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Pesquisa : B03.440.450.980 [Categoria DeCS]
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[PMID]:28506829
[Au] Autor:Gu DH; Park MY; Kim JS
[Ad] Endereço:Department of Chemistry, Chonnam National University, Gwangju 61186, South Korea.
[Ti] Título:An asymmetric dimeric structure of TrmJ tRNA methyltransferase from Zymomonas mobilis with a flexible C-terminal dimer.
[So] Source:Biochem Biophys Res Commun;488(2):407-412, 2017 Jun 24.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The tRNA methyltransferase J (TrmJ) and D (TrmD) catalyze the transferring reaction of a methyl group to the tRNA anticodon loop. They commonly have the N-terminal domain (NTD) and the C-terminal domain (CTD). Whereas two monomeric CTDs symmetrically interact with a dimeric NTD in TrmD, a CTD dimer has exhibited an asymmetric interaction with the NTD dimer in the presence of a product. The elucidated apo-structure of the full-length TrmJ from Zymomonas mobilis ZM4 shows a dimeric CTD that asymmetrically interacts with the NTD dimer, thereby distributing non-symmetrical potential charge on the both side of the protein surface. Comparison with the product-bound structures reveals a local re-orientation of the two arginine-containing loop at the active site, which interacts with the product. Further, the CTD dimers have diverse orientations compared to the NTD dimers, suggesting their flexibility. These data indicate that an asymmetric interaction between the NTD dimer and the CTD dimer is a common structural feature among TrmJ proteins, regardless of the presence of a substrate or a product.
[Mh] Termos MeSH primário: Zymomonas/enzimologia
tRNA Metiltransferases/química
[Mh] Termos MeSH secundário: Dimerização
Modelos Moleculares
tRNA Metiltransferases/genética
tRNA Metiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.1.1.- (tRNA Methyltransferases)
[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:170517
[St] Status:MEDLINE


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[PMID]:28419165
[Au] Autor:Ehrmann FR; Stojko J; Metz A; Debaene F; Barandun LJ; Heine A; Diederich F; Cianférani S; Reuter K; Klebe G
[Ad] Endereço:Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marburg, Germany.
[Ti] Título:Soaking suggests "alternative facts": Only co-crystallization discloses major ligand-induced interface rearrangements of a homodimeric tRNA-binding protein indicating a novel mode-of-inhibition.
[So] Source:PLoS One;12(4):e0175723, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For the efficient pathogenesis of Shigella, the causative agent of bacillary dysentery, full functionality of tRNA-guanine transglycosylase (TGT) is mandatory. TGT performs post-transcriptional modifications of tRNAs in the anticodon loop taking impact on virulence development. This suggests TGT as a putative target for selective anti-shigellosis drug therapy. Since bacterial TGT is only functional as homodimer, its activity can be inhibited either by blocking its active site or by preventing dimerization. Recently, we discovered that in some crystal structures obtained by soaking the full conformational adaptation most likely induced in solution upon ligand binding is not displayed. Thus, soaked structures may be misleading and suggest irrelevant binding modes. Accordingly, we re-investigated these complexes by co-crystallization. The obtained structures revealed large conformational rearrangements not visible in the soaked complexes. They result from spatial perturbations in the ribose-34/phosphate-35 recognition pocket and, consequently, an extended loop-helix motif required to prevent access of water molecules into the dimer interface loses its geometric integrity. Thermodynamic profiles of ligand binding in solution indicate favorable entropic contributions to complex formation when large conformational adaptations in the dimer interface are involved. Native MS titration experiments reveal the extent to which the homodimer is destabilized in the presence of each inhibitor. Unexpectedly, one ligand causes a complete rearrangement of subunit packing within the homodimer, never observed in any other TGT crystal structure before. Likely, this novel twisted dimer is catalytically inactive and, therefore, suggests that stabilizing this non-productive subunit arrangement may be used as a further strategy for TGT inhibition.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Modelos Moleculares
Multimerização Proteica
RNA de Transferência/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Cristalização
Cristalografia por Raios X
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Interações Hidrofóbicas e Hidrofílicas
Ligantes
Pentosiltransferases/antagonistas & inibidores
Pentosiltransferases/química
Pentosiltransferases/metabolismo
Ligação Proteica
Conformação Proteica
Domínios Proteicos
Estabilidade Proteica
Estrutura Secundária de Proteína
RNA de Transferência/genética
RNA de Transferência/metabolismo
Soluções
Termodinâmica
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzyme Inhibitors); 0 (Ligands); 0 (Solutions); 9014-25-9 (RNA, Transfer); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.29 (queuine tRNA-ribosyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175723


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[PMID]:28296385
[Au] Autor:Paulikat M; Wechsler C; Tittmann K; Mata RA
[Ad] Endereço:Institute of Physical Chemistry, University of Goettingen , Tammannstraße 6, D-37077 Göttingen, Germany.
[Ti] Título:Theoretical Studies of the Electronic Absorption Spectra of Thiamin Diphosphate in Pyruvate Decarboxylase.
[So] Source:Biochemistry;56(13):1854-1864, 2017 Apr 04.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Electronic absorption spectra are oftentimes used to identify reaction intermediates or substrates/products in enzymatic systems, as long as absorption bands can be unequivocally assigned to the species being studied. The latter task is far from trivial given the transient nature of some states and the complexity of the surrounding environment around the active site. To identify unique spectral fingerprints, controlled experiments with model compounds have been used in the past, but even these can sometimes be unreliable. Circular dichroism (CD) and ultraviolet-visible spectra have been tools of choice in the study of the rich chemistry of thiamin diphosphate-dependent enzymes. In this study, we focus on the Zymomonas mobilis pyruvate decarboxylase, and mutant analogues thereof, as a prototypical representative of the thiamin diphosphate (ThDP) enzyme superfamily. Through the use of electronic structure methods, we analyze the nature of electronic excitations in the cofactor. We find that all the determining CD bands around the 280-340 nm spectral range correspond to charge-transfer excitations between the pyrimidine and thiazolium rings of ThDP, which, most likely, is a general property of related ThDP-dependent enzymes. While we can confirm the assignments of previously proposed bands to chemical states, our calculations further suggest that a hitherto unassigned band of enzyme-bound ThDP reports on the ionization state of the canonical glutamate that is required for cofactor activation. This finding expands the spectroscopic "library" of chemical states of ThDP enzymes, permitting a simultaneous assignment of both the cofactor ThDP and the activating glutamate. We anticipate this finding to be helpful for mechanistic analyses of related ThDP enzymes.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Coenzimas/química
Ácido Glutâmico/química
Piruvato Descarboxilase/química
Tiamina Pirofosfato/química
Zymomonas/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Coenzimas/metabolismo
Transporte de Elétrons
Expressão Gênica
Ácido Glutâmico/metabolismo
Cinética
Simulação de Dinâmica Molecular
Mutação
Estrutura Secundária de Proteína
Pirimidinas/química
Piruvato Descarboxilase/genética
Piruvato Descarboxilase/metabolismo
Eletricidade Estática
Termodinâmica
Tiamina Pirofosfato/metabolismo
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Pyrimidines); 3KX376GY7L (Glutamic Acid); EC 4.1.1.1 (Pyruvate Decarboxylase); K8CXK5Q32L (pyrimidine); Q57971654Y (Thiamine Pyrophosphate)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00984


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[PMID]:28176464
[Au] Autor:Kress N; Rapp J; Hauer B
[Ad] Endereço:Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
[Ti] Título:Enantioselective Reduction of Citral Isomers in NCR Ene Reductase: Analysis of an Active-Site Mutant Library.
[So] Source:Chembiochem;18(8):717-720, 2017 Apr 18.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A deeper understanding of the >99 % S-selective reduction of both isomers of citral catalyzed by NCR ene reductase was achieved by active-site mutational studies and docking simulation. Though structurally similar, the E/Z isomers of citral showed a significantly varying selectivity response to introduced mutations. Although it was possible to invert (E)-citral reduction enantioselectivity to ee 46 % (R) by introducing mutation W66A, for (Z)-citral it remained ≥88 % (S) for all single-residue variants. Residue 66 seems to act as a lever for opposite binding modes. This was underlined by a W66A-based double-mutant library that enhanced the (E)-citral derived enantioselectivity to 63 % (R) and significantly lowered the S selectivity for (Z)-citral to 44 % (S). Formation of (R)-citronellal from an (E/Z)-citral mixture is a desire in industrial (-)-menthol synthesis. Our findings pave the way for a rational enzyme engineering solution.
[Mh] Termos MeSH primário: Proteínas Fúngicas/química
Monoterpenos/química
Oxirredutases/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Proteínas Fúngicas/genética
Simulação de Acoplamento Molecular
Mutagênese Sítio-Dirigida
Oxirredução
Oxirredutases/genética
Mutação Puntual
Engenharia de Proteínas
Saccharomyces/enzimologia
Estereoisomerismo
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Monoterpenes); EC 1.- (Oxidoreductases); T7EU0O9VPP (citral)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700011


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[PMID]:28103254
[Au] Autor:Mardo K; Visnapuu T; Vija H; Aasamets A; Viigand K; Alamäe T
[Ad] Endereço:Department of Genetics, Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
[Ti] Título:A Highly Active Endo-Levanase BT1760 of a Dominant Mammalian Gut Commensal Bacteroides thetaiotaomicron Cleaves Not Only Various Bacterial Levans, but Also Levan of Timothy Grass.
[So] Source:PLoS One;12(1):e0169989, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteroides thetaiotaomicron, an abundant commensal of the human gut, degrades numerous complex carbohydrates. Recently, it was reported to grow on a ß-2,6-linked polyfructan levan produced by Zymomonas mobilis degrading the polymer into fructooligosaccharides (FOS) with a cell surface bound endo-levanase BT1760. The FOS are consumed by B. thetaiotaomicron, but also by other gut bacteria, including health-promoting bifidobacteria and lactobacilli. Here we characterize biochemical properties of BT1760, including the activity of BT1760 on six bacterial levans synthesized by the levansucrase Lsc3 of Pseudomonas syringae pv. tomato, its mutant Asp300Asn, levansucrases of Zymomonas mobilis, Erwinia herbicola, Halomonas smyrnensis as well as on levan isolated from timothy grass. For the first time a plant levan is shown as a perfect substrate for an endo-fructanase of a human gut bacterium. BT1760 degraded levans to FOS with degree of polymerization from 2 to 13. At optimal reaction conditions up to 1 g of FOS were produced per 1 mg of BT1760 protein. Low molecular weight (<60 kDa) levans, including timothy grass levan and levan synthesized from sucrose by the Lsc3Asp300Asn, were degraded most rapidly whilst levan produced by Lsc3 from raffinose least rapidly. BT1760 catalyzed finely at human body temperature (37°C) and in moderately acidic environment (pH 5-6) that is typical for the gut lumen. According to differential scanning fluorimetry, the Tm of the endo-levanase was 51.5°C. All tested levans were sufficiently stable in acidic conditions (pH 2.0) simulating the gastric environment. Therefore, levans of both bacterial and plant origin may serve as a prebiotic fiber for B. thetaiotaomicron and contribute to short-chain fatty acids synthesis by gut microbiota. In the genome of Bacteroides xylanisolvens of human origin a putative levan degradation locus was disclosed.
[Mh] Termos MeSH primário: Bacteroides thetaiotaomicron/enzimologia
Frutanos/metabolismo
Glicosídeo Hidrolases/metabolismo
Phleum/metabolismo
[Mh] Termos MeSH secundário: Erwinia/enzimologia
Frutanos/genética
Frutanos/isolamento & purificação
Halomonas/enzimologia
Hexosiltransferases/metabolismo
Seres Humanos
Hidrólise
Intestinos/microbiologia
Peso Molecular
Oligossacarídeos/metabolismo
Pseudomonas syringae/enzimologia
Homologia de Sequência
Especificidade por Substrato
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fructans); 0 (Oligosaccharides); 0 (fructooligosaccharide); EC 2.4.1.- (Hexosyltransferases); EC 2.4.1.10 (levansucrase); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.65 (levanase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0169989


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[PMID]:28100303
[Au] Autor:Pade N; Mikkat S; Hagemann M
[Ad] Endereço:1​Department Plant Physiology, University of Rostock, Institute for Biological Science, Albert-Einstein-Str. 3, 18059 Rostock, Germany.
[Ti] Título:Ethanol, glycogen and glucosylglycerol represent competing carbon pools in ethanol-producing cells of Synechocystis sp. PCC 6803 under high-salt conditions.
[So] Source:Microbiology;163(3):300-307, 2017 Mar.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cyanobacteria are photoautotrophic micro-organisms, which are increasingly being used as microbial cell factories to produce, for example, ethanol directly from solar energy and CO2. Here, we analysed the effects of different salt concentrations on an ethanol-producing strain of Synechocystis sp. PCC 6803 that overexpresses the pyruvate decarboxylase (pdc) from Zymomonas mobilis and the native alcohol dehydrogenase (adhA). Moderate salinities of 2 % NaCl had no negative impact on ethanol production, whereas the addition of 4 % NaCl resulted in significantly decreased ethanol yields compared to low-salt conditions. Proteomic analysis identified a defined set of proteins with increased abundances in ethanol-producing cells. Among them, we found strong up-regulation of α-1,4 glucan phosphorylase (GlgP, Slr1367) in the producer strain, which consistently resulted in a massive depletion of glycogen pools in these cells regardless of the salinity. The salt-induced accumulation of the compatible solute glucosylglycerol was not affected by the ethanol production. Glycogen and probably compatible solutes could present competing pools with respect to organic carbon, explaining the decreased ethanol production at the highest salinity.
[Mh] Termos MeSH primário: Etanol/metabolismo
Glucosídeos/biossíntese
Glicogênio/biossíntese
Cloreto de Sódio/metabolismo
Synechocystis/metabolismo
[Mh] Termos MeSH secundário: Álcool Desidrogenase/metabolismo
Metabolismo Energético/genética
Metabolismo Energético/fisiologia
Fosforilases/biossíntese
Piruvato Descarboxilase/genética
Piruvato Descarboxilase/metabolismo
Synechocystis/genética
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucosides); 0 (glucosylglycerol); 3K9958V90M (Ethanol); 451W47IQ8X (Sodium Chloride); 9005-79-2 (Glycogen); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 2.4.1.- (Phosphorylases); EC 4.1.1.1 (Pyruvate Decarboxylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000433


  7 / 500 MEDLINE  
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[PMID]:27936490
[Au] Autor:Holinski A; Heyn K; Merkl R; Sterner R
[Ad] Endereço:Institute of Biophysics and Physical Biochemistry, University of Regensburg, Regensburg, D-93040, Germany.
[Ti] Título:Combining ancestral sequence reconstruction with protein design to identify an interface hotspot in a key metabolic enzyme complex.
[So] Source:Proteins;85(2):312-321, 2017 Feb.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is important to identify hotspot residues that determine protein-protein interactions in interfaces of macromolecular complexes. We have applied a combination of ancestral sequence reconstruction and protein design to identify hotspots within imidazole glycerol phosphate synthase (ImGPS). ImGPS is a key metabolic enzyme complex, which links histidine and de novo purine biosynthesis and consists of the cyclase subunit HisF and the glutaminase subunit HisH. Initial fluorescence titration experiments showed that HisH from Zymomonas mobilis (zmHisH) binds with high affinity to the reconstructed HisF from the last universal common ancestor (LUCA-HisF) but not to HisF from Pyrobaculum arsenaticum (paHisF), which differ by 103 residues. Subsequent titration experiments with a reconstructed evolutionary intermediate linking LUCA-HisF and paHisF and inspection of the subunit interface of a contemporary ImGPS allowed us to narrow down the differences crucial for zmHisH binding to nine amino acids of HisF. Homology modeling and in silico mutagenesis studies suggested that at most two of these nine HisF residues are crucial for zmHisH binding. These computational results were verified by experimental site-directed mutagenesis, which finally enabled us to pinpoint a single amino acid residue in HisF that is decisive for high-affinity binding of zmHisH. Our work shows that the identification of protein interface hotspots can be very efficient when reconstructed proteins with different binding properties are included in the analysis. Proteins 2017; 85:312-321. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Aminoidrolases/química
Subunidades Proteicas/química
Pyrobaculum/genética
Thermotoga maritima/genética
Zymomonas/genética
[Mh] Termos MeSH secundário: Aminoidrolases/genética
Aminoidrolases/metabolismo
Sítios de Ligação
Evolução Biológica
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Mutação
Filogenia
Ligação Proteica
Engenharia de Proteínas
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Pyrobaculum/classificação
Pyrobaculum/enzimologia
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Termodinâmica
Thermotoga maritima/classificação
Thermotoga maritima/enzimologia
Zymomonas/classificação
Zymomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Recombinant Proteins); EC 3.5.1.- (imidazole glycerol phosphate synthase); EC 3.5.4.- (Aminohydrolases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161210
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25225


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[PMID]:27900888
[Au] Autor:Cao QH; Shao HH; Qiu H; Li T; Zhang YZ; Tan XM
[Ad] Endereço:a Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, College of Life Sciences , Sichuan University , Chengdu , Sichuan , China.
[Ti] Título:Using the CRISPR/Cas9 system to eliminate native plasmids of Zymomonas mobilis ZM4.
[So] Source:Biosci Biotechnol Biochem;81(3):453-459, 2017 Mar.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The CRISPR/Cas system can be used to simply and efficiently edit the genomes of various species, including animals, plants, and microbes. Zymomonas mobilis ZM4 is a highly efficient, ethanol-producing bacterium that contains five native plasmids. Here, we constructed the pSUZM2a-Cas9 plasmid and a single-guide RNA expression plasmid. The pSUZM2a-Cas9 plasmid was used to express the Cas9 gene cloned from Streptococcus pyogenes CICC 10464. The single-guide RNA expression plasmid pUC-T7sgRNA, with a T7 promoter, can be used for the in vitro synthesis of single-guide RNAs. This system was successfully employed to knockout the upp gene of Escherichia coli and the replicase genes of native Z. mobilis plasmids. This is the first study to apply the CRISPR/Cas9 system of S. pyogenes to eliminate native plasmids in Z. mobilis. It provides a new method for plasmid curing and paves the way for the genomic engineering of Z. mobilis.
[Mh] Termos MeSH primário: Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Técnicas de Inativação de Genes/métodos
Plasmídeos/genética
Zymomonas/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Endonucleases/genética
Escherichia coli/genética
Dosagem de Genes
Zymomonas/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.1.- (Cas9 endonuclease Streptococcus pyogenes); EC 3.1.- (Endonucleases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170306
[Lr] Data última revisão:
170306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2016.1189312


  9 / 500 MEDLINE  
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[PMID]:27722827
[Au] Autor:Kumar C; Wagh J; Archana G; Naresh Kumar G
[Ad] Endereço:Molecular Microbial Biochemistry Laboratory, Department of Biochemistry, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara, Gujarat, 390 002, India.
[Ti] Título:Sucrose dependent mineral phosphate solubilization in Enterobacter asburiae PSI3 by heterologous overexpression of periplasmic invertases.
[So] Source:World J Microbiol Biotechnol;32(12):194, 2016 Dec.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Enterobacter asburiae PSI3 solubilizes mineral phosphates in the presence of glucose by the secretion of gluconic acid generated by the action of a periplasmic pyrroloquinoline quinone dependent glucose dehydrogenase. In order to achieve mineral phosphate solubilization phenotype in the presence of sucrose, plasmids pCNK4 and pCNK5 containing genes encoding the invertase enzyme of Zymomonas mobilis (invB) and of Saccharomyces cerevisiae (suc2) under constitutive promoters were constructed with malE signal sequence (in case of invB alone as the suc2 is secreted natively). When introduced into E. asburiae PSI3, E. a. (pCNK4) and E. a. (pCNK5) transformants secreted 21.65 ± 0.94 and 22 ± 1.3 mM gluconic acid, respectively, in the presence of 75 mM sucrose and they also solubilized 180 ± 4.3 and 438 ± 7.3 µM P from the rock phosphate. In the presence of a mixture of 50 mM sucrose and 25 mM glucose, E. a. (pCNK5) secreted 34 ± 2.3 mM gluconic acid and released 479 ± 8.1 µM P. Moreover, in the presence of a mixture of eight sugars (10 mM each) in the medium, E. a. (pCNK5) released 414 ± 5.3 µM P in the buffered medium. Thus, this study demonstrates incorporation of periplasmic invertase imparted P solubilization ability to E. asburiae PSI3 in the presence of sucrose and mixture of sugars.
[Mh] Termos MeSH primário: Enterobacter/genética
Fosfatos/química
Sacarose/metabolismo
beta-Frutofuranosidase/metabolismo
[Mh] Termos MeSH secundário: Enterobacter/metabolismo
Engenharia Genética
Gluconatos/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Zymomonas/enzimologia
Zymomonas/genética
beta-Frutofuranosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gluconates); 0 (Phosphates); 57-50-1 (Sucrose); EC 3.2.1.26 (beta-Fructofuranosidase); R4R8J0Q44B (gluconic acid)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161011
[St] Status:MEDLINE


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[PMID]:27629544
[Au] Autor:Yang S; Fei Q; Zhang Y; Contreras LM; Utturkar SM; Brown SD; Himmel ME; Zhang M
[Ad] Endereço:National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA. shhyoung@hotmail.com.
[Ti] Título:Zymomonas mobilis as a model system for production of biofuels and biochemicals.
[So] Source:Microb Biotechnol;9(6):699-717, 2016 Nov.
[Is] ISSN:1751-7915
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zymomonas mobilis is a natural ethanologen with many desirable industrial biocatalyst characteristics. In this review, we will discuss work to develop Z. mobilis as a model system for biofuel production from the perspectives of substrate utilization, development for industrial robustness, potential product spectrum, strain evaluation and fermentation strategies. This review also encompasses perspectives related to classical genetic tools and emerging technologies in this context.
[Mh] Termos MeSH primário: Biocombustíveis
Produtos Biológicos/metabolismo
Zymomonas/metabolismo
[Mh] Termos MeSH secundário: Biotecnologia/métodos
Fermentação
Engenharia Metabólica/métodos
Zymomonas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biofuels); 0 (Biological Products)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE
[do] DOI:10.1111/1751-7915.12408



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