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Pesquisa : B03.440.400.425.625.150 [Categoria DeCS]
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[PMID]:28875911
[Au] Autor:Sheu SY; Huang CW; Hsu MY; Sheu C; Chen WM
[Ad] Endereço:1​Department of Marine Biotechnology, National Kaohsiung Marine University, No. 142, Hai-Chuan Rd, Nan-Tzu, Kaohsiung City 811, Taiwan, ROC.
[Ti] Título:Cellvibrio zantedeschiae sp. nov., isolated from the roots of Zantedeschia aethiopica.
[So] Source:Int J Syst Evol Microbiol;67(9):3615-3621, 2017 Sep.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A bacterial strain, designated TPY-10T, was isolated from calla lily roots in Taiwan and characterized by using a polyphasic taxonomy approach. Cells of strain TPY-10T were Gram-stain-negative, strictly aerobic, motile and creamy white rods. Growth occurred at 15-35 °C (optimum, 25-30 °C), at pH 6-7 (optimum, pH 6) and with 0-1 % NaCl (optimum, 0 %). Phylogenetic analyses based on 16S rRNA gene sequences showed that strain TPY-10T belonged to the genus Cellvibrio and was most closely related to Cellvibriomixtus ACM 2601T with sequence similarity of 97.8 %. Strain TPY-10T contained C16 : 0, summed feature 3 (C16 : 1ω7c and/or C16 : 1ω6c) and C18 : 1ω7c as the predominant fatty acids. The only isoprenoid quinone was Q-9. The major polar lipids were phosphatidylethanolamine and phosphatidylglycerol. The DNA G+C content of the genomic DNA was 49.8 mol%. The DNA-DNA hybridization value for strain TPY-10T with Cellvibriomixtus ACM 2601T was less than 21 %. On the basis of the phylogenetic inference and phenotypic data, strain TPY-10T should be classified as a novel species, for which the name Cellvibrio zantedeschiae sp. nov. is proposed. The type strain is TPY-10T (=BCRC 80525T=LMG 27291T=KCTC 32239T).
[Mh] Termos MeSH primário: Cellvibrio/classificação
Filogenia
Raízes de Plantas/microbiologia
Zantedeschia/microbiologia
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
Cellvibrio/genética
Cellvibrio/isolamento & purificação
DNA Bacteriano/genética
Ácidos Graxos/química
Hibridização de Ácido Nucleico
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Taiwan
Vitamina K 2/análogos & derivados
Vitamina K 2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-39-7 (menaquinone 9)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002178


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[PMID]:28771122
[Au] Autor:Chen WM; Liu LP; Sheu SY
[Ad] Endereço:1​Laboratory of Microbiology, Department of Seafood Science, National Kaohsiung Marine University, No. 142, Hai-Chuan Rd. Nan-Tzu, Kaohsiung City 811, Taiwan, ROC.
[Ti] Título:Cellvibrio fontiphilus sp. nov., isolated from a spring.
[So] Source:Int J Syst Evol Microbiol;67(8):2532-2537, 2017 Aug.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A bacterial strain, designated MVW-40T, was isolated from Maolin Spring in Taiwan and characterized using a polyphasic taxonomy approach. Cells of strain MVW-40T were Gram-negative, strictly aerobic, motile by a single polar flagellum and bright yellow-pigmented rods with pointed ends. Growth occurred at 15-40 °C (optimum, 20-30 °C), at pH 6-9 (optimum, pH 6) and with 0-2 % NaCl (optimum, 0 %). Phylogenetic analyses based on 16S rRNA gene sequences showed that strain MVW-40T belonged to the genus Cellvibrio and showed the highest levels of sequence similarity with respect to Cellvibrio mixtussubsp. mixtus ACM 2601T (98.1 %) and Cellvibrio fibrivorans R-4079T (97.2 %). Strain MVW-40T contained summed feature 3 (C16 : 1ω7c and/or C16 : 1ω6c), C16 : 0 and C18 : 1ω7c as the predominant fatty acids. The polar lipid profile consisted of phosphatidylethanolamine, phosphatidylglycerol, two uncharacterized aminophospholipids, two uncharacterized phospholipids and an uncharacterized lipid. The DNA G+C content of the genomic DNA was 52.8 mol%. The DNA-DNA hybridization value for strain MVW-40T with C. mixtussubsp. mixtus ACM 2601T and C. fibrivorans R-4079T was less than 45 %. On the basis of the phylogenetic inference and phenotypic data, strain MVW-40T should be classified as a novel species, for which the name Cellvibrio fontiphilus sp. nov. is proposed. The type strain is MVW-40T (=BCRC 80977T=LMG 29557T=KCTC 52237T).
[Mh] Termos MeSH primário: Cellvibrio/classificação
Nascentes Naturais/microbiologia
Filogenia
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
Cellvibrio/genética
Cellvibrio/isolamento & purificação
DNA Bacteriano/genética
Ácidos Graxos/química
Hibridização de Ácido Nucleico
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Taiwan
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001952


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[PMID]:28118504
[Au] Autor:Nelson CE; Rogowski A; Morland C; Wilhide JA; Gilbert HJ; Gardner JG
[Ad] Endereço:Department of Biological Sciences, University of Maryland - Baltimore County, Baltimore, Maryland, USA.
[Ti] Título:Systems analysis in Cellvibrio japonicus resolves predicted redundancy of ß-glucosidases and determines essential physiological functions.
[So] Source:Mol Microbiol;104(2):294-305, 2017 Apr.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Degradation of polysaccharides forms an essential arc in the carbon cycle, provides a percentage of our daily caloric intake, and is a major driver in the renewable chemical industry. Microorganisms proficient at degrading insoluble polysaccharides possess large numbers of carbohydrate active enzymes (CAZymes), many of which have been categorized as functionally redundant. Here we present data that suggests that CAZymes that have overlapping enzymatic activities can have unique, non-overlapping biological functions in the cell. Our comprehensive study to understand cellodextrin utilization in the soil saprophyte Cellvibrio japonicus found that only one of four predicted ß-glucosidases is required in a physiological context. Gene deletion analysis indicated that only the cel3B gene product is essential for efficient cellodextrin utilization in C. japonicus and is constitutively expressed at high levels. Interestingly, expression of individual ß-glucosidases in Escherichia coli K-12 enabled this non-cellulolytic bacterium to be fully capable of using cellobiose as a sole carbon source. Furthermore, enzyme kinetic studies indicated that the Cel3A enzyme is significantly more active than the Cel3B enzyme on the oligosaccharides but not disaccharides. Our approach for parsing related CAZymes to determine actual physiological roles in the cell can be applied to other polysaccharide-degradation systems.
[Mh] Termos MeSH primário: Metabolismo dos Carboidratos/fisiologia
Celulases/fisiologia
Cellvibrio/fisiologia
[Mh] Termos MeSH secundário: Celulases/metabolismo
Celulose/análogos & derivados
Celulose/metabolismo
Dextrinas/metabolismo
Dissacarídeos/metabolismo
Enzimas
Escherichia coli/genética
Cinética
Polissacarídeos/metabolismo
Análise de Sistemas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dextrins); 0 (Disaccharides); 0 (Enzymes); 0 (Polysaccharides); 9004-34-6 (Cellulose); 9061-30-7 (cellodextrin); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170125
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13625


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[PMID]:27664455
[Au] Autor:Nelson CE; Beri NR; Gardner JG
[Ad] Endereço:Department of Biological Sciences, University of Maryland - Baltimore County, Baltimore, MD, USA.
[Ti] Título:Custom fabrication of biomass containment devices using 3-D printing enables bacterial growth analyses with complex insoluble substrates.
[So] Source:J Microbiol Methods;130:136-143, 2016 Nov.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Physiological studies of recalcitrant polysaccharide degradation are challenging for several reasons, one of which is the difficulty in obtaining a reproducibly accurate real-time measurement of bacterial growth using insoluble substrates. Current methods suffer from several problems including (i) high background noise due to the insoluble material interspersed with cells, (ii) high consumable and reagent cost and (iii) significant time delay between sampling and data acquisition. A customizable substrate and cell separation device would provide an option to study bacterial growth using optical density measurements. To test this hypothesis we used 3-D printing to create biomass containment devices that allow interaction between insoluble substrates and microbial cells but do not interfere with spectrophotometer measurements. Evaluation of materials available for 3-D printing indicated that UV-cured acrylic plastic was the best material, being superior to nylon or stainless steel when examined for heat tolerance, reactivity, and ability to be sterilized. Cost analysis of the 3-D printed devices indicated they are a competitive way to quantitate bacterial growth compared to viable cell counting or protein measurements, and experimental conditions were scalable over a 100-fold range. The presence of the devices did not alter growth phenotypes when using either soluble substrates or insoluble substrates. We applied biomass containment to characterize growth of Cellvibrio japonicus on authentic lignocellulose (non-pretreated corn stover), and found physiological evidence that xylan is a significant nutritional source despite an abundance of cellulose present.
[Mh] Termos MeSH primário: Bactérias/crescimento & desenvolvimento
Biomassa
Contaminação de Equipamentos
Impressão Tridimensional/instrumentação
Solubilidade
[Mh] Termos MeSH secundário: Bactérias/metabolismo
Metabolismo dos Carboidratos
Celulose/metabolismo
Cellvibrio/genética
Cellvibrio/crescimento & desenvolvimento
Cellvibrio/metabolismo
Desenho de Equipamento/economia
Desenho de Equipamento/instrumentação
Lignina/química
Viabilidade Microbiana
Mutação
Nylons/química
Espectrofotometria
Aço Inoxidável/química
Esterilização
Xilanos/metabolismo
Zea mays/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nylons); 0 (Xylans); 11132-73-3 (lignocellulose); 12597-68-1 (Stainless Steel); 9004-34-6 (Cellulose); 9005-53-2 (Lignin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


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[PMID]:27263016
[Au] Autor:Gardner JG
[Ad] Endereço:Department of Biological Sciences, University of Maryland - Baltimore County, Baltimore, MD, USA. jgardner@umbc.edu.
[Ti] Título:Polysaccharide degradation systems of the saprophytic bacterium Cellvibrio japonicus.
[So] Source:World J Microbiol Biotechnol;32(7):121, 2016 Jul.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Study of recalcitrant polysaccharide degradation by bacterial systems is critical for understanding biological processes such as global carbon cycling, nutritional contributions of the human gut microbiome, and the production of renewable fuels and chemicals. One bacterium that has a robust ability to degrade polysaccharides is the Gram-negative saprophyte Cellvibrio japonicus. A bacterium with a circuitous history, C. japonicus underwent several taxonomy changes from an initially described Pseudomonas sp. Most of the enzymes described in the pre-genomics era have also been renamed. This review aims to consolidate the biochemical, structural, and genetic data published on C. japonicus and its remarkable ability to degrade cellulose, xylan, and pectin substrates. Initially, C. japonicus carbohydrate-active enzymes were studied biochemically and structurally for their novel polysaccharide binding and degradation characteristics, while more recent systems biology approaches have begun to unravel the complex regulation required for lignocellulose degradation in an environmental context. Also included is a discussion for the future of C. japonicus as a model system, with emphasis on current areas unexplored in terms of polysaccharide degradation and emerging directions for C. japonicus in both environmental and biotechnological applications.
[Mh] Termos MeSH primário: Cellvibrio/metabolismo
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Metabolismo dos Carboidratos
Cellvibrio/enzimologia
Cellvibrio/genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Polysaccharides)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160606
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-016-2068-6


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[PMID]:27169553
[Au] Autor:Tuveng TR; Arntzen MØ; Bengtsson O; Gardner JG; Vaaje-Kolstad G; Eijsink VG
[Ad] Endereço:Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Aas, Norway.
[Ti] Título:Proteomic investigation of the secretome of Cellvibrio japonicus during growth on chitin.
[So] Source:Proteomics;16(13):1904-14, 2016 Jul.
[Is] ISSN:1615-9861
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Studies of the secretomes of microbes grown on insoluble substrates are important for the discovery of novel proteins involved in biomass conversion. However, data in literature and this study indicate that secretome samples tend to be contaminated with cytoplasmic proteins. We have examined the secretome of the Gram-negative soil bacterium Cellvibrio japonicus using a simple plate-based culturing technique that yields samples with high fractions (60-75%) of proteins that are predicted to be secreted. By combining this approach with label-free quantification using the MaxLFQ algorithm, we have mapped and quantified proteins secreted by C. japonicus during growth on α- and ß-chitin. Hierarchical clustering of the detected protein quantities revealed groups of up-regulated proteins that include all five putative C. japonicus chitinases as well as a chitin-specific lytic polysaccharide monooxygenase (CjLPMO10A). A small set of secreted proteins were co-regulated with known chitin-specific enzymes, including several with unknown catalytic functions. These proteins provide interesting targets for further studies aimed at unraveling the enzymatic machineries used by C. japonicus for recalcitrant polysaccharide degradation. Studies of chitin degradation indicated that C. japonicus indeed produces an efficient chitinolytic enzyme cocktail. All MS data have been deposited in the ProteomeXchange with the dataset identifier PXD002843 (http://proteomecentral.proteomexchange.org/dataset/PXD002843).
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Cellvibrio/enzimologia
Cellvibrio/crescimento & desenvolvimento
Quitina/metabolismo
Quitinases/metabolismo
[Mh] Termos MeSH secundário: Metabolismo dos Carboidratos
Cellvibrio/metabolismo
Proteômica/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 1398-61-4 (Chitin); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE
[do] DOI:10.1002/pmic.201500419


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[PMID]:27031293
[Au] Autor:Saburi W
[Ad] Endereço:a Research Faculty of Agriculture , Hokkaido University , Sapporo , Japan.
[Ti] Título:Functions, structures, and applications of cellobiose 2-epimerase and glycoside hydrolase family 130 mannoside phosphorylases.
[So] Source:Biosci Biotechnol Biochem;80(7):1294-305, 2016 Jul.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Carbohydrate isomerases/epimerases are essential in carbohydrate metabolism, and have great potential in industrial carbohydrate conversion. Cellobiose 2-epimerase (CE) reversibly epimerizes the reducing end d-glucose residue of ß-(1→4)-linked disaccharides to d-mannose residue. CE shares catalytic machinery with monosaccharide isomerases and epimerases having an (α/α)6-barrel catalytic domain. Two histidine residues act as general acid and base catalysts in the proton abstraction and addition mechanism. ß-Mannoside hydrolase and 4-O-ß-d-mannosyl-d-glucose phosphorylase (MGP) were found as neighboring genes of CE, meaning that CE is involved in ß-mannan metabolism, where it epimerizes ß-d-mannopyranosyl-(1→4)-d-mannose to ß-d-mannopyranosyl-(1→4)-d-glucose for further phosphorolysis. MGPs form glycoside hydrolase family 130 (GH130) together with other ß-mannoside phosphorylases and hydrolases. Structural analysis of GH130 enzymes revealed an unusual catalytic mechanism involving a proton relay and the molecular basis for substrate and reaction specificities. Epilactose, efficiently produced from lactose using CE, has superior physiological functions as a prebiotic oligosaccharide.
[Mh] Termos MeSH primário: Aldose-Cetose Isomerases/metabolismo
Bacteroides fragilis/enzimologia
Carboidratos Epimerases/metabolismo
Cellvibrio/enzimologia
Regulação Bacteriana da Expressão Gênica
Prótons
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/genética
Sequência de Aminoácidos
Bacteroides fragilis/genética
Carboidratos Epimerases/genética
Metabolismo dos Carboidratos
Domínio Catalítico
Celobiose/química
Celobiose/metabolismo
Cellvibrio/genética
Dissacarídeos/química
Dissacarídeos/metabolismo
Glucose/química
Glucose/metabolismo
Manose/química
Manose/metabolismo
Modelos Moleculares
Nucleotidiltransferases/genética
Nucleotidiltransferases/metabolismo
Especificidade por Substrato
beta-Manosidase/genética
beta-Manosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Disaccharides); 0 (Protons); 16462-44-5 (Cellobiose); 3515BNP809 (epilactose); EC 2.7.7.- (Nucleotidyltransferases); EC 3.2.1.25 (beta-Mannosidase); EC 5.1.3.- (Carbohydrate Epimerases); EC 5.3.1.- (Aldose-Ketose Isomerases); IY9XDZ35W2 (Glucose); PHA4727WTP (Mannose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2016.1166934


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[PMID]:26929175
[Au] Autor:Attia M; Stepper J; Davies GJ; Brumer H
[Ad] Endereço:Michael Smith Laboratories and Department of Chemistry, University of British Columbia, Vancouver, Canada.
[Ti] Título:Functional and structural characterization of a potent GH74 endo-xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation.
[So] Source:FEBS J;283(9):1701-19, 2016 05.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The heteropolysaccharide xyloglucan (XyG) comprises up to one-quarter of the total carbohydrate content of terrestrial plant cell walls and, as such, represents a significant reservoir in the global carbon cycle. The complex composition of XyG requires a consortium of backbone-cleaving endo-xyloglucanases and side-chain cleaving exo-glycosidases for complete saccharification. The biochemical basis for XyG utilization by the model Gram-negative soil saprophytic bacterium Cellvibrio japonicus is incompletely understood, despite the recent characterization of associated side-chain cleaving exo-glycosidases. We present a detailed functional and structural characterization of a multimodular enzyme encoded by gene locus CJA_2477. The CJA_2477 gene product comprises an N-terminal glycoside hydrolase family 74 (GH74) endo-xyloglucanase module in train with two carbohydrate-binding modules (CBMs) from families 10 and 2 (CBM10 and CBM2). The GH74 catalytic domain generates Glc4 -based xylogluco-oligosaccharide (XyGO) substrates for downstream enzymes through an endo-dissociative mode of action. X-ray crystallography of the GH74 module, alone and in complex with XyGO products spanning the entire active site, revealed a broad substrate-binding cleft specifically adapted to XyG recognition, which is composed of two seven-bladed propeller domains characteristic of the GH74 family. The appended CBM10 and CBM2 members notably did not bind XyG, nor other soluble polysaccharides, and instead were specific cellulose-binding modules. Taken together, these data shed light on the first step of xyloglucan utilization by C. japonicus and expand the repertoire of GHs and CBMs for selective biomass analysis and utilization. DATABASE: Structural data have been deposited in the RCSB protein database under the Protein Data Bank codes: 5FKR, 5FKS, 5FKT and 5FKQ.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cellvibrio/química
Glucanos/química
Glicosídeo Hidrolases/química
Prolina/química
Microbiologia do Solo
Xilanos/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Cellvibrio/enzimologia
Clonagem Molecular
Biologia Computacional
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Cadeia Alimentar
Expressão Gênica
Glucanos/metabolismo
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Cinética
Modelos Moleculares
Prolina/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Glucans); 0 (Recombinant Fusion Proteins); 0 (Xylans); 37294-28-3 (xyloglucan); 9DLQ4CIU6V (Proline); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (xyloglucan endo(1-4)-beta-D-glucanase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13696


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[PMID]:26920485
[Au] Autor:Syazni; Yanagisawa M; Kasuu M; Ariga O; Nakasaki K
[Ad] Endereço:Department of International Development Engineering, Graduate School of Engineering, Tokyo Institute of Technology, 2-12-1 I4-2 Ookayama, Meguro-ku, Tokyo 152-8550, Japan.
[Ti] Título:Direct production of ethanol from neoagarobiose using recombinant yeast that secretes α-neoagarooligosaccharide hydrolase.
[So] Source:Enzyme Microb Technol;85:82-9, 2016 Apr.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An α-neoagarooligosaccharide hydrolase, AgaNash, was purified from Cellvibrio sp. OA-2007, which utilizes agarose as a substrate. The agaNash gene, which encodes AgaNash, was obtained by comparing the N-terminal amino acid sequence of AgaNash with that deduced from the nucleotide sequence of the full-length OA-2007 genome. The agaNash gene combined with the Saccharomyces cerevisiae signal peptide α-mating factor was transformed into the YPH499 strain of S. cerevisiae to generate YPH499/pTEF-MF-agaNash, and the recombinant yeast was confirmed to produce AgaNash, though it was mainly retained within the recombinant cell. To enhance AgaNash secretion from the cell, the signal peptide was replaced with a combination of the signal peptide and a threonine- and serine-rich tract (T-S region) of the S. diastaticus STA1 gene. The new recombinant yeast, YPH499/pTEF-STA1SP-agaNash, was demonstrated to secrete AgaNash and hydrolyze neoagarobiose with an efficiency of as high as 84%, thereby producing galactose, which is a fermentable sugar for the yeast, and ethanol, at concentrations of up to 1.8 g/L, directly from neoagarobiose.
[Mh] Termos MeSH primário: Dissacarídeos/metabolismo
Etanol/metabolismo
Glicosídeo Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Biocombustíveis
Cellvibrio/enzimologia
Cellvibrio/genética
Clonagem Molecular
Fermentação
Galactose/metabolismo
Genes Bacterianos
Glicosídeo Hidrolases/genética
Fator de Acasalamento/genética
Sinais Direcionadores de Proteínas/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biofuels); 0 (Disaccharides); 0 (Protein Sorting Signals); 0 (Recombinant Proteins); 3K9958V90M (Ethanol); 484-58-2 (neoagarobiose); 61194-02-3 (Mating Factor); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (alpha-neoagarooligosaccharide hydrolase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160228
[St] Status:MEDLINE


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[PMID]:26858252
[Au] Autor:Forsberg Z; Nelson CE; Dalhus B; Mekasha S; Loose JS; Crouch LI; Røhr ÅK; Gardner JG; Eijsink VG; Vaaje-Kolstad G
[Ad] Endereço:From the Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, 1432 Ås, Norway.
[Ti] Título:Structural and Functional Analysis of a Lytic Polysaccharide Monooxygenase Important for Efficient Utilization of Chitin in Cellvibrio japonicus.
[So] Source:J Biol Chem;291(14):7300-12, 2016 Apr 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellvibrio japonicusis a Gram-negative soil bacterium that is primarily known for its ability to degrade plant cell wall polysaccharides through utilization of an extensive repertoire of carbohydrate-active enzymes. Several putative chitin-degrading enzymes are also found among these carbohydrate-active enzymes, such as chitinases, chitobiases, and lytic polysaccharide monooxygenases (LPMOs). In this study, we have characterized the chitin-active LPMO,CjLPMO10A, a tri-modular enzyme containing a catalytic family AA10 LPMO module, a family 5 chitin-binding module, and a C-terminal unclassified module of unknown function. Characterization of the latter module revealed tight and specific binding to chitin, thereby unraveling a new family of chitin-binding modules (classified as CBM73). X-ray crystallographic elucidation of theCjLPMO10A catalytic module revealed that the active site of the enzyme combines structural features previously only observed in either cellulose or chitin-active LPMO10s. Analysis of the copper-binding site by EPR showed a signal signature more similar to those observed for cellulose-cleaving LPMOs. The full-length LPMO shows no activity toward cellulose but is able to bind and cleave both α- and ß-chitin. Removal of the chitin-binding modules reduced LPMO activity toward α-chitin compared with the full-length enzyme. Interestingly, the full-length enzyme and the individual catalytic LPMO module boosted the activity of an endochitinase equally well, also yielding similar amounts of oxidized products. Finally, gene deletion studies show thatCjLPMO10A is needed byC. japonicusto obtain efficient growth on both purified chitin and crab shell particles.
[Mh] Termos MeSH primário: Cellvibrio/enzimologia
Quitina/química
Oxigenases de Função Mista/química
[Mh] Termos MeSH secundário: Quitina/metabolismo
Cristalografia por Raios X
Oxigenases de Função Mista/metabolismo
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
1398-61-4 (Chitin); EC 1.- (Mixed Function Oxygenases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.700161



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