Base de dados : MEDLINE
Pesquisa : B03.300.390.825 [Categoria DeCS]
Referências encontradas : 69 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 7 ir para página                  

  1 / 69 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28857549
[Au] Autor:Mazzei L; Cianci M; Contaldo U; Musiani F; Ciurli S
[Ad] Endereço:Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna , Bologna, Italy.
[Ti] Título:Urease Inhibition in the Presence of N-(n-Butyl)thiophosphoric Triamide, a Suicide Substrate: Structure and Kinetics.
[So] Source:Biochemistry;56(40):5391-5404, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nickel-dependent enzyme urease is a virulence factor for a large number of pathogenic and antibiotic-resistant bacteria, as well as a negative factor for the efficiency of soil nitrogen fertilization for crop production. The use of urease inhibitors to offset these effects requires knowledge, at a molecular level, of their mode of action. The 1.28 Å resolution structure of the enzyme-inhibitor complex obtained upon incubation of Sporosarcina pasteurii urease with N-(n-butyl)thiophosphoric triamide (NBPT), a molecule largely utilized in agriculture, reveals the presence of the monoamidothiophosphoric acid (MATP) moiety, obtained upon enzymatic hydrolysis of the diamide derivative of NBPT (NBPD) to yield n-butyl amine. MATP is bound to the two Ni(II) ions in the active site of urease using a µ -bridging O atom and terminally bound O and NH groups, with the S atom of the thiophosphoric amide pointing away from the metal center. The mobile flap modulating the size of the active site cavity is found in the closed conformation. Docking calculations suggest that the interaction between urease in the open flap conformation and NBPD involves a role for the conserved αArg339 in capturing and orienting the inhibitor prior to flap closure. Calorimetric and spectrophotometric determinations of the kinetic parameters of this inhibition indicate the occurrence of a reversible slow inhibition mode of action, characterized, for both bacterial and plant ureases, by a very small value of the dissociation constant of the urease-MATP complex. No need to convert NBPT to its oxo derivative NBPTO, as previously proposed, is necessary for urease inhibition.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Compostos Organofosforados/metabolismo
Compostos Organofosforados/farmacologia
Urease/antagonistas & inibidores
Urease/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Hidrólise
Cinética
Simulação de Acoplamento Molecular
Sporosarcina/enzimologia
Ureia/metabolismo
Urease/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (N-(n-butyl) thiophosphoric triamide); 0 (Organophosphorus Compounds); 8W8T17847W (Urea); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00750


  2 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28384543
[Au] Autor:Ntatsopoulos V; Vassiliou S; Macegoniuk K; Berlicki L; Mucha A
[Ad] Endereço:Laboratory of Organic Chemistry, Department of Chemistry, University of Athens, Panepistimiopolis, Zografou, 15701 Athens, Greece.
[Ti] Título:Novel organophosphorus scaffolds of urease inhibitors obtained by substitution of Morita-Baylis-Hillman adducts with phosphorus nucleophiles.
[So] Source:Eur J Med Chem;133:107-120, 2017 Jun 16.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The reactivity of Morita-Baylis-Hillman allyl acetates was employed to introduce phosphorus-containing functionalities to the side chain of the cinnamic acid conjugated system by nucleophilic displacement. The proximity of two acidic groups, the carboxylate and phosphonate/phosphinate groups, was necessary to form interactions in the active site of urease by recently described inhibitor frameworks. Several organophosphorus scaffolds were obtained and screened for inhibition of the bacterial urease, an enzyme that is essential for survival of urinary and gastrointestinal tract pathogens. α-Substituted phosphonomethyl- and 2-phosphonoethyl-cinnamate appeared to be the most potent and were further optimized. As a result, one of the most potent organophosphorus inhibitors of urease, α-phosphonomethyl-p-methylcinnamic acid, was identified, with K = 0.6 µM for Sporosarcina pasteurii urease. High complementarity to the enzyme active site was achieved with this structure, as any further modifications significantly decreased its affinity. Finally, this work describes the challenges faced in developing ligands for urease.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Organofosfonatos/química
Organofosfonatos/farmacologia
Sporosarcina/enzimologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Acetatos/química
Acetatos/farmacologia
Compostos Alílicos/química
Compostos Alílicos/farmacologia
Domínio Catalítico/efeitos dos fármacos
Cinamatos/química
Cinamatos/farmacologia
Simulação de Acoplamento Molecular
Sporosarcina/efeitos dos fármacos
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Allyl Compounds); 0 (Cinnamates); 0 (Enzyme Inhibitors); 0 (Organophosphonates); E4U5E5990I (allyl acetate); EC 3.5.1.5 (Urease); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE


  3 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28141487
[Au] Autor:Sun Y; Zhao Q; Zhi D; Wang Z; Wang Y; Xie Q; Wu Z; Wang X; Li Y; Yu L; Yang H; Zhou J; Li H
[Ad] Endereço:1​Gansu Key Laboratory of Biomonitoring and Bioremediation for Environmental Pollution, Institute of Microbiology, School of Life Science, Lanzhou University, Tianshui Road No.222, Lanzhou 730000, PR China 2​Gansu Institute for Drug Control, Yinan Road No.7, Lanzhou 730070, PR China.
[Ti] Título:Sporosarcina terrae sp. nov., isolated from orchard soil.
[So] Source:Int J Syst Evol Microbiol;67(7):2104-2108, 2017 Jul.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A Gram-stain-positive, motile and rod-shaped bacterium, designated strain LZ2T, was isolated from a sample of orchard soil from Laizhou city, Shandong province, PR China. On the basis of 16S rRNA gene sequence analysis, strain LZ2T was closely related to members of the genus Sporosarcina, sharing highest levels of sequence similarity with Sporosarcina pasteurii NCIMB 8841T (98.8 %), Sporosarcina soli I80T (95.9 %). The value for the DNA-DNA relatedness between strain LZ2T and Sporosarcina pasteurii NCIMB 8841T was 39.8±1.7 %. Growth occurred at 10-44 °C (optimum, 30-35 °C), pH 5.0-11.0 (optimum pH 9.0-10.0); NaCl concentrations of up to 7.0 % (w/v) were tolerated. The dominant respiratory quinone was MK-7 and the G+C content was 39.2 mol%. The major fatty acids were anteiso-C15 : 0 and iso-C15 : 0. The major polar lipids of strain LZ2T were diphosphatidylglycerol, phosphatidylcholine, phosphatidylethanolamine, phosphatidylglycerol and an unidentified phospholipid. Based on phenotypic and chemotaxonomic characteristics, and phylogenetic data strain LZ2T represents a novel species of the genus Sporosarcina, for which the name Sporosarcina terrae sp. nov. (type strain LZ2T=KACC 18822T=MCCC 1K03174T) is proposed.
[Mh] Termos MeSH primário: Filogenia
Microbiologia do Solo
Sporosarcina/classificação
[Mh] Termos MeSH secundário: Agricultura
Técnicas de Tipagem Bacteriana
Composição de Bases
China
DNA Bacteriano/genética
DNA Ribossômico/genética
Ácidos Graxos/química
Hibridização de Ácido Nucleico
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Sporosarcina/genética
Sporosarcina/isolamento & purificação
Vitamina K 2/análogos & derivados
Vitamina K 2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (DNA, Ribosomal); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 8427BML8NY (vitamin MK 7)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001835


  4 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27997145
[Au] Autor:Kirkland CM; Zanetti S; Grunewald E; Walsh DO; Codd SL; Phillips AJ
[Ad] Endereço:Center for Biofilm Engineering, Montana State University , Bozeman, Montana 59717, United States.
[Ti] Título:Detecting Microbially Induced Calcite Precipitation in a Model Well-Bore Using Downhole Low-Field NMR.
[So] Source:Environ Sci Technol;51(3):1537-1543, 2017 Feb 07.
[Is] ISSN:1520-5851
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microbially induced calcite precipitation (MICP) has been widely researched recently due to its relevance for subsurface engineering applications including sealing leakage pathways and permeability modification. These applications of MICP are inherently difficult to monitor nondestructively in time and space. Nuclear magnetic resonance (NMR) can characterize the pore size distributions, porosity, and permeability of subsurface formations. This investigation used a low-field NMR well-logging probe to monitor MICP in a sand-filled bioreactor, measuring NMR signal amplitude and T relaxation over an 8 day experimental period. Following inoculation with the ureolytic bacteria, Sporosarcina pasteurii, and pulsed injections of urea and calcium substrate, the NMR measured water content in the reactor decreased to 76% of its initial value. T relaxation distributions bifurcated from a single mode centered about approximately 650 ms into a fast decaying population (T less than 10 ms) and a larger population with T greater than 1000 ms. The combination of changes in pore volume and surface minerology accounts for the changes in the T distributions. Destructive sampling confirmed final porosity was approximately 88% of the original value. These results indicate the low-field NMR well-logging probe is sensitive to the physical and chemical changes caused by MICP in a laboratory bioreactor.
[Mh] Termos MeSH primário: Carbonato de Cálcio/química
Sporosarcina/metabolismo
[Mh] Termos MeSH secundário: Imagem por Ressonância Magnética
Espectroscopia de Ressonância Magnética
Porosidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
H0G9379FGK (Calcium Carbonate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1021/acs.est.6b04833


  5 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27888701
[Au] Autor:Mazzei L; Cianci M; Musiani F; Lente G; Palombo M; Ciurli S
[Ad] Endereço:Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy.
[Ti] Título:Inactivation of urease by catechol: Kinetics and structure.
[So] Source:J Inorg Biochem;166:182-189, 2017 Jan.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 10 times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50Å resolution, reveals the structural details of the enzyme inhibition.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Canavalia/enzimologia
Catecóis
Modelos Moleculares
Proteínas de Plantas
Sporosarcina/enzimologia
Urease
[Mh] Termos MeSH secundário: Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/química
Catecóis/antagonistas & inibidores
Catecóis/química
Proteínas de Plantas/antagonistas & inibidores
Proteínas de Plantas/química
Urease/antagonistas & inibidores
Urease/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Catechols); 0 (Plant Proteins); EC 3.5.1.5 (Urease); LF3AJ089DQ (catechol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170904
[Lr] Data última revisão:
170904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161127
[St] Status:MEDLINE


  6 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27766852
[Au] Autor:Johnstone EV; Hofmann S; Cherkouk A; Schmidt M
[Ad] Endereço:Helmholtz-Zentrum Dresden - Rossendorf, Institute of Resource Ecology, Bautzner Landstrasse 400, 01328 Dresden, Germany.
[Ti] Título:Study of the Interaction of Eu with Microbiologically Induced Calcium Carbonate Precipitates using TRLFS.
[So] Source:Environ Sci Technol;50(22):12411-12420, 2016 Nov 15.
[Is] ISSN:1520-5851
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The microbial induced biomineralization of calcium carbonate using the ureolytic bacterium Sporosarcina pasteurii in the presence of trivalent europium, a substitute for trivalent actinides, was investigated by time-resolved laser-induced fluorescence spectroscopy (TRLFS) and a variety of physicochemical techniques. Results showed that the bacterial-driven hydrolysis of urea provides favorable conditions for CaCO precipitation and Eu uptake due to subsequent increases in NH and pH in the local environment. Precipitate morphologies were characteristic of biogenically formed CaCO and consistent with the respective mineral phase compositions. The formation of vaterite with some calcite was observed after 1 day, calcite with some vaterite after 1 week, and pure calcite after 2 weeks. The presence of organic material associated with the mineral was also identified and quantified. TRLFS was used to track the interaction and speciation of Eu as a molecular probe with the mineral as a function of time. Initially, Eu is incorporated into the vaterite phase, while during CaCO phase transformation Eu speciation changes resulting in several species incorporated in the calcite phase either substituting at the Ca site or in a previously unidentified, low-symmetry site. Comparison of the biogenic precipitates to an abiotic sample shows mineral origin can affect Eu speciation within the mineral.
[Mh] Termos MeSH primário: Carbonato de Cálcio/química
Sporosarcina
[Mh] Termos MeSH secundário: Európio/química
Lasers
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
444W947O8O (Europium); H0G9379FGK (Calcium Carbonate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


  7 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27739253
[Au] Autor:Brocca S; Ferrari C; Barbiroli A; Pesce A; Lotti M; Nardini M
[Ad] Endereço:Department of Biotechnology and Biosciences, University of Milano-Bicocca, Italy.
[Ti] Título:A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.
[So] Source:FEBS J;283(23):4310-4324, 2016 Dec.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Life in cold environments requires an overall increase in the flexibility of macromolecular and supramolecular structures to allow biological processes to take place at low temperature. Conformational flexibility supports high catalytic rates of enzymes in the cold but in several cases is also a cause of instability. The three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) reported in this paper highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. In its functional form SpAAP is a dimer, and an increase in flexibility is achieved through loosening of intersubunit hydrophobic interactions. The release of subunits from the quaternary structure is hindered by an 'arm exchange' mechanism, in which a tiny structural element at the N terminus of one subunit inserts into the other subunit. Mutants lacking the 'arm' are monomeric, inactive and highly prone to aggregation. Another feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. DATABASE: Structural data are available in the Protein Data Bank under the accession number 5L8S.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Proteínas de Bactérias/química
Temperatura Baixa
Peptídeo Hidrolases/química
Sporosarcina/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Cristalografia por Raios X
Bases de Dados de Proteínas
Estabilidade Enzimática
Interações Hidrofóbicas e Hidrofílicas
Modelos Moleculares
Mutação
Peptídeo Hidrolases/genética
Peptídeo Hidrolases/metabolismo
Multimerização Proteica
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Homologia de Sequência de Aminoácidos
Sporosarcina/genética
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.4.- (Peptide Hydrolases); EC 3.4.19.1 (acylaminoacyl-peptidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161015
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13925


  8 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27599735
[Au] Autor:Zander U; Cianci M; Foos N; Silva CS; Mazzei L; Zubieta C; de Maria A; Nanao MH
[Ad] Endereço:Structural Biology Group, European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38000 Grenoble, France.
[Ti] Título:Merging of synchrotron serial crystallographic data by a genetic algorithm.
[So] Source:Acta Crystallogr D Struct Biol;72(Pt 9):1026-35, 2016 09.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent advances in macromolecular crystallography have made it practical to rapidly collect hundreds of sub-data sets consisting of small oscillations of incomplete data. This approach, generally referred to as serial crystallography, has many uses, including an increased effective dose per data set, the collection of data from crystals without harvesting (in situ data collection) and studies of dynamic events such as catalytic reactions. However, selecting which data sets from this type of experiment should be merged can be challenging and new methods are required. Here, it is shown that a genetic algorithm can be used for this purpose, and five case studies are presented in which the merging statistics are significantly improved compared with conventional merging of all data.
[Mh] Termos MeSH primário: Algoritmos
Cristalografia por Raios X/métodos
Proteínas/química
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/química
Arabidopsis/química
Proteínas de Arabidopsis/química
Bacillus/química
Proteínas de Bactérias/química
Análise por Conglomerados
Insulina/química
Sporosarcina/química
Síncrotrons
Termolisina/química
Fatores de Transcrição/química
Urease/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Bacterial Proteins); 0 (Insulin); 0 (Lux Arrhythmo protein, Arabidopsis); 0 (Proteins); 0 (Transcription Factors); EC 3.4.24.27 (Thermolysin); EC 3.5.1.5 (Urease); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.5 (xylose isomerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160908
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798316012079


  9 / 69 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27563868
[Au] Autor:Varga M
[Ad] Endereço:Electronics Packaging Laboratory, Department of Electrical Engineering and Information Technology, Technische Universität Dresden, 01069 Dresden, Germany. varga@avt.et.tu-dresden.de.
[Ti] Título:Truncation Derivatives of the S-Layer Protein of Sporosarcina ureae ATCC 13881 (SslA): Towards Elucidation of the Protein Domain Responsible for Self-Assembly.
[So] Source:Molecules;21(9), 2016 Aug 24.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The cell surface of Sporosarcina ureae ATCC 13881 is covered by an S-layer (SslA) consisting of identical protein subunits that assemble into lattices exhibiting square symmetry. In this work the self-assembly properties of the recombinant SslA were characterised with an emphasis on the identification of protein regions responsible for self-assembly. To this end, recombinant mature SslA (aa 31-1097) and three SslA truncation derivatives (one N-terminal, one C-terminal and one CN-terminal) were produced in a heterologous expression system, isolated, purified and their properties analysed by in vitro recrystallisation experiments on a functionalised silicon wafer. As a result, recombinant mature SslA self-assembled into crystalline monolayers with lattices resembling the one of the wild-type SslA. The study identifies the central protein domain consisting of amino acids 341-925 self-sufficient for self-assembly. Neither the first 341 amino acids nor the last 172 amino acids of the protein sequence are required to self-assemble into lattices.
[Mh] Termos MeSH primário: Sequência de Aminoácidos
Glicoproteínas de Membrana/química
Deleção de Sequência
Sporosarcina/química
[Mh] Termos MeSH secundário: Glicoproteínas de Membrana/genética
Domínios Proteicos
Proteínas Recombinantes
Sporosarcina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Recombinant Proteins); 0 (S-layer proteins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160827
[St] Status:MEDLINE


  10 / 69 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27524377
[Au] Autor:Macegoniuk K; Grela E; Palus J; Rudzinska-Szostak E; Grabowiecka A; Biernat M; Berlicki L
[Ad] Endereço:Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology , Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
[Ti] Título:1,2-Benzisoselenazol-3(2H)-one Derivatives As a New Class of Bacterial Urease Inhibitors.
[So] Source:J Med Chem;59(17):8125-33, 2016 Sep 08.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Urease inhibitors are considered promising compounds for the treatment of ureolytic bacterial infections, particularly infections resulting from Helicobacter pylori in the gastric tract. Herein, we present the synthesis and the inhibitory activity of novel and highly effective organoselenium compounds as inhibitors of Sporosarcina pasteurii and Helicobacter pylori ureases. These studied compounds represent a class of competitive reversible urease inhibitors. The most active compound, 2-phenyl-1,2-benzisoselenazol-3(2H)-one (ebselen), displayed Ki values equal to 2.11 and 226 nM against S. pasteurii and H. pylori enzymes, respectively, indicating ebselen as one of the most potent low-molecular-weight inhibitors of bacterial ureases reported to date. Most of these molecules penetrated through the cell membrane of the Gram-negative bacteria Escherichia coli (pGEM::ureOP) in vitro. Furthermore, whole-cell studies on the H. pylori J99 reference strain confirmed the high efficiency of the examined organoselenium compounds as urease inhibitors against pathogenic bacteria.
[Mh] Termos MeSH primário: Azóis/química
Proteínas de Bactérias/antagonistas & inibidores
Compostos Organosselênicos/química
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Azóis/metabolismo
Azóis/farmacologia
Proteínas de Bactérias/química
Permeabilidade da Membrana Celular
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Helicobacter pylori/efeitos dos fármacos
Helicobacter pylori/enzimologia
Modelos Moleculares
Compostos Organosselênicos/metabolismo
Compostos Organosselênicos/farmacologia
Proteínas Recombinantes/metabolismo
Sporosarcina/enzimologia
Urease/química
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azoles); 0 (Bacterial Proteins); 0 (Organoselenium Compounds); 0 (Recombinant Proteins); 40X2P7DPGH (ebselen); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.6b00986



página 1 de 7 ir para página                  
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde