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Pesquisa : D08.811.277.352.650.575 [Categoria DeCS]
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[PMID]:25282639
[Au] Autor:Sakihama Y; Hasunuma T; Kondo A
[Ad] Endereço:Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
[Ti] Título:Improved ethanol production from xylose in the presence of acetic acid by the overexpression of the HAA1 gene in Saccharomyces cerevisiae.
[So] Source:J Biosci Bioeng;119(3):297-302, 2015 Mar.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The hydrolysis of lignocellulosic biomass liberates sugars, primarily glucose and xylose, which are subsequently converted to ethanol by microbial fermentation. The rapid and efficient fermentation of xylose by recombinant Saccharomyces cerevisiae strains is limited by weak acids generated during biomass pretreatment processes. In particular, acetic acid negatively affects cell growth, xylose fermentation rate, and ethanol production. The ability of S. cerevisiae to efficiently utilize xylose in the presence of acetic acid is an essential requirement for the cost-effective production of ethanol from lignocellulosic hydrolysates. Here, an acetic acid-responsive transcriptional activator, HAA1, was overexpressed in a recombinant xylose-fermenting S. cerevisiae strain to yield BY4741X/HAA1. This strain exhibited improved cell growth and ethanol production from xylose under aerobic and oxygen limited conditions, respectively, in the presence of acetic acid. The HAA1p regulon enhanced transcript levels in BY4741X/HAA1. The disruption of PHO13, a p-nitrophenylphosphatase gene, in BY4741X/HAA1 led to further improvement in both yeast growth and the ability to ferment xylose, indicating that HAA1 overexpression and PHO13 deletion act by different mechanisms to enhance ethanol production.
[Mh] Termos MeSH primário: Ácido Acético/metabolismo
Etanol/metabolismo
Fermentação
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Xilose/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/genética
Ácido Acético/farmacologia
Aerobiose
Meios de Cultura/química
Fermentação/efeitos dos fármacos
Expressão Gênica
Saccharomyces cerevisiae/efeitos dos fármacos
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); 0 (Haa1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 3K9958V90M (Ethanol); A1TA934AKO (Xylose); EC 3.1.3.41 (4-Nitrophenylphosphatase); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:150210
[Lr] Data última revisão:
150210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141006
[St] Status:MEDLINE


  2 / 656 MEDLINE  
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[PMID]:24966040
[Au] Autor:Li YC; Gou ZX; Liu ZS; Tang YQ; Akamatsu T; Kida K
[Ad] Endereço:College of Light Industry Textile and Food Engineering, Sichuan University, Chengdu, 610064, Sichuan, China.
[Ti] Título:Synergistic effects of TAL1 over-expression and PHO13 deletion on the weak acid inhibition of xylose fermentation by industrial Saccharomyces cerevisiae strain.
[So] Source:Biotechnol Lett;36(10):2011-21, 2014 Oct.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the industrial production of bioethanol from lignocellulosic biomass, a strain of Saccharomyces cerevisiae that can ferment xylose in the presence of inhibitors is of utmost importance. The recombinant, industrial-flocculating S. cerevisiae strain NAPX37, which can ferment xylose, was used as the parent to delete the gene encoding p-nitrophenylphosphatase (PHO13) and overexpress the gene encoding transaldolase (TAL1) to evaluate the synergistic effects of these two genes on xylose fermentation in the presence of weak acid inhibitors, including formic, acetic, or levulinic acids. TAL1 over-expression or PHO13 deletion improved xylose fermentation as well as the tolerance of NAPX37 to all three weak acids. The simultaneous deletion of PHO13 and the over-expression of TAL1 had synergistic effects and improved ethanol production and reduction of xylitol accumulation in the absence and presence of weak acid inhibitors.
[Mh] Termos MeSH primário: Microbiologia Industrial
Saccharomyces cerevisiae/genética
Xilose/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/genética
Ácido Acético/metabolismo
Fermentação
Formiatos/metabolismo
Deleção de Genes
Expressão Gênica
Ácidos Levulínicos/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/metabolismo
Transaldolase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Formates); 0 (Levulinic Acids); 0YIW783RG1 (formic acid); A1TA934AKO (Xylose); EC 2.2.1.2 (Transaldolase); EC 3.1.3.41 (4-Nitrophenylphosphatase); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140627
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-014-1581-7


  3 / 656 MEDLINE  
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[PMID]:24915075
[Au] Autor:Shen T; Guo Z; Ji C
[Ad] Endereço:State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
[Ti] Título:Structure of a His170Tyr mutant of thermostable pNPPase from Geobacillus stearothermophilus.
[So] Source:Acta Crystallogr F Struct Biol Commun;70(Pt 6):697-702, 2014 Jun.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Using directed evolution based on random mutagenesis and heat-treated selection, a thermostable His170Tyr mutant of Geobacillus stearothermophilus thermostable p-nitrophenylphosphatase (TpNPPase) was obtained. The temperature at which the His170Tyr mutant lost 50% of its activity (T1/2) was found to be 4.40 K higher than that of wild-type TpNPPase, and the melting temperature of the His170Tyr mutant increased by 2.39 K. The crystal structure of the His170Tyr mutant was then determined at 2.0 Šresolution in the presence of a sodium ion and a sulfate ion in the active site. The cap domain of chain B shows a half-closed conformation. The hydrophobic side chain of the mutated residue, the hydroxyphenyl group, forms a hydrophobic contact with the methyl group of Ala166. This hydrophobic interaction was found using the Protein Interactions Calculator (PIC) web server with an interaction distance of 4.6 Å, and might be a key factor in the thermostabilization of the His170Tyr mutant. This study potentially offers a molecular basis for both investigation of the catalytic mechanism and thermostable protein engineering.
[Mh] Termos MeSH primário: 4-Nitrofenilfosfatase/metabolismo
Geobacillus stearothermophilus/enzimologia
Histidina/química
Tirosina/química
[Mh] Termos MeSH secundário: Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
42HK56048U (Tyrosine); 4QD397987E (Histidine); EC 3.1.3.41 (4-Nitrophenylphosphatase)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140611
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X14007341


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[PMID]:24816799
[Au] Autor:Mahmmoud YA; Shattock M; Cornelius F; Pavlovic D
[Ad] Endereço:Department of Biomedicine, University of Aarhus, DK-8000 Aarhus C, Denmark.
[Ti] Título:Inhibition of K+ transport through Na+, K+-ATPase by capsazepine: role of membrane span 10 of the α-subunit in the modulation of ion gating.
[So] Source:PLoS One;9(5):e96909, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Capsazepine (CPZ) inhibits Na+,K+-ATPase-mediated K+-dependent ATP hydrolysis with no effect on Na+-ATPase activity. In this study we have investigated the functional effects of CPZ on Na+,K+-ATPase in intact cells. We have also used well established biochemical and biophysical techniques to understand how CPZ modifies the catalytic subunit of Na+,K+-ATPase. In isolated rat cardiomyocytes, CPZ abolished Na+,K+-ATPase current in the presence of extracellular K+. In contrast, CPZ stimulated pump current in the absence of extracellular K+. Similar conclusions were attained using HEK293 cells loaded with the Na+ sensitive dye Asante NaTRIUM green. Proteolytic cleavage of pig kidney Na+,K+-ATPase indicated that CPZ stabilizes ion interaction with the K+ sites. The distal part of membrane span 10 (M10) of the α-subunit was exposed to trypsin cleavage in the presence of guanidinum ions, which function as Na+ congener at the Na+ specific site. This effect of guanidinium was amplified by treatment with CPZ. Fluorescence of the membrane potential sensitive dye, oxonol VI, was measured following addition of substrates to reconstituted inside-out Na+,K+-ATPase. CPZ increased oxonol VI fluorescence in the absence of K+, reflecting increased Na+ efflux through the pump. Surprisingly, CPZ induced an ATP-independent increase in fluorescence in the presence of high extravesicular K+, likely indicating opening of an intracellular pathway selective for K+. As revealed by the recent crystal structure of the E1.AlF4-.ADP.3Na+ form of the pig kidney Na+,K+-ATPase, movements of M5 of the α-subunit, which regulate ion selectivity, are controlled by the C-terminal tail that extends from M10. We propose that movements of M10 and its cytoplasmic extension is affected by CPZ, thereby regulating ion selectivity and transport through the K+ sites in Na+,K+-ATPase.
[Mh] Termos MeSH primário: Capsaicina/análogos & derivados
Domínio Catalítico
Membrana Celular/efeitos dos fármacos
Ativação do Canal Iônico/efeitos dos fármacos
Potássio/metabolismo
ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores
ATPase Trocadora de Sódio-Potássio/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/antagonistas & inibidores
4-Nitrofenilfosfatase/metabolismo
Animais
Transporte Biológico/efeitos dos fármacos
Capsaicina/farmacologia
Membrana Celular/enzimologia
Endopeptidase K/metabolismo
Inibidores Enzimáticos/farmacologia
Concentração de Íons de Hidrogênio
Hidrólise/efeitos dos fármacos
Espaço Intracelular/efeitos dos fármacos
Espaço Intracelular/metabolismo
Isoxazóis/metabolismo
Miócitos Cardíacos/citologia
Miócitos Cardíacos/efeitos dos fármacos
Miócitos Cardíacos/metabolismo
Proteólise/efeitos dos fármacos
Ratos
Sódio/metabolismo
ATPase Trocadora de Sódio-Potássio/química
Temperatura Ambiente
Tripsina/metabolismo
Vanadatos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Isoxazoles); 3WHH0066W5 (Vanadates); 64724-75-0 (oxonol VI); 9NEZ333N27 (Sodium); EC 3.1.3.41 (4-Nitrophenylphosphatase); EC 3.4.21.4 (Trypsin); EC 3.4.21.64 (Endopeptidase K); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); LFW48MY844 (capsazepine); RWP5GA015D (Potassium); S07O44R1ZM (Capsaicin)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140513
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0096909


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[PMID]:24256105
[Au] Autor:Guo Z; Wang F; Shen T; Huang J; Wang Y; Ji C
[Ti] Título:Crystal structure of thermostable p-nitrophenylphosphatase from Bacillus Stearothermophilus (Bs-TpNPPase).
[So] Source:Protein Pept Lett;21(5):483-9, 2014 May.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Thermostable p-nitrophenylphosphatase from Bacillus Stearothermophilus (Bs-TpNPPase) is involved in the Mg(2+)-dependent hydrolysis of the phosphoenzyme at an optimum reaction temperature of 55°C. Bs-TpNPPase has been cloned and overexpressed in the E.coli M15 strain. Based on the conserved active sites, the protein was suggested to be a member of the haloalkanoate dehalogenase (HAD) superfamily. Two site-specific point mutants of Bs-TpNPPase were prepared by changing the catalytic Asp10 and Thr43 to Ala10 and Ala43, respectively. The activity of the two mutants further confirms Bs-TpNPPase as a member of the HAD superfamily. HAD superfamily can be divided into the four subfamilies and play several biochemical roles such as DNA repair, signal transduction and secondary metabolism. To understand the relationship between structure and thermostability in HAD superfamily, Bs-TpNPPase from Bacillus Stearothermophilus was selected. The X-ray crystal structure of Bs-TpNPPase was determined at 1.5A resolution using the molecular replacement phasing method. The structure of Bs-TpNPPase has been deposited and the PDB code is 4KN8. Compared with Bsp, a mesophilic prokaryotic putative p-nitrophenyl phosphatase from Bacillus Subtilis, Bs- TpNPPase showed highly homology but variations in the level of leucine content, aromatic clusters, cation-Pi and hydrophobic interaction. These differences may affect the thermal stability of the protein. The crystal structure of Bs-TpNPPase described herein may serve as a guide to better understand the mechanism of thermostability and provide insights for further mutation work.
[Mh] Termos MeSH primário: 4-Nitrofenilfosfatase/química
Geobacillus stearothermophilus/enzimologia
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/genética
Cristalografia por Raios X
Geobacillus stearothermophilus/química
Geobacillus stearothermophilus/genética
Modelos Moleculares
Mutagênese Sítio-Dirigida
Conformação Proteica
Estabilidade Proteica
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.1.3.41 (4-Nitrophenylphosphatase)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:140221
[Lr] Data última revisão:
140221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131122
[St] Status:MEDLINE


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[PMID]:23810666
[Au] Autor:Tomitaka M; Taguchi H; Fukuda K; Akamatsu T; Kida K
[Ad] Endereço:Department of Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto 860-0082, Japan.
[Ti] Título:Isolation and characterization of a mutant recombinant Saccharomyces cerevisiae strain with high efficiency xylose utilization.
[So] Source:J Biosci Bioeng;116(6):706-15, 2013 Dec.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:A recombinant xylose-utilizing Saccharomyces cerevisiae strain carrying one copy of heterologous XYL1 and XYL2 from Pichia stipitis and endogenous XKS1 under the control of the TDH3 promoter in the chromosomal DNA was constructed from the industrial haploid yeast strain NAM34-4C, which showed thermotolerance and acid tolerance. The recombinant S. cerevisiae strain SCB7 grew in minimal medium containing xylose as the sole carbon source, and its shortest generation time (G(short)) was 5 h. From this strain, four mutants showing rapid growth (G(short) = 2.5 h) in the minimal medium were isolated. The mutants carried four mutations that were classified into three linkage groups. Three mutations were dominant and one mutation was recessive to the wild type allele. The recessive mutation was in the PHO13 gene encoding para-nitrophenyl phosphatase. The other mutant genes were not linked to TAL1 gene encoding transaldolase. When the mutants and their parental strain were used for the batch fermentation in a complex medium at pH 4.0 containing 30 g/L xylose at 35 °C with shaking (60 rpm) and an initial cell density (Absorbance at 660 nm) of 1.0, all mutants showed efficient ethanol production and xylose consumption from the early stage of the fermentation culture. In two mutants, within 24 h, 4.8 g/L ethanol was produced, and the ethanol yield was 47%, which was 1.4 times higher than that achieved with the parental strain. The xylose concentration in the medium containing the mutant decreased linearly at a rate of 1 g/L/h until 24 h.
[Mh] Termos MeSH primário: Biocombustíveis/microbiologia
Etanol/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Xilose/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/genética
4-Nitrofenilfosfatase/metabolismo
Endo-1,4-beta-Xilanases/genética
Endo-1,4-beta-Xilanases/metabolismo
Fermentação
Genes Dominantes
Genes Recessivos
Gliceraldeído-3-Fosfato Desidrogenase (Fosforiladora)/genética
Mutação
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/metabolismo
Transaldolase/genética
Transaldolase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biofuels); 0 (Saccharomyces cerevisiae Proteins); 3K9958V90M (Ethanol); A1TA934AKO (Xylose); EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)); EC 1.2.1.12 (TDH3 protein, S cerevisiae); EC 2.2.1.2 (Transaldolase); EC 2.2.1.2. (TAL1 protein, S cerevisiae); EC 3.1.3.41 (4-Nitrophenylphosphatase); EC 3.2.1.8 (Endo-1,4-beta Xylanases); EC 3.2.1.8 (xyl1 xylanase)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131101
[Lr] Data última revisão:
131101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130702
[St] Status:MEDLINE


  7 / 656 MEDLINE  
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[PMID]:22901764
[Au] Autor:Landry RP; Martinez E; DeLeo JA; Romero-Sandoval EA
[Ad] Endereço:Dartmouth Medical School, Department of Anesthesiology, Lebanon, New Hampshire, USA.
[Ti] Título:Spinal cannabinoid receptor type 2 agonist reduces mechanical allodynia and induces mitogen-activated protein kinase phosphatases in a rat model of neuropathic pain.
[So] Source:J Pain;13(9):836-48, 2012 Sep.
[Is] ISSN:1528-8447
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Peripheral nerve injury generally results in spinal neuronal and glial plastic changes associated with chronic behavioral hypersensitivity. Spinal mitogen-activated protein kinases (MAPKs), eg, p38 or extracellular signal-regulated kinases (ERKs), are instrumental in the development of chronic allodynia in rodents, and new p38 inhibitors have shown potential in acute and neuropathic pain patients. We have previously shown that the cannabinoid type 2 receptor agonist JWH015 inhibits ERK activity by inducing MAPK phosphatase (MKP)-1 and MKP-3 (the major regulators of MAPKs) in vitro in microglial cells. Therefore, we decided to investigate the role of these phosphatases in the mechanisms of action of JWH015 in vivo using the rat L5 nerve transection model of neuropathic pain. We observed that peripheral nerve injury reduced spinal MKP-1/3 expression and activity and that intrathecal JWH015 reduced established L5 nerve injury-induced allodynia, enhanced spinal MKP-1/3 expression and activity, and reduced the phosphorylated form of p38 and ERK-1/2. Triptolide, a pharmacological blocker of MKP-1 and MKP-3 expression, inhibited JWH015's effects, suggesting that JWH015 exerts its antinociceptive effects by modulating MKP-1 and MKP-3. JWH015-induced antinociception and MKP-1 and MKP-3 expression were inhibited by the cannabinoid type 2 receptor antagonist AM630. Our data suggest that MKP-1 and MKP-3 are potential targets for novel analgesic drugs. PERSPECTIVE: MAPKs are pivotal in the development of chronic allodynia in rodent models of neuropathic pain. A cannabinoid type 2 receptor agonist, JWH015, reduced neuropathic allodynia in rats by reducing MAPK phosphorylation and inducing spinal MAPK phosphatases 1 and 3, the major regulators of MAPKs.
[Mh] Termos MeSH primário: Hiperalgesia
Indóis/uso terapêutico
Fosfatases da Proteína Quinase Ativada por Mitógeno/metabolismo
Neuralgia/complicações
Receptor CB2 de Canabinoide/agonistas
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/metabolismo
Animais
Modelos Animais de Doenças
Diterpenos/uso terapêutico
Fosfatase 1 de Especificidade Dupla/metabolismo
Fosfatase 6 de Especificidade Dupla/metabolismo
Compostos de Epóxi/uso terapêutico
Regulação da Expressão Gênica/efeitos dos fármacos
Hiperalgesia/tratamento farmacológico
Hiperalgesia/etiologia
Hiperalgesia/patologia
Imunossupressores/uso terapêutico
Indóis/farmacologia
Masculino
Fosfatases da Proteína Quinase Ativada por Mitógeno/classificação
Proteínas do Tecido Nervoso/metabolismo
Fenantrenos/uso terapêutico
Ratos
Ratos Sprague-Dawley
Receptor CB2 de Canabinoide/antagonistas & inibidores
Transdução de Sinais/efeitos dos fármacos
Medula Espinal/efeitos dos fármacos
Medula Espinal/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diterpenes); 0 (Epoxy Compounds); 0 (Immunosuppressive Agents); 0 (Indoles); 0 (Nerve Tissue Proteins); 0 (Phenanthrenes); 0 (Receptor, Cannabinoid, CB2); 19ALD1S53J (triptolide); EC 3.1.3.16 (Mitogen-Activated Protein Kinase Phosphatases); EC 3.1.3.41 (4-Nitrophenylphosphatase); EC 3.1.3.48 (Dual Specificity Phosphatase 1); EC 3.1.3.48 (Dual Specificity Phosphatase 6); EC 3.1.3.48 (Dusp1 protein, rat); EC 3.1.3.48 (Dusp6 protein, rat); U1LNJ6NBKA (iodopravadoline); W4FL204T10 (JHW 015)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120821
[St] Status:MEDLINE
[do] DOI:10.1016/j.jpain.2012.05.013


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[PMID]:22574873
[Au] Autor:Contó MB; Venditti MA
[Ad] Endereço:Departamento de Psicobiologia, Universidade Federal de São Paulo, Escola Paulista de Medicina, São Paulo, SP, Brazil. mmmarcos@uol.com.br
[Ti] Título:In vitro studies of the influence of glutamatergic agonists on the Na+,K(+)-ATPase and K(+)-p-nitrophenylphosphatase activities in the hippocampus and frontal cortex of rats.
[So] Source:J Negat Results Biomed;11:12, 2012 May 10.
[Is] ISSN:1477-5751
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The overstimulation of excitatory glutamatergic neurotransmission and the inhibition of Na(+),K(+)-ATPase enzymatic activity have both been implicated in neurotoxicity and are possibly related to the pathogenesis of epilepsy and neurodegenerative disorders. In the present study, we investigated whether glutamatergic stimulation by the glutamatergic agonists glutamate, α-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA), kainate and N-methyl-d-aspartate (NMDA) modulates the Na(+),K(+)-ATPase and the K(+)-p-nitrophenylphosphatase activities in the crude synaptosomal fraction of the hippocampus and the frontal cortex of rats. RESULTS: Our results demonstrated that these glutamatergic agonists did not influence the activities of Na(+),K(+)-ATPase or K(+)-p-nitrophenylphosphatase in the brain structures analyzed. Assays with lower concentrations of ATP to analyze the preferential activity of the Na(+),K(+)-ATPase isoform with high affinity for ATP did not show any influence either. CONCLUSIONS: These findings suggest that under our experimental conditions, the stimulation of glutamatergic receptors does not influence the kinetics of the Na(+),K(+)-ATPase enzyme in the hippocampus and frontal cortex.
[Mh] Termos MeSH primário: 4-Nitrofenilfosfatase/metabolismo
Agonistas de Aminoácidos Excitatórios/farmacologia
Lobo Frontal/efeitos dos fármacos
Hipocampo/efeitos dos fármacos
ATPase Trocadora de Sódio-Potássio/metabolismo
[Mh] Termos MeSH secundário: Animais
Lobo Frontal/enzimologia
Hipocampo/enzimologia
Ácido Caínico/farmacologia
Masculino
N-Metilaspartato/farmacologia
Ratos
Ratos Wistar
Transmissão Sináptica
Ácido alfa-Amino-3-hidroxi-5-metil-4-isoxazol Propiônico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Excitatory Amino Acid Agonists); 6384-92-5 (N-Methylaspartate); 77521-29-0 (alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid); EC 3.1.3.41 (4-Nitrophenylphosphatase); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); SIV03811UC (Kainic Acid)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120512
[St] Status:MEDLINE
[do] DOI:10.1186/1477-5751-11-12


  9 / 656 MEDLINE  
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[PMID]:22235655
[Au] Autor:Porowinska D; Czarnecka J; Komoszynski M
[Ad] Endereço:Zaklad Biochemii, Instytut Biologii Ogólnej i Molekularnej, Wydzial Biologii i Nauk o Ziemi, Uniwersytet Mikolaja Kopernika, Torun.
[Ti] Título:[The role of ectonucleotides metabolizing enzymes in purinergic signaling].
[Ti] Título:Rola enzymów metabolizujacych ektonukleotydy w sygnalizacji z udzialem puryn..
[So] Source:Postepy Biochem;57(3):294-303, 2011.
[Is] ISSN:0032-5422
[Cp] País de publicação:Poland
[La] Idioma:pol
[Ab] Resumo:Purinergic signaling plays an important role in the regulation of many physiological processes. The concentration of nucleotides in extracellular space is controlled by at least two families of nucleotidases: NPPases and NTPDases. These families are examples of convergent evolution of proteins. Above ezymes are not phylogenetically related, but they catalyze the same type of reaction. They hydrolyzed tri- and diphosphonucleosides to monophosphonucleosides and orthophosphate or pyrophosphate. This degradation terminates the nucleotide signaling process and also produces other signaling molecules like ADP, and with 5'-nucleotidase, adenosine. Most of known animal NPPases and NTPDases were found as membranous ectoenzymes or soluble proteins localized in tissue fluids. The aim of this work is to provide information about localization, structure, properties and function of NPPases and NTPDases in the regulation of extracellular concentration of nucleotides and purinergic signaling.
[Mh] Termos MeSH primário: 4-Nitrofenilfosfatase/química
4-Nitrofenilfosfatase/metabolismo
Nucleotídeos/metabolismo
Pirofosfatases/química
Pirofosfatases/metabolismo
Receptores Purinérgicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Comunicação Celular/fisiologia
Espaço Extracelular/metabolismo
Seres Humanos
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Nucleotides); 0 (Receptors, Purinergic); EC 3.1.3.41 (4-Nitrophenylphosphatase); EC 3.6.1.- (Pyrophosphatases)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:120112
[Lr] Data última revisão:
120112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120113
[St] Status:MEDLINE


  10 / 656 MEDLINE  
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[PMID]:21538547
[Au] Autor:Han GW; Ko J; Farr CL; Deller MC; Xu Q; Chiu HJ; Miller MD; Sefcikova J; Somarowthu S; Beuning PJ; Elsliger MA; Deacon AM; Godzik A; Lesley SA; Wilson IA; Ondrechen MJ
[Ad] Endereço:Joint Center for Structural Genomics, Scripps Research Institute, La Jolla, California 92037, USA.
[Ti] Título:Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity.
[So] Source:Proteins;79(7):2146-60, 2011 Jul.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The crystal structures of an unliganded and adenosine 5'-monophosphate (AMP) bound, metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis are reported at 2.4 and 1.94 Å, respectively. Functional characterization of this enzyme was guided by computational analysis and then confirmed by experiment. The structure consists of a polymerase and histidinol phosphatase (PHP, Pfam: PF02811) domain with a second domain (residues 105-178) inserted in the middle of the PHP sequence. The insert domain functions in binding AMP, but the precise function and substrate specificity of this domain are unknown. Initial bioinformatics analyses yielded multiple potential functional leads, with most of them suggesting DNA polymerase or DNA replication activity. Phylogenetic analysis indicated a potential DNA polymerase function that was somewhat supported by global structural comparisons identifying the closest structural match to the alpha subunit of DNA polymerase III. However, several other functional predictions, including phosphoesterase, could not be excluded. Theoretical microscopic anomalous titration curve shapes, a computational method for the prediction of active sites from protein 3D structures, identified potential reactive residues in YP_910028.1. Further analysis of the predicted active site and local comparison with its closest structure matches strongly suggested phosphoesterase activity, which was confirmed experimentally. Primer extension assays on both normal and mismatched DNA show neither extension nor degradation and provide evidence that YP_910028.1 has neither DNA polymerase activity nor DNA-proofreading activity. These results suggest that many of the sequence neighbors previously annotated as having DNA polymerase activity may actually be misannotated.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Bifidobacterium/enzimologia
Esterases/química
Esterases/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/química
4-Nitrofenilfosfatase/metabolismo
Difosfato de Adenosina/química
Difosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Sítios de Ligação
Domínio Catalítico
Simulação por Computador
Cristalografia
DNA Polimerase III/química
DNA Polimerase III/metabolismo
Histidinol-Fosfatase/química
Histidinol-Fosfatase/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Filogenia
Reprodutibilidade dos Testes
Relação Estrutura-Atividade
[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.
[Nm] Nome de substância:
0 (Bacterial Proteins); 61D2G4IYVH (Adenosine Diphosphate); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (DNA polymerase III, alpha subunit); EC 3.1.- (Esterases); EC 3.1.3.15 (Histidinol-Phosphatase); EC 3.1.3.41 (4-Nitrophenylphosphatase)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110504
[St] Status:MEDLINE
[do] DOI:10.1002/prot.23035



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