI3NDX (calcium phosphate); EC 1.- (Oxidoreductases); EC 1.2.- (Ketone Oxidoreductases); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating)); EC 1.4.- (Amino Acid Oxidoreductases); HG18B9YRS7 (Valine); L11K75P92J (calcium phosphate, dibasic, anhydrous); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:9512
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:950901
[St] Status:MEDLINE


  4 / 6 MEDLINE  
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[PMID]:4004935
[Au] Autor:Wagenmakers AJ; Veerkamp JH; Schepens JT; van Moerkerk HT
[Ti] Título:Effect of clofibrate on branched-chain amino acid metabolism.
[So] Source:Biochem Pharmacol;34(12):2169-73, 1985 Jun 15.
[Is] ISSN:0006-2952
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Clofibric acid inhibited the oxidative decarboxylation of 4-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate in mitochondria and homogenates of rat liver and quadriceps muscle. In rat hemidiaphragms clofibric acid inhibited the oxidative decarboxylation of 4-methyl-2-oxopentanoate and had no effect on that of 3-methyl-2-oxobutanoate. Clofibric acid displaced branched-chain 2-oxo acids from bovine serum albumin. Clofibrate-treatment of rats decreased the actual activity and activity state of the branched-chain 2-oxo acid dehydrogenase complex in quadriceps muscle, and increased the total activity in heart and liver without a change of the activity state. All interactions of clofibric acid with the metabolism of branched-chain amino acids appear to relate to its structural resemblance to the branched-chain 2-oxo acids. Both reduced plasma and muscle concentrations of branched-chain amino acids and reduced muscle oxidation may play a role in the myopathic side-effects of clofibrate-treatment.
[Mh] Termos MeSH primário: Aminoácidos de Cadeia Ramificada/metabolismo
Clofibrato/farmacologia
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)
Animais
Descarboxilação
Técnicas In Vitro
Cetona Oxirredutases/análise
Fígado/metabolismo
Masculino
Músculos/metabolismo
Ligação Proteica
Ratos
Ratos Endogâmicos
Albumina Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); 0 (Serum Albumin); EC 1.2.- (Ketone Oxidoreductases); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating)); HPN91K7FU3 (Clofibrate)
[Em] Mês de entrada:8507
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:850615
[St] Status:MEDLINE


  5 / 6 MEDLINE  
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[PMID]:3841150
[Au] Autor:Yoshida I; Søvik O; Sweetman L; Nyhan WL
[Ti] Título:Metabolism of leucine in fibroblasts from patients with deficiencies in each of the major catabolic enzymes: branched-chain ketoacid dehydrogenase, isovaleryl-CoA dehydrogenase, 3-methylcrotonyl-CoA carboxylase, 3-methylglutaconyl-CoA hydratase, and 3-hydroxy-3-methylglutaryl-CoA lyase.
[So] Source:J Neurogenet;2(6):413-24, 1985 Dec.
[Is] ISSN:0167-7063
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The metabolism of leucine was studied in cultured human fibroblasts derived from patients with defects in each of the major steps in the catabolism of the amino acid. Intact fibroblasts were incubated with [U-14C]leucine and the organic acid products were isolated by liquid partition chromatography. In control fibroblasts the major product of leucine was 3-hydroxyisovaleric acid. This was also the case for fibroblasts with deficiency of 3-hydroxy-3-methylglutaryl-CoA lyase, 3-methylcrotonyl-CoA carboxylase and 3-methylglutaconyl-CoA hydratase. There was little or no accumulation of the compound with fibroblasts from patients with maple syrup urine disease and isovaleric acidemia.
[Mh] Termos MeSH primário: Carbono-Carbono Ligases
Hidroliases/deficiência
Cetona Oxirredutases/deficiência
Leucina/metabolismo
Ligases/deficiência
Doença da Urina de Xarope de Bordo/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-CH
Oxirredutases/deficiência
Oxo-Ácido-Liases/deficiência
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)
Células Cultivadas
Fibroblastos/metabolismo
Seres Humanos
Isovaleril-CoA Desidrogenase
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
EC 1.- (Oxidoreductases); EC 1.2.- (Ketone Oxidoreductases); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating)); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.8.4 (Isovaleryl-CoA Dehydrogenase); EC 4.1.3.- (Oxo-Acid-Lyases); EC 4.1.3.4 (3-hydroxy-3-methylglutaryl-coenzyme A lyase); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.18 (methylglutaconyl-CoA hydratase); EC 6.- (Ligases); EC 6.4.- (Carbon-Carbon Ligases); EC 6.4.1.4 (methylcrotonoyl-CoA carboxylase); GMW67QNF9C (Leucine)
[Em] Mês de entrada:8601
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:851201
[St] Status:MEDLINE


  6 / 6 MEDLINE  
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[PMID]:7330498
[Au] Autor:Velázquez A; Montiel F; Sahw KN; Carnevale A; del Castillo V
[Ti] Título:[Maple syrup urine disease. Genetic heterogeneity, heterozygote diagnosis and new therapeutic approach (author's transl)].
[Ti] Título:Enfermedad de orina de jarabe de arce: heterogeneidad genética, diagnóstico de heterocigotos y un nuevo enfoque terapéutico..
[So] Source:Rev Invest Clin;33(3):273-9, 1981 Jul-Sep.
[Is] ISSN:0034-8376
[Cp] País de publicação:Mexico
[La] Idioma:spa
[Mh] Termos MeSH primário: Doença da Urina de Xarope de Bordo/genética
[Mh] Termos MeSH secundário: 2-Oxoisovalerato Desidrogenase (Acilante)
Aminoácidos/administração & dosagem
Aminoácidos de Cadeia Ramificada/análise
Aminoácidos de Cadeia Ramificada/metabolismo
Proteínas na Dieta/administração & dosagem
Triagem de Portadores Genéticos
Seres Humanos
Lactente
Cetoácidos/análise
Cetona Oxirredutases/análise
Masculino
Doença da Urina de Xarope de Bordo/diagnóstico
Doença da Urina de Xarope de Bordo/dietoterapia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Amino Acids, Branched-Chain); 0 (Dietary Proteins); 0 (Keto Acids); EC 1.2.- (Ketone Oxidoreductases); EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating))
[Em] Mês de entrada:8204
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:810701
[St] Status:MEDLINE



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