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[PMID]:28115347
[Au] Autor:Mishra NN; Tran TT; Seepersaud R; Garcia-de-la-Maria C; Faull K; Yoon A; Proctor R; Miro JM; Rybak MJ; Bayer AS; Arias CA; Sullam PM
[Ad] Endereço:LA Biomedical Research Institute, Torrance, California, USA.
[Ti] Título:Perturbations of Phosphatidate Cytidylyltransferase (CdsA) Mediate Daptomycin Resistance in Streptococcus mitis/oralis by a Novel Mechanism.
[So] Source:Antimicrob Agents Chemother;61(4), 2017 Apr.
[Is] ISSN:1098-6596
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is an important pathogen, causing life-threatening infections such as endocarditis and severe sepsis in immunocompromised patients. The ß-lactam antibiotics are the usual therapy of choice for this organism, but their effectiveness is threatened by the frequent emergence of resistance. The lipopeptide daptomycin (DAP) has been suggested for therapy against such resistant strains due to its bactericidal activity and demonstrated efficacy against other Gram-positive pathogens. Unlike other bacteria, however, has the unique ability to rapidly develop stable, high-level resistance to DAP upon exposure to the drug both and Using isogenic DAP-susceptible and DAP-resistant strain pairs, we describe a mechanism of resistance to both DAP and cationic antimicrobial peptides that involves loss-of-function mutations in (encoding a phosphatidate cytidylyltransferase). CdsA catalyzes the synthesis of cytidine diphosphate-diacylglycerol, an essential phospholipid intermediate for the production of membrane phosphatidylglycerol and cardiolipin. DAP-resistant strains demonstrated a total disappearance of phosphatidylglycerol, cardiolipin, and anionic phospholipid microdomains from membranes. In addition, these strains exhibited cross-resistance to cationic antimicrobial peptides from human neutrophils (i.e., hNP-1). Interestingly, CdsA-mediated changes in phospholipid metabolism were associated with DAP hyperaccumulation in a small subset of the bacterial population, without any binding by the remaining larger population. Our results indicate that CdsA is the major mediator of high-level DAP resistance in and suggest a novel mechanism of bacterial survival against attack by antimicrobial peptides of both innate and exogenous origins.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Daptomicina/farmacologia
Nucleotidiltransferases/metabolismo
Streptococcus oralis/efeitos dos fármacos
Streptococcus oralis/enzimologia
[Mh] Termos MeSH secundário: Cistina Difosfato/metabolismo
Farmacorresistência Bacteriana/genética
Bactérias Gram-Positivas/efeitos dos fármacos
Bactérias Gram-Positivas/enzimologia
Testes de Sensibilidade Microbiana
Neutrófilos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 63-38-7 (Cytidine Diphosphate); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.41 (phosphatidate cytidylyltransferase); NWQ5N31VKK (Daptomycin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170125
[St] Status:MEDLINE


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[PMID]:28103007
[Au] Autor:Ravichandran K; Minnihan EC; Lin Q; Yokoyama K; Taguchi AT; Shao J; Nocera DG; Stubbe J
[Ti] Título:Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.
[So] Source:Biochemistry;56(6):856-868, 2017 Feb 14.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Escherichia coli class Ia ribonucleotide reductase (RNR) is composed of two subunits that form an active α2ß2 complex. The nucleoside diphosphate substrates (NDP) are reduced in α2, 35 Å from the essential diferric-tyrosyl radical (Y ) cofactor in ß2. The Y -mediated oxidation of C in α2 occurs by a pathway (Y ⇆ [W ] ⇆ Y in ß2 to Y ⇆ Y ⇆ C in α2) across the α/ß interface. The absence of an α2ß2 structure precludes insight into the location of Y and Y at the subunit interface. The proximity in the primary sequence of the conserved E to Y in ß2 suggested its importance in catalysis and/or conformational gating. To study its function, pH-rate profiles of wild-type ß2/α2 and mutants in which 3,5-difluorotyrosine (F Y) replaces residue 356, 731, or both are reported in the presence of E or E X (X = A, D, or Q) mutants. With E , activity is maintained at the pH extremes, suggesting that protonated and deprotonated states of F Y and F Y are active and that radical transport (RT) can occur across the interface by proton-coupled electron transfer at low pH or electron transfer at high pH. With E X mutants, all RNRs were inactive, suggesting that E could be a proton acceptor during oxidation of the interface Ys. To determine if E plays a role in conformational gating, the strong oxidants, NO Y -ß2 and 2,3,5-F Y -ß2, were reacted with α2, CDP, and ATP in E and E X backgrounds and the reactions were monitored for pathway radicals by rapid freeze-quench electron paramagnetic resonance spectroscopy. Pathway radicals are generated only when E is present, supporting its essential role in gating the conformational change(s) that initiates RT and masking its role as a proton acceptor.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Radicais Livres/metabolismo
Ácido Glutâmico/química
Modelos Moleculares
Ribonucleotídeo Redutases/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Substituição de Aminoácidos
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Ligação Competitiva
Biocatálise
Cistina Difosfato/metabolismo
Espectroscopia de Ressonância de Spin Eletrônica
Transporte de Elétrons
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Concentração de Íons de Hidrogênio
Cinética
Mutagênese Sítio-Dirigida
Mutação
Oxirredução
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Ribonucleotídeo Redutases/química
Ribonucleotídeo Redutases/genética
Tirosina/análogos & derivados
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Escherichia coli Proteins); 0 (Free Radicals); 0 (Recombinant Proteins); 369-96-0 (3,5-difluorotyrosine); 3KX376GY7L (Glutamic Acid); 42HK56048U (Tyrosine); 63-38-7 (Cytidine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 1.17.4.- (NrdB protein, E coli); EC 1.17.4.- (Ribonucleotide Reductases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171118
[Lr] Data última revisão:
171118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01145


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[PMID]:27643605
[Au] Autor:McCluskey GD; Mohamady S; Taylor SD; Bearne SL
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, B3H 4R2, Canada.
[Ti] Título:Exploring the Potent Inhibition of CTP Synthase by Gemcitabine-5'-Triphosphate.
[So] Source:Chembiochem;17(23):2240-2249, 2016 Dec 02.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:CTP synthase (CTPS) catalyzes the conversion of UTP to CTP and is a target for the development of antiviral, anticancer, antiprotozoal, and immunosuppressive agents. Exposure of cell lines to the antineoplastic cytidine analogue gemcitabine causes depletion of intracellular CTP levels, but the direct inhibition of CTPS by its metabolite gemcitabine-5'-triphosphate (dF-dCTP) has not been demonstrated. We show that dF-dCTP is a potent competitive inhibitor of Escherichia coli CTPS with respect to UTP [K =(3.0±0.1) µm], and that its binding affinity exceeds that of CTP ≈75-fold. Site-directed mutagenesis studies indicated that Glu149 is an important binding determinant for both CTP and dF-dCTP. Comparison of the binding affinities of the 5'-triphosphates of 2'-fluoro-2'-deoxycytidine and 2'-fluoro-2'-deoxyarabinocytidine revealed that the 2'-F-arabino group contributes markedly to the strong binding of dF-dCTP. Geminal 2'-F substitution on UTP (dF-dUTP) did not result in an increase in binding affinity with CTPS. Remarkably, CTPS catalyzed the conversion of dF-dUTP into dF-dCTP, thus suggesting that dF-dCTP might be regenerated in vivo from its catabolite dF-dUTP.
[Mh] Termos MeSH primário: Carbono-Nitrogênio Ligases/antagonistas & inibidores
Citidina Trifosfato/análogos & derivados
Inibidores Enzimáticos/farmacologia
[Mh] Termos MeSH secundário: Carbono-Nitrogênio Ligases/metabolismo
Cistina Difosfato/análogos & derivados
Citidina Trifosfato/química
Citidina Trifosfato/farmacologia
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Escherichia coli/enzimologia
Estrutura Molecular
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (gemcitabine-5'-diphosphate); 0 (gemcitabine-5'-triphosphate); 63-38-7 (Cytidine Diphosphate); 65-47-4 (Cytidine Triphosphate); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.2 (CTP synthetase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160920
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600405


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[PMID]:26841430
[Au] Autor:Lito P; Solomon M; Li LS; Hansen R; Rosen N
[Ad] Endereço:Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY, USA. rosenn@mskcc.org litop@mskcc.org.
[Ti] Título:Allele-specific inhibitors inactivate mutant KRAS G12C by a trapping mechanism.
[So] Source:Science;351(6273):604-8, 2016 Feb 05.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is thought that KRAS oncoproteins are constitutively active because their guanosine triphosphatase (GTPase) activity is disabled. Consequently, drugs targeting the inactive or guanosine 5'-diphosphate-bound conformation are not expected to be effective. We describe a mechanism that enables such drugs to inhibit KRAS(G12C) signaling and cancer cell growth. Inhibition requires intact GTPase activity and occurs because drug-bound KRAS(G12C) is insusceptible to nucleotide exchange factors and thus trapped in its inactive state. Indeed, mutants completely lacking GTPase activity and those promoting exchange reduced the potency of the drug. Suppressing nucleotide exchange activity downstream of various tyrosine kinases enhanced KRAS(G12C) inhibition, whereas its potentiation had the opposite effect. These findings reveal that KRAS(G12C) undergoes nucleotide cycling in cancer cells and provide a basis for developing effective therapies to treat KRAS(G12C)-driven cancers.
[Mh] Termos MeSH primário: Adenocarcinoma/enzimologia
Antineoplásicos/farmacologia
Azetidinas/farmacologia
Inibidores Enzimáticos/farmacologia
Neoplasias Pulmonares/enzimologia
Piperazinas/farmacologia
Proteínas Proto-Oncogênicas p21(ras)/antagonistas & inibidores
Proteínas Proto-Oncogênicas p21(ras)/genética
[Mh] Termos MeSH secundário: Adenocarcinoma/tratamento farmacológico
Adenocarcinoma/genética
Alelos
Antineoplásicos/química
Antineoplásicos/uso terapêutico
Azetidinas/química
Azetidinas/uso terapêutico
Linhagem Celular Tumoral
Cisteína/genética
Cistina Difosfato/química
Inibidores Enzimáticos/química
Inibidores Enzimáticos/uso terapêutico
Glicina/genética
Guanosina Trifosfato/química
Células HEK293
Seres Humanos
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/genética
Terapia de Alvo Molecular
Mutação
Piperazinas/química
Piperazinas/uso terapêutico
Conformação Proteica/efeitos dos fármacos
Proteínas Proto-Oncogênicas p21(ras)/química
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 (ARS853); 0 (Antineoplastic Agents); 0 (Azetidines); 0 (Enzyme Inhibitors); 0 (KRAS protein, human); 0 (Piperazines); 63-38-7 (Cytidine Diphosphate); 86-01-1 (Guanosine Triphosphate); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras)); K848JZ4886 (Cysteine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160204
[St] Status:MEDLINE
[do] DOI:10.1126/science.aad6204


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[PMID]:26811286
[Au] Autor:Calzada E; Onguka O; Claypool SM
[Ad] Endereço:Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
[Ti] Título:Phosphatidylethanolamine Metabolism in Health and Disease.
[So] Source:Int Rev Cell Mol Biol;321:29-88, 2016.
[Is] ISSN:1937-6448
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Phosphatidylethanolamine (PE) is the second most abundant glycerophospholipid in eukaryotic cells. The existence of four only partially redundant biochemical pathways that produce PE, highlights the importance of this essential phospholipid. The CDP-ethanolamine and phosphatidylserine decarboxylase pathways occur in different subcellular compartments and are the main sources of PE in cells. Mammalian development fails upon ablation of either pathway. Once made, PE has diverse cellular functions that include serving as a precursor for phosphatidylcholine and a substrate for important posttranslational modifications, influencing membrane topology, and promoting cell and organelle membrane fusion, oxidative phosphorylation, mitochondrial biogenesis, and autophagy. The importance of PE metabolism in mammalian health has recently emerged following its association with Alzheimer's disease, Parkinson's disease, nonalcoholic liver disease, and the virulence of certain pathogenic organisms.
[Mh] Termos MeSH primário: Fosfatidiletanolaminas/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/metabolismo
Animais
Autofagia
Candida
Carboxiliases/metabolismo
Membrana Celular/metabolismo
Cistina Difosfato/análogos & derivados
Cistina Difosfato/metabolismo
Etanolaminas/metabolismo
Seres Humanos
Metabolismo dos Lipídeos
Metilação
Mitocôndrias/metabolismo
Hepatopatia Gordurosa não Alcoólica/metabolismo
Fosforilação Oxidativa
Doença de Parkinson/metabolismo
Fosfatidilcolinas/metabolismo
Fosfolipídeos/metabolismo
Príons/metabolismo
Processamento de Proteína Pós-Traducional
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Ethanolamines); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); 0 (Phospholipids); 0 (Prions); 3036-18-8 (CDP ethanolamine); 63-38-7 (Cytidine Diphosphate); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.65 (phosphatidylserine decarboxylase)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160127
[St] Status:MEDLINE


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[PMID]:25955207
[Au] Autor:Selathurai A; Kowalski GM; Burch ML; Sepulveda P; Risis S; Lee-Young RS; Lamon S; Meikle PJ; Genders AJ; McGee SL; Watt MJ; Russell AP; Frank M; Jackowski S; Febbraio MA; Bruce CR
[Ad] Endereço:Centre for Physical Activity and Nutrition (C-PAN) Research, School of Exercise and Nutrition Sciences, Deakin University, Burwood, 3125 VIC, Australia.
[Ti] Título:The CDP-Ethanolamine Pathway Regulates Skeletal Muscle Diacylglycerol Content and Mitochondrial Biogenesis without Altering Insulin Sensitivity.
[So] Source:Cell Metab;21(5):718-30, 2015 May 05.
[Is] ISSN:1932-7420
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulation of diacylglycerol (DG) in muscle is thought to cause insulin resistance. DG is a precursor for phospholipids, thus phospholipid synthesis could be involved in regulating muscle DG. Little is known about the interaction between phospholipid and DG in muscle; therefore, we examined whether disrupting muscle phospholipid synthesis, specifically phosphatidylethanolamine (PtdEtn), would influence muscle DG content and insulin sensitivity. Muscle PtdEtn synthesis was disrupted by deleting CTP:phosphoethanolamine cytidylyltransferase (ECT), the rate-limiting enzyme in the CDP-ethanolamine pathway, a major route for PtdEtn production. While PtdEtn was reduced in muscle-specific ECT knockout mice, intramyocellular and membrane-associated DG was markedly increased. Importantly, however, this was not associated with insulin resistance. Unexpectedly, mitochondrial biogenesis and muscle oxidative capacity were increased in muscle-specific ECT knockout mice and were accompanied by enhanced exercise performance. These findings highlight the importance of the CDP-ethanolamine pathway in regulating muscle DG content and challenge the DG-induced insulin resistance hypothesis.
[Mh] Termos MeSH primário: Cistina Difosfato/análogos & derivados
Diglicerídeos/metabolismo
Etanolaminas/metabolismo
Resistência à Insulina
Músculo Esquelético/metabolismo
Biogênese de Organelas
[Mh] Termos MeSH secundário: Animais
Cistina Difosfato/metabolismo
Glucose/metabolismo
Metabolismo dos Lipídeos
Camundongos
Camundongos Knockout
Obesidade/genética
Obesidade/metabolismo
RNA Nucleotidiltransferases/genética
RNA Nucleotidiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (1,2-diacylglycerol); 0 (Diglycerides); 0 (Ethanolamines); 3036-18-8 (CDP ethanolamine); 63-38-7 (Cytidine Diphosphate); EC 2.7.7.- (RNA Nucleotidyltransferases); EC 2.7.7.14 (Ethanolamine-phosphate cytidylyltransferase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150509
[Lr] Data última revisão:
150509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150509
[St] Status:MEDLINE


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[PMID]:25472423
[Au] Autor:Jorge CD; Borges N; Santos H
[Ad] Endereço:Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República-EAN, Apartado 127, Oeiras, 2780-157, Portugal.
[Ti] Título:A novel pathway for the synthesis of inositol phospholipids uses cytidine diphosphate (CDP)-inositol as donor of the polar head group.
[So] Source:Environ Microbiol;17(7):2492-504, 2015 Jul.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We describe a novel biosynthetic pathway for glycerophosphoinositides in Rhodothermus marinus in which inositol is activated by cytidine triphosphate (CTP); this is unlike all known pathways that involve activation of the lipid group instead. This work was motivated by the detection in the R. marinus genome of a gene with high similarity to CTP:L-myo-inositol-1-phosphate cytidylyltransferase, the enzyme that synthesizes cytidine diphosphate (CDP)-inositol, a metabolite only known in the synthesis of di-myo-inositol phosphate. However, this solute is absent in R. marinus. The fate of radiolabelled CDP-inositol was investigated in cell extracts to reveal that radioactive inositol was incorporated into the chloroform-soluble fraction. Mass spectrometry showed that the major lipid product has a molecular mass of 810 Da and contains inositol phosphate and alkyl chains attached to glycerol by ether bonds. The occurrence of ether-linked lipids is rare in bacteria and has not been described previously in R. marinus. The relevant synthase was identified by functional expression of the candidate gene in Escherichia coli. The enzyme catalyses the transfer of L-myo-inositol-1-phosphate from CDP-inositol to dialkylether glycerol yielding dialkylether glycerophosphoinositol. Database searching showed homologous proteins in two bacterial classes, Sphingobacteria and Alphaproteobacteria. This is the first report of the involvement of CDP-inositol in phospholipid synthesis.
[Mh] Termos MeSH primário: Cistina Difosfato/metabolismo
Citidina Trifosfato/metabolismo
Fosfatos de Inositol/metabolismo
Inositol/metabolismo
Fosfatidilinositóis/biossíntese
Rhodothermus/metabolismo
[Mh] Termos MeSH secundário: Vias Biossintéticas
Nucleotidiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Inositol Phosphates); 0 (Phosphatidylinositols); 15421-51-9 (inositol 1-phosphate); 16824-65-0 (glycerylphosphoinositol); 4L6452S749 (Inositol); 63-38-7 (Cytidine Diphosphate); 65-47-4 (Cytidine Triphosphate); EC 2.7.7.- (Nucleotidyltransferases)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150716
[Lr] Data última revisão:
150716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141205
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.12734


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[PMID]:25387590
[Au] Autor:Karadsheh NS; Simmonds HA
[Ad] Endereço:Department of Biochemistry and Physiology, Faculty of Medicine, The University of Jordan, Amman, Jordan. nsohk@ju.edu.jo, nsohk@yahoo.com.
[Ti] Título:Chronic hemolytic anemia and accumulation of pyrimidine nucleotide metabolites.
[So] Source:Int J Lab Hematol;37(4):e72-4, 2015 Aug.
[Is] ISSN:1751-553X
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Anemia Hemolítica Congênita/diagnóstico
Citidina Difosfato Colina/sangue
Cistina Difosfato/análogos & derivados
Etanolaminas/sangue
[Mh] Termos MeSH secundário: Adenosina Desaminase/sangue
Adenilato Quinase/sangue
Idoso
Anemia Hemolítica Congênita/sangue
Anemia Hemolítica Congênita/patologia
Doença Crônica
Cistina Difosfato/sangue
Feminino
Glucosefosfato Desidrogenase/sangue
Glutationa Peroxidase/sangue
Glutationa Redutase/sangue
Seres Humanos
[Pt] Tipo de publicação:CASE REPORTS; LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ethanolamines); 3036-18-8 (CDP ethanolamine); 536BQ2JVC7 (Cytidine Diphosphate Choline); 63-38-7 (Cytidine Diphosphate); EC 1.1.1.49 (Glucosephosphate Dehydrogenase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.8.1.7 (Glutathione Reductase); EC 2.7.4.3 (Adenylate Kinase); EC 3.5.4.4 (Adenosine Deaminase)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150716
[Lr] Data última revisão:
150716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141113
[St] Status:MEDLINE
[do] DOI:10.1111/ijlh.12310


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[PMID]:24942835
[Au] Autor:Nogly P; Gushchin I; Remeeva A; Esteves AM; Borges N; Ma P; Ishchenko A; Grudinin S; Round E; Moraes I; Borshchevskiy V; Santos H; Gordeliy V; Archer M
[Ad] Endereço:1] Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa (ITQB-UNL), Av. República, EAN, 2780-157 Oeiras, Portugal [2].
[Ti] Título:X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism.
[So] Source:Nat Commun;5:4169, 2014 Jun 19.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phospholipids have major roles in the structure and function of all cell membranes. Most integral membrane proteins from the large CDP-alcohol phosphatidyltransferase family are involved in phospholipid biosynthesis across the three domains of life. They share a conserved sequence pattern and catalyse the displacement of CMP from a CDP-alcohol by a second alcohol. Here we report the crystal structure of a bifunctional enzyme comprising a cytoplasmic nucleotidyltransferase domain (IPCT) fused with a membrane CDP-alcohol phosphotransferase domain (DIPPS) at 2.65 Å resolution. The bifunctional protein dimerizes through the DIPPS domains, each comprising six transmembrane α-helices. The active site cavity is hydrophilic and widely open to the cytoplasm with a magnesium ion surrounded by four highly conserved aspartate residues from helices TM2 and TM3. We show that magnesium is essential for the enzymatic activity and is involved in catalysis. Substrates docking is validated by mutagenesis studies, and a structure-based catalytic mechanism is proposed.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Archaeoglobus fulgidus/enzimologia
Membrana Celular/enzimologia
Cistina Difosfato/metabolismo
Fosfotransferases/química
Fosfotransferases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/genética
Archaeoglobus fulgidus/química
Archaeoglobus fulgidus/genética
Biocatálise
Domínio Catalítico
Membrana Celular/química
Membrana Celular/genética
Cristalografia por Raios X
Cistina Difosfato/química
Magnésio/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Fosfotransferases/genética
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 63-38-7 (Cytidine Diphosphate); EC 2.7.- (Phosphotransferases); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:140619
[Lr] Data última revisão:
140619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140620
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms5169


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[PMID]:24692494
[Au] Autor:Nilsen TW
[Ti] Título:3'-end labeling of RNA with [5'-32P]Cytidine 3',5'-bis(phosphate) and T4 RNA ligase 1.
[So] Source:Cold Spring Harb Protoc;2014(4):444-6, 2014 Apr 01.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This protocol is used to radiolabel the 3' ends of RNAs, either synthesized by in vitro transcription or purified from cells or tissues, by ligation of [5'-(32)P]cytidine 3',5'-bis(phosphate) (pCp). [5'-(32)P]pCp can be obtained commercially or prepared in the laboratory using polynucleotide kinase to phosphorylate cytidine-3'-monophosphate (Cp) with [γ-(32)P]ATP. "Homemade" [5'-(32)P]pCp is considerably cheaper and has a higher final concentration than that obtained from commercial sources. The labeling protocol uses T4 RNA ligase 1, which covalently joins [5'-(32)P]pCp to the free 3' hydroxyl of RNA. For best labeling, [5'-(32)P]pCp should be at least equimolar or higher to available 3'-hydroxyl ends. The reaction requires overnight incubation at low temperature. At the end of the procedure, the reaction is desalted by gel filtration to remove any unincorporated [5'-(32)P]pCp.
[Mh] Termos MeSH primário: Cistina Difosfato/metabolismo
Radioisótopos de Fósforo/metabolismo
RNA Ligase (ATP)/metabolismo
RNA/metabolismo
Coloração e Rotulagem/métodos
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Bacteriófago T4/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphorus Radioisotopes); 0 (Viral Proteins); 2922-94-3 (cytidine 3',5'-diphosphate); 63-38-7 (Cytidine Diphosphate); 63231-63-0 (RNA); EC 6.5.1.3 (RNA Ligase (ATP)); EC 6.5.1.3 (bacteriophage T4 RNA ligase 1)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:140402
[Lr] Data última revisão:
140402
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140403
[St] Status:MEDLINE



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