Base de dados : MEDLINE
Pesquisa : G02.111.672 [Categoria DeCS]
Referências encontradas : 637 [refinar]
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[PMID]:28455256
[Au] Autor:Kim JH; Cho CW; Kim HY; Kim KT; Choi GS; Kim HH; Cho IS; Kwon SJ; Choi SK; Yoon JY; Yang SY; Kang JS; Kim YH
[Ad] Endereço:College of Pharmacy, Chungnam National University, Daejeon 34134, Republic of Korea; Department of Horticultural and Crop Environment, National Institute of Horticultural and Herbal Science, RDA, Wanju, 55365, Republic of Korea; Advanced Radiation Technology Institute, Korea Atomic Energy Research I
[Ti] Título:α-Glucosidase inhibition by prenylated and lavandulyl compounds from Sophora flavescens roots and in silico analysis.
[So] Source:Int J Biol Macromol;102:960-969, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The enzyme α-glucosidase is a good drug target for the treatment of diabetes mellitus. Four minor flavonoids (1-4) from roots of Sophora flavescens showed the inhibitory activity, with IC values ranging from 11.0±0.3 to 50.6±1.3µM, toward α-glucosidase. An enzyme kinetics analysis of them revealed that the compounds 1 and 4 were non-competitive, and compounds 2 and 3 were un-competitive inhibitors. For molecular docking, 3-dimensional structure of α-glucosidase was built by homology modeling. As the result, four compounds 1-4 were confirmed to interact into common binding site of α-glucosidase. In addition, all of the four prenylated and lavandulyl compounds (1-4) were abundant in an ethyl acetate fraction separated from a methanol extract, and the potential inhibitor (3) was extracted best using tetrahydrofuran.
[Mh] Termos MeSH primário: Simulação por Computador
Extratos Vegetais/farmacologia
Raízes de Plantas/química
Prenilação
Sophora/química
Terpenos/química
alfa-Glucosidases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Inibidores de Glicosídeo Hidrolases/química
Inibidores de Glicosídeo Hidrolases/metabolismo
Inibidores de Glicosídeo Hidrolases/farmacologia
Simulação de Acoplamento Molecular
Extratos Vegetais/química
Extratos Vegetais/metabolismo
Conformação Proteica
alfa-Glucosidases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoside Hydrolase Inhibitors); 0 (Plant Extracts); 0 (Terpenes); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:29269486
[Au] Autor:Barghetti A; Sjögren L; Floris M; Paredes EB; Wenkel S; Brodersen P
[Ad] Endereço:Department of Biology, University of Copenhagen, DK-2200 Copenhagen N, Denmark.
[Ti] Título:Heat-shock protein 40 is the key farnesylation target in meristem size control, abscisic acid signaling, and drought resistance.
[So] Source:Genes Dev;31(22):2282-2295, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein farnesylation is central to molecular cell biology. In plants, protein farnesyl transferase mutants are pleiotropic and exhibit defective meristem organization, hypersensitivity to the hormone abscisic acid, and increased drought resistance. The precise functions of protein farnesylation in plants remain incompletely understood because few relevant farnesylated targets have been identified. Here, we show that defective farnesylation of a single factor-heat-shock protein 40 (HSP40), encoded by the and genes-is sufficient to confer ABA hypersensitivity, drought resistance, late flowering, and enlarged meristems, indicating that altered function of chaperone client proteins underlies most farnesyl transferase mutant phenotypes. We also show that expression of an abiotic stress-related microRNA (miRNA) regulon controlled by the transcription factor SPL7 requires HSP40 farnesylation. Expression of a truncated SPL7 form mimicking its activated proteolysis fragment of the membrane-bound SPL7 precursor partially restores accumulation of SPL7-dependent miRNAs in farnesyl transferase mutants. These results implicate the pathway directing SPL7 activation from its membrane-bound precursor as an important target of farnesylated HSP40, consistent with our demonstration that HSP40 farnesylation facilitates its membrane association. The results also suggest that altered gene regulation via select miRNAs contributes to abiotic stress-related phenotypes of farnesyl transferase mutants.
[Mh] Termos MeSH primário: Ácido Abscísico/fisiologia
Proteínas de Arabidopsis/metabolismo
Proteínas de Choque Térmico HSP40/metabolismo
Meristema/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/anatomia & histologia
Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Membrana Celular/metabolismo
Proteínas de Ligação a DNA/metabolismo
Secas
Farnesiltranstransferase/genética
Proteínas de Choque Térmico HSP90/genética
Meristema/anatomia & histologia
MicroRNAs/metabolismo
Mutação
Prenilação
Transdução de Sinais
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (DNA-Binding Proteins); 0 (ERA1 protein, Arabidopsis); 0 (HSP40 Heat-Shock Proteins); 0 (HSP90 Heat-Shock Proteins); 0 (MicroRNAs); 0 (SPL7 protein, Arabidopsis); 0 (Transcription Factors); 72S9A8J5GW (Abscisic Acid); EC 2.5.1.29 (Farnesyltranstransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1101/gad.301242.117


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[PMID]:29253870
[Au] Autor:Sasidhar MV; Chevooru SK; Eickelberg O; Hartung HP; Neuhaus O
[Ad] Endereço:Department of Neurology, Heinrich Heine University, Düsseldorf, Germany.
[Ti] Título:Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors.
[So] Source:PLoS One;12(12):e0189701, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD147 is an activation induced glycoprotein that promotes the secretion and activation of matrix metalloproteinases (MMPs) and is upregulated during the differentiation of macrophages. Interestingly, some of the molecular functions of CD147 rely on its glycosylation status: the highly glycosylated forms of CD147 induce MMPs whereas the lowly glycosylated forms inhibit MMP activation. Statins are hydroxy-methylglutaryl coenzyme A reductase inhibitors that block the synthesis of mevalonate, thereby inhibiting all mevalonate-dependent pathways, including isoprenylation, N-glycosylation and cholesterol synthesis. In this study, we investigated the role of statins in the inhibition of macrophage differentiation and the associated process of MMP secretion through modulation of CD147. We observed that differentiation of the human monocytic cell line THP-1 to a macrophage phenotype led to upregulation of CD147 and CD14 and that this effect was inhibited by statins. At the molecular level, statins altered CD147 expression, structure and function by inhibiting isoprenylation and N-glycosylation. In addition, statins induced a shift of CD147 from its highly glycosylated form to its lowly glycosylated form. This shift in N-glycosylation status was accompanied by a decrease in the production and functional activity of MMP-2 and MMP-9. In conclusion, these findings describe a novel molecular mechanism of immune regulation by statins, making them interesting candidates for autoimmune disease therapy.
[Mh] Termos MeSH primário: Basigina/metabolismo
Inibidores de Hidroximetilglutaril-CoA Redutases/química
Receptores de Lipopolissacarídeos/metabolismo
Monócitos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Doenças Autoimunes
Biotinilação
Diferenciação Celular
Membrana Celular/metabolismo
Glicosilação
Seres Humanos
Sistema Imunitário
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Monócitos/citologia
Permeabilidade
Fenótipo
Prenilação
Células THP-1
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BSG protein, human); 0 (Hydroxymethylglutaryl-CoA Reductase Inhibitors); 0 (Lipopolysaccharide Receptors); 136894-56-9 (Basigin); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189701


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[PMID]:28943437
[Au] Autor:Huang J; Yang X; Peng X; Huang W
[Ad] Endereço:Department of Integrative Medicine, The Second Clinical School, Yangtze University, Jingzhou, Hubei, China; Department of Integrative Medicine, Medical School of Yangtze University, Jingzhou, Hubei, China.
[Ti] Título:Inhibiting prenylation augments chemotherapy efficacy in renal cell carcinoma through dual inhibition on mitochondrial respiration and glycolysis.
[So] Source:Biochem Biophys Res Commun;493(2):921-927, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prenylation is a posttranslational lipid modification required for the proper functions of a number of proteins involved in cell regulation. Here, we show that prenylation inhibition is important for renal cell carcinoma (RCC) growth, survival and response to chemotherapy, and its underlying mechanism may be contributed to mitochondrial dysfunction. We first demonstrated that a HMG-CoA reductase inhibitor pitavastatin inhibited mevalonate pathway and thereby prenylation in RCC cells. In addition, pitavastatin is effective in inhibiting growth and inducing apoptosis in a panel of RCC cell lines. Combination of pitavastatin and paclitaxel is significantly more effective than pitavastatin or paclitaxel alone as shown by both in vitro cell culture system and in vivo RCC xenograft model. Importantly, pitavastatin treatment inhibits mitochondrial respiration via suppressing mitochondrial complex I and II enzyme activities. Interestingly, different from mitochondrial inhibitor phenformin that inhibits mitochondrial respiration but activates glycolytic rate in RCC cells, pitavastatin significantly decreases glycolytic rate. The dual inhibitory action of pitavastatin on mitochondrial respiration and glycolysis results in remarkable energy depletion and oxidative stress in RCC cells. In addition, inhibition of prenylation by depleting Isoprenylcysteine carboxylmethyltransferase (Icmt) also mimics the inhibitory effects of pitavastatin in RCC cells. Our work demonstrates the previously unappreciated association between prenylation inhibition and energy metabolism in RCC, which can be therapeutically exploited, likely in tumors that largely rely on energy metabolism.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Carcinoma de Células Renais/tratamento farmacológico
Inibidores de Hidroximetilglutaril-CoA Redutases/farmacologia
Neoplasias Renais/tratamento farmacológico
Mitocôndrias/efeitos dos fármacos
Prenilação/efeitos dos fármacos
Quinolinas/farmacologia
[Mh] Termos MeSH secundário: Carcinoma de Células Renais/metabolismo
Carcinoma de Células Renais/patologia
Linhagem Celular Tumoral
Respiração Celular/efeitos dos fármacos
Metabolismo Energético/efeitos dos fármacos
Glicólise/efeitos dos fármacos
Seres Humanos
Rim/efeitos dos fármacos
Rim/metabolismo
Rim/patologia
Neoplasias Renais/metabolismo
Neoplasias Renais/patologia
Mitocôndrias/metabolismo
Mitocôndrias/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Hydroxymethylglutaryl-CoA Reductase Inhibitors); 0 (Quinolines); M5681Q5F9P (pitavastatin)
[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:170926
[St] Status:MEDLINE


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[PMID]:28916258
[Au] Autor:Huang QH; Lei C; Wang PP; Li JY; Li J; Hou AJ
[Ad] Endereço:Department of Pharmacognosy, School of Pharmacy, Fudan University, Shanghai 201203, PR China.
[Ti] Título:Isoprenylated phenolic compounds with PTP1B inhibition from Morus alba.
[So] Source:Fitoterapia;122:138-143, 2017 Oct.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Two new Diels-Alder adducts, albasins A and B (1 and 2), one new isoprenylated 2-arylbenzofuran, albasin C (3), one new isoprenylated flavone, albasin D (4), together with sixteen known phenolic compounds, were isolated from the root bark of Morus alba. Their structures were elucidated by extensive spectroscopic analysis, including NMR, MS, and ECD data. All the new compounds and most of the known ones showed significant inhibitory effects on PTP1B in vitro with IC values ranging from 0.57 to 7.49µM.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Morus/química
Fenóis/química
Proteína Tirosina Fosfatase não Receptora Tipo 1/antagonistas & inibidores
[Mh] Termos MeSH secundário: Benzofuranos/química
Benzofuranos/isolamento & purificação
Inibidores Enzimáticos/isolamento & purificação
Flavonas/química
Flavonas/isolamento & purificação
Seres Humanos
Estrutura Molecular
Fenóis/isolamento & purificação
Casca de Planta/química
Raízes de Plantas/química
Prenilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzofurans); 0 (Enzyme Inhibitors); 0 (Flavones); 0 (Phenols); EC 3.1.3.48 (PTPN1 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1); S2V45N7G3B (flavone)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170917
[St] Status:MEDLINE


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[PMID]:28853883
[Au] Autor:Genovese S; Taddeo VA; Epifano F; Fiorito S; Bize C; Rives A; de Medina P
[Ad] Endereço:Department of Pharmacy, University "G. D'Annunzio" of Chieti-Pescara , Via dei Vestini 31, 66100 Chieti Scalo (CH), Italy.
[Ti] Título:Characterization of the Degradation Profile of Umbelliprenin, a Bioactive Prenylated Coumarin of a Ferulago Species.
[So] Source:J Nat Prod;80(9):2424-2431, 2017 Sep 22.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Umbelliprenin is a secondary plant metabolite that displays promising chemopreventive, anti-inflammatory, and antigenotoxic properties. It possesses potential for applications to human welfare notably to prevent the emergence of cancer. For this purpose, stability studies are needed to define proper storage conditions and adapted formulations for this drug candidate. The identification of degradative products is a major concern for the preclinical development of umbelliprenin, providing also interesting information related to potential original phytochemicals formed in plants exposed to stressors. The stability profile of umbelliprenin under various stress conditions including exposure to heat, light, oxidation, and hydrolytic medium was assessed via HPLC/UV data. The data support that umbelliprenin undergoes inter- and intramolecular [2+2] cycloaddition under light exposure, leading respectively to a cyclobutane-umbelliprenin dimer and a 16-membered macrocycle. Their structures were characterized via MS and NMR data. It was shown that UV-A filters prevent this process, whereas UV-B filters and antioxidants are not or weakly effective. The study provides useful information for the preclinical development of umbelliprenin as an original chemopreventive agent.
[Mh] Termos MeSH primário: Anti-Inflamatórios/química
Anti-Inflamatórios/farmacologia
Antioxidantes/química
Antioxidantes/farmacologia
Apiaceae/química
Cumarínicos/química
Cumarínicos/farmacologia
Umbeliferonas/química
[Mh] Termos MeSH secundário: Seres Humanos
Hidrólise
Estrutura Molecular
Oxirredução
Prenilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antioxidants); 0 (Coumarins); 0 (Umbelliferones); A4VZ22K1WT (coumarin); MSD8N8A1LQ (umbelliprenin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170831
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.7b00175


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[PMID]:28803474
[Au] Autor:Tanaka S; Shiomi S; Ishikawa H
[Ad] Endereço:Department of Chemistry, Graduate School of Science and Technology, Kumamoto University , 2-39-1, Kurokami, Chuo-ku, Kumamoto 860-8555, Japan.
[Ti] Título:Bioinspired Indole Prenylation Reactions in Water.
[So] Source:J Nat Prod;80(8):2371-2378, 2017 Aug 25.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Isoprene units derived from dimethylallyl diphosphate (DMAPP) are an important motif in many natural products including terpenoids, carotenoids, steroids, and natural rubber. Understanding the chemical characteristics of DMAPP is an important topic in natural products chemistry, organic chemistry, and biochemistry. We have developed a direct bioinspired indole prenylation reaction using DMAPP or its equivalents as the electrophile in homogeneous aqueous acidic media in the absence of enzyme to provide prenylated indole products. After establishing the bioinspired indole prenylation reaction, this was then used to achieve the synthesis of a series of natural products, namely, N-prenylcyclo-l-tryptophyl-l-proline, tryprostatins, rhinocladins, and terezine D.
[Mh] Termos MeSH primário: Butadienos/química
Dipeptídeos/química
Hemiterpenos/química
Indóis/química
Compostos Organofosforados/química
Pentanos/química
Prolina/análogos & derivados
Prolina/química
Terpenos/química
[Mh] Termos MeSH secundário: Produtos Biológicos
Indóis/síntese química
Estrutura Molecular
Prenilação
Terpenos/síntese química
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Products); 0 (Butadienes); 0 (Dipeptides); 0 (Hemiterpenes); 0 (Indoles); 0 (Organophosphorus Compounds); 0 (Pentanes); 0 (Terpenes); 0 (tryptophyl-proline); 059QF0KO0R (Water); 0A62964IBU (isoprene); 358-72-5 (3,3-dimethylallyl pyrophosphate); 9DLQ4CIU6V (Proline)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.7b00464


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[PMID]:28797051
[Au] Autor:Vochyánová Z; Pokorná M; Rotrekl D; Smékal V; Fictum P; Suchý P; Gajdziok J; Smejkal K; Hosek J
[Ad] Endereço:Department of Molecular Biology and Pharmaceutical Biotechnology, Faculty of Pharmacy, University of Veterinary and Pharmaceutical Sciences Brno, Brno, Czech Republic.
[Ti] Título:Prenylated flavonoid morusin protects against TNBS-induced colitis in rats.
[So] Source:PLoS One;12(8):e0182464, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Morusin is a prenylated flavonoid isolated from the root bark of Morus alba. Many studies have shown the ability of flavonoids to act as anti-inflammatory agents. The aim of this study was to evaluate the effect of morusin on experimentally colitis induced by 2,4,6-trinitrobenzensulfonic acid in Wistar rats and to compare it with sulfasalazine, a drug conventionally used in the treatment of inflammatory bowel disease. Morusin was administered by gavage at doses of 12.5, 25, or 50 mg/kg/day for five days. The colonic tissue was evaluated macroscopically, histologically, and by performing immunodetection and zymographic analysis to determine the levels of antioxidant enzymes [superoxide dismutase (SOD) and catalase (CAT)], interleukin (IL)-1ß, and transforming growth factor (TGF)-ß1 and the activities of matrix metalloproteinases (MMP) 2 and 9. The tissue damage scores were significantly reduced with increasing dose of morusin, however efficacy was not demonstrated at the highest dose. At the dose of 12.5 mg/kg, morusin exerted therapeutic effectivity similar to that of sulfasalazine (50 mg/kg). This was associated with significant reduction of TGF-ß1 levels and MMP2 and MMP9 activities, and slight reduction of IL-1ß. Our results suggest that morusin possesses therapeutic potential for the treatment of chronic inflammatory diseases.
[Mh] Termos MeSH primário: Colite/prevenção & controle
Flavonoides/farmacologia
[Mh] Termos MeSH secundário: Animais
Colite/induzido quimicamente
Colite/enzimologia
Colo/efeitos dos fármacos
Colo/enzimologia
Colo/patologia
Masculino
Metaloproteinase 2 da Matriz/metabolismo
Prenilação
Ratos Wistar
Ácido Trinitrobenzenossulfônico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Flavonoids); 62596-29-6 (morusin); 8T3HQG2ZC4 (Trinitrobenzenesulfonic Acid); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.24 (Mmp2 protein, rat)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182464


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[PMID]:28754323
[Au] Autor:Marshall SA; Payne KAP; Leys D
[Ad] Endereço:Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
[Ti] Título:The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN).
[So] Source:Arch Biochem Biophys;632:209-221, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.
[Mh] Termos MeSH primário: Carboxiliases
Dimetilaliltranstransferase
Proteínas de Escherichia coli
Escherichia coli
Flavinas
Flavoproteínas
Prenilação/fisiologia
[Mh] Termos MeSH secundário: Carboxiliases/química
Carboxiliases/genética
Carboxiliases/metabolismo
Dimetilaliltranstransferase/química
Dimetilaliltranstransferase/genética
Dimetilaliltranstransferase/metabolismo
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Flavinas/biossíntese
Flavinas/química
Flavinas/genética
Flavoproteínas/química
Flavoproteínas/genética
Flavoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Flavins); 0 (Flavoproteins); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 4.1.1.- (3-octaprenyl-4-hydroxybenzoate carboxy-lyase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.- (ubiX protein, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


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[PMID]:28627163
[Au] Autor:Mizoguchi T; Isaji M; Yamano N; Harada J; Fujii R; Tamiaki H
[Ad] Endereço:Graduate School of Life Sciences, Ritsumeikan University , Kusatsu, Shiga 525-8577, Japan.
[Ti] Título:Molecular Structures and Functions of Chlorophylls-a Esterified with Geranylgeranyl, Dihydrogeranylgeranyl, and Tetrahydrogeranylgeranyl Groups at the 17-Propionate Residue in a Diatom, Chaetoceros calcitrans.
[So] Source:Biochemistry;56(28):3682-3688, 2017 Jul 18.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The 17-propionate ester group of chlorophyll(Chl)-a in some oxygenic phototrophs was investigated using HPLC. Chls-a esterified with partially dehydrogenated forms of a phytyl group were found in fully grown cells of a diatom, Chaetoceros calcitrans: geranylgeranyl (GG), dihydrogeranylgeranyl (DHGG), and tetrahydrogeranylgeranyl (THGG). Chls-a bearing such esterifying groups were reported to be found only in greening processes of higher plants, and thus these Chls-a have been thought to be biosynthetic precursors for phytylated Chl-a. Their molecular structures were unambiguously determined using H and C NMR spectroscopy and mass spectrometry. In particular, the positions of C═C double bonds in DHGG were identified at C2═C3, C6═C7, and C14═C15, and those in THGG were determined to be at C2═C3 and C14═C15. Notably, the present DHGG was different from the previously determined DHGG of bacteriochlorophyll-a in purple bacteria (C2═C3, C10═C11, and C14═C15). Moreover, thylakoid membranes as well as fucoxanthin-chlorophyll-a/c proteins called FCPs were isolated from the diatom, and their Chl-a compositions were analyzed. Chls-a esterified with GG, DHGG, and THGG were detected by HPLC, indicating that such Chls-a were not merely biosynthetic precursors, but photosynthetically active pigments.
[Mh] Termos MeSH primário: Clorofila/química
Diatomáceas/química
Tilacoides/química
[Mh] Termos MeSH secundário: Esterificação
Hordeum/química
Prenilação
Propionatos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Propionates); 1406-65-1 (Chlorophyll); YF5Q9EJC8Y (chlorophyll a)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00381



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