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Pesquisa : B03.440.400.425.625.625.675 [Categoria DeCS]
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[PMID]:28923662
[Au] Autor:Kammoonah S; Prasad B; Balaraman P; Mundhada H; Schwaneberg U; Plettner E
[Ad] Endereço:Department of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada.
[Ti] Título:Selecting of a cytochrome P450 SeSaM library with 3-chloroindole and endosulfan - Identification of mutants that dehalogenate 3-chloroindole.
[So] Source:Biochim Biophys Acta;1866(1):68-79, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cytochrome P450 (a camphor hydroxylase) from the soil bacterium Pseudomonas putida shows potential importance in environmental applications such as the degradation of chlorinated organic pollutants. Seven P450 mutants generated from Sequence Saturation Mutagenesis (SeSaM) and isolated by selection on minimal media with either 3-chloroindole or the insecticide endosulfan were studied for their ability to oxidize of 3-chloroindole to isatin. The wild-type enzyme did not accept 3-chloroindole as a substrate. Mutant (E156G/V247F/V253G/F256S) had the highest maximal velocity in the conversion of 3-chloroindole to isatin, whereas mutants (T56A/N116H/D297N) and (G60S/Y75H) had highest k /K values. Six of the mutants had more than one mutation, and within this set, mutation of residues 297 and 179 was observed twice. Docking simulations were performed on models of the mutant enzymes; the wild-type did not accommodate 3-chloroindole in the active site, whereas all the mutants did. We propose two potential reaction pathways for dechlorination of 3-chloroindole. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cânfora 5-Mono-Oxigenase/química
Endossulfano/metabolismo
Biblioteca Gênica
Indóis/metabolismo
Pseudomonas putida/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Biodegradação Ambiental
Cânfora 5-Mono-Oxigenase/genética
Cânfora 5-Mono-Oxigenase/metabolismo
Clonagem Molecular
Endossulfano/química
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Halogenação
Indóis/química
Isatina/química
Isatina/metabolismo
Cinética
Simulação de Acoplamento Molecular
Mutação
Oxirredução
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Pseudomonas putida/química
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Indoles); 0 (Recombinant Proteins); 82X95S7M06 (Isatin); EC 1.14.15.1 (Camphor 5-Monooxygenase); OKA6A6ZD4K (Endosulfan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE


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[PMID]:27777366
[Au] Autor:Hernández-Arranz S; Sánchez-Hevia D; Rojo F; Moreno R
[Ad] Endereço:Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC, Cantoblanco, 28049 Madrid, Spain.
[Ti] Título:Effect of Crc and Hfq proteins on the transcription, processing, and stability of the Pseudomonas putida CrcZ sRNA.
[So] Source:RNA;22(12):1902-1917, 2016 12.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Pseudomonas putida, the Hfq and Crc proteins regulate the expression of many genes in response to nutritional and environmental cues, by binding to mRNAs that bear specific target motifs and inhibiting their translation. The effect of these two proteins is antagonized by the CrcZ and CrcY small RNAs (sRNAs), the levels of which vary greatly according to growth conditions. The crcZ and crcY genes are transcribed from promoters PcrcZ and PcrcY, respectively, a process that relies on the CbrB transcriptional activator and the RpoN σ factor. Here we show that crcZ can also be transcribed from the promoter of the immediate upstream gene, cbrB, a weak constitutive promoter. The cbrB-crcZ transcript was processed to render a sRNA very similar in size to the CrcZ produced from promoter PcrcZ The processed sRNA, termed CrcZ*, was able to antagonize Hfq/Crc because, when provided in trans, it relieved the deregulated Hfq/Crc-dependent hyperrepressing phenotype of a ΔcrcZΔcrcY strain. CrcZ* may help in attaining basal levels of CrcZ/CrcZ* that are sufficient to protect the cell from an excessive Hfq/Crc-dependent repression. Since a functional sRNA can be produced from PcrcZ, an inducible strong promoter, or by cleavage of the cbrB-crcZ mRNA, crcZ can be considered a 3'-untranslated region of the cbrB-crcZ mRNA. In the absence of Hfq, the processed form of CrcZ was not observed. In addition, we show that Crc and Hfq increase CrcZ stability, which supports the idea that these proteins can form a complex with CrcZ and protect it from degradation by RNases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Pseudomonas putida/genética
Processamento Pós-Transcricional do RNA
RNA Bacteriano/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Regiões Promotoras Genéticas
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (RNA, Bacterial); 0 (RNA, Messenger)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171223
[Lr] Data última revisão:
171223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  3 / 3857 MEDLINE  
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[PMID]:28741929
[Au] Autor:Liou SH; Myers WK; Oswald JD; Britt RD; Goodin DB
[Ad] Endereço:Department of Chemistry, University of California , Davis, California 95616, United States.
[Ti] Título:Putidaredoxin Binds to the Same Site on Cytochrome P450cam in the Open and Closed Conformation.
[So] Source:Biochemistry;56(33):4371-4378, 2017 08 22.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytochrome P450 CYP101A1 (P450cam) hydroxylates camphor by receiving two distinct electrons from its unique reductase, putidaredoxin (Pdx). Upon binding ferric P450cam, Pdx is now known to trigger a conformational change in the enzyme. This Pdx-induced conversion may provide the trigger to coordinate enzyme turnover and protect the enzyme from oxidative damage, so the interactions responsible for this conversion are of significant interest at present. This proposed role for Pdx requires that its interactions with P450cam be different for the open and closed conformations. In this study, we show that the binding thermodynamics of Pdx does indeed differ in the predicted way when the conformation of P450cam is held in different states. However, double electron-electron resonance measurements of intermolecular distances in the Pdx/P450cam complex show that the geometry of the complex is nearly identical for the open and closed states of P450cam. These studies show that Pdx appears to make a single distinct interaction with its binding site on the enzyme and triggers the conformational change through very subtle structural interactions.
[Mh] Termos MeSH primário: Cânfora 5-Mono-Oxigenase/química
Ferredoxinas/química
Complexos Multiproteicos/química
Pseudomonas putida/química
[Mh] Termos MeSH secundário: Cânfora 5-Mono-Oxigenase/genética
Ferredoxinas/genética
Complexos Multiproteicos/genética
Estrutura Quaternária de Proteína
Pseudomonas putida/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Ferredoxins); 0 (Multiprotein Complexes); 57087-75-9 (putidaredoxin); EC 1.14.15.1 (Camphor 5-Monooxygenase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171206
[Lr] Data última revisão:
171206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00564


  4 / 3857 MEDLINE  
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[PMID]:28945818
[Au] Autor:Ainelo H; Lahesaare A; Teppo A; Kivisaar M; Teras R
[Ad] Endereço:Chair of Genetics, Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
[Ti] Título:The promoter region of lapA and its transcriptional regulation by Fis in Pseudomonas putida.
[So] Source:PLoS One;12(9):e0185482, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:LapA is the biggest protein in Pseudomonas putida and a key factor for biofilm formation. Its importance and posttranslational regulation is rather thoroughly studied but less is known about the transcriptional regulation. Here we give evidence that transcription of lapA in LB-grown bacteria is initiated from six promoters, three of which display moderate RpoS-dependence. The global transcription regulator Fis binds to the lapA promoter area at six positions in vitro, and Fis activates the transcription of lapA while overexpressed in cells. Two of the six Fis binding sites, Fis-A7 and Fis-A5, are necessary for the positive effect of Fis on the transcription of lapA in vivo. Our results indicate that Fis binding to the Fis-A7 site increases the level of transcription from the most distal promoter of lapA, whereas Fis binding to the Fis-A5 site could be important for modifying the promoter area topology.
[Mh] Termos MeSH primário: Genes Bacterianos
Pseudomonas putida/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sequência de Bases
Sítios de Ligação/genética
Biofilmes/crescimento & desenvolvimento
Mapeamento Cromossômico
DNA Bacteriano/genética
Fator Proteico para Inversão de Estimulação/genética
Fator Proteico para Inversão de Estimulação/metabolismo
Regulação Bacteriana da Expressão Gênica
Regiões Promotoras Genéticas
Pseudomonas putida/fisiologia
Fator sigma/genética
Fator sigma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Factor For Inversion Stimulation Protein); 0 (Sigma Factor); 0 (sigma factor KatF protein, Bacteria)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185482


  5 / 3857 MEDLINE  
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[PMID]:28877269
[Au] Autor:Magill DJ; Krylov VN; Shaburova OV; McGrath JW; Allen CCR; Quinn JP; Kulakov LA
[Ad] Endereço:Queen's University Belfast, School of Biological Sciences, Medical Biology Centre, Belfast, Northern Ireland.
[Ti] Título:Pf16 and phiPMW: Expanding the realm of Pseudomonas putida bacteriophages.
[So] Source:PLoS One;12(9):e0184307, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We present the analysis of two novel Pseudomonas putida phages, pf16 and phiPMW. Pf16 represents a peripherally related T4-like phage, and is the first of its kind infecting a Pseudomonad, with evidence suggesting cyanophage origins. Extensive divergence has resulted in pf16 occupying a newly defined clade designated as the pf16-related phages, lying at the interface of the Schizo T-Evens and Exo T-Evens. Recombination with an ancestor of the P. putida phage AF is likely responsible for the tropism of this phage. phiPMW represents a completely novel Pseudomonas phage with a genome containing substantial genetic novelty through its many hypothetical proteins. Evidence suggests that this phage has been extensively shaped through gene transfer events and vertical evolution. Phylogenetics shows that this phage has an evolutionary history involving FelixO1-related viruses but is in itself highly distinct from this group.
[Mh] Termos MeSH primário: Filogenia
Fagos de Pseudomonas/genética
Pseudomonas putida/virologia
[Mh] Termos MeSH secundário: Biofilmes
Proteínas do Capsídeo/genética
Análise por Conglomerados
Biologia Computacional
Biblioteca Gênica
Técnicas de Transferência de Genes
Genoma Bacteriano
Genoma Viral
Mutação
Regiões Promotoras Genéticas
Recombinação Genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184307


  6 / 3857 MEDLINE  
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[PMID]:28873512
[Au] Autor:Dong TT; Gong JS; Gu BC; Zhang Q; Li H; Lu ZM; Lu ML; Shi JS; Xu ZH
[Ad] Endereço:School of Pharmaceutical Science, Jiangnan University, Wuxi 214122, PR China; National Engineering Laboratory for Cereal Fermentation Technology, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China.
[Ti] Título:Significantly enhanced substrate tolerance of Pseudomonas putida nitrilase via atmospheric and room temperature plasma and cell immobilization.
[So] Source:Bioresour Technol;244(Pt 1):1104-1110, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The objective of the study was to enhance the substrate tolerance of Pseudomonas putida nitrilase via atmospheric and room temperature plasma (ARTP) and cell immobilization. The mutant library was constructed by ARTP and rapidly screened by an OPA-TCA microscale reaction. A mutant strain of mut-D3 was obtained and its optimum substrate concentration was improved to 150mM from 100mM. It could accumulate 189g/L nicotinic acid (NA) from 3-cyanopyridine (3-CP), which was increased by 42% compared with that of wild type (WT). Additionally, composite immobilization of mut-D3 was performed and SA-PVA immobilized cells could catalyze 250mM 3-CP each batch with finally accumulating 346g/L NA, while free cells accumulated 175g/L NA. These results indicated that the free or immobilized catalysts of mut-D3 could serve as a good choice for NA production. This is the first report on mutation breeding of nitrilase-producing microorganisms by ARTP.
[Mh] Termos MeSH primário: Aminoidrolases
Pseudomonas putida
[Mh] Termos MeSH secundário: Piridinas
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyridines); EC 3.5.4.- (Aminohydrolases); EC 3.5.5.1 (nitrilase); X64V0K6260 (3-cyanopyridine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  7 / 3857 MEDLINE  
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[PMID]:28847921
[Au] Autor:Jiang T; Guo X; Yan J; Zhang Y; Wang Y; Zhang M; Sheng B; Ma C; Xu P; Gao C
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
[Ti] Título:A Bacterial Multidomain NAD-Independent d-Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d-Lactate Oxidization.
[So] Source:J Bacteriol;199(22), 2017 Nov 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial membrane-associated NAD-independent d-lactate dehydrogenase (Fe-S d-iLDH) oxidizes d-lactate into pyruvate. A sequence analysis of the enzyme reveals that it contains an Fe-S oxidoreductase domain in addition to a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain, which differs from other typical d-iLDHs. Fe-S d-iLDH from KT2440 was purified as a His-tagged protein and characterized in detail. This monomeric enzyme exhibited activities with l-lactate and several d-2-hydroxyacids. Quinone was shown to be the preferred electron acceptor of the enzyme. The two domains of the enzyme were then heterologously expressed and purified separately. The Fe-S cluster-binding motifs predicted by sequence alignment were preliminarily verified by site-directed mutagenesis of the Fe-S oxidoreductase domain. The FAD-containing dehydrogenase domain retained 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S d-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain showed increased catalytic efficiency with cytochrome as the electron acceptor, but it completely lost the ability to use coenzyme Q Additionally, the FAD-containing dehydrogenase domain was no longer associated with the cell membrane, and it could not support the utilization of d-lactate as a carbon source. Based on the results obtained, we conclude that the Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S d-iLDH, and it helps the enzyme associate with the cell membrane. These functions make the Fe-S oxidoreductase domain crucial for the d-lactate utilization function of Fe-S d-iLDH. Lactate metabolism plays versatile roles in most domains of life. Lactate utilization processes depend on certain enzymes to oxidize lactate to pyruvate. In recent years, novel bacterial lactate-oxidizing enzymes have been continually reported, including the unique NAD-independent d-lactate dehydrogenase that contains an Fe-S oxidoreductase domain besides the typical flavin-containing domain (Fe-S d-iLDH). Although Fe-S d-iLDH is widely distributed among bacterial species, the investigation of it is insufficient. Fe-S d-iLDH from KT2440, which is the major d-lactate-oxidizing enzyme for the strain, might be a representative of this type of enzyme. A study of it will be helpful in understanding the detailed mechanisms underlying the lactate utilization processes.
[Mh] Termos MeSH primário: Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Lactato Desidrogenases/genética
Lactato Desidrogenases/metabolismo
Ácido Láctico/metabolismo
Quinonas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Coenzimas
Citocromos c/metabolismo
Elétrons
Lactato Desidrogenases/isolamento & purificação
Mutagênese Sítio-Dirigida
NAD/metabolismo
Oxirredução
Pseudomonas putida/enzimologia
Ubiquinona/análogos & derivados
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Iron-Sulfur Proteins); 0 (Quinones); 0U46U6E8UK (NAD); 1339-63-5 (Ubiquinone); 146-14-5 (Flavin-Adenine Dinucleotide); 33X04XA5AT (Lactic Acid); 9007-43-6 (Cytochromes c); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.1.28 (D-lactate dehydrogenase); EJ27X76M46 (coenzyme Q10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE


  8 / 3857 MEDLINE  
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[PMID]:28820109
[Au] Autor:Frasson D; Opoku M; Picozzi T; Torossi T; Balada S; Smits THM; Hilber U
[Ad] Endereço:1​Department of Life Sciences and Facility Management, Zürich University of Applied Sciences ZHAW, Wädenswil, Switzerland 2​Microbiology and Molecular Biology, Institute for Chemistry and Biotechnology (ICBT), Zürich University of Applied Sciences ZHAW, Wädenswil, Switzerland.
[Ti] Título:Pseudomonas wadenswilerensis sp. nov. and Pseudomonas reidholzensis sp. nov., two novel species within the Pseudomonas putida group isolated from forest soil.
[So] Source:Int J Syst Evol Microbiol;67(8):2853-2861, 2017 Aug.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Within the frame of a biotechnological screening, we isolated two Pseudomonas strains from forest soil. 16S rRNA gene sequence analysis indicated that strain CCOS 864T shared 99.8 % similarity with Pseudomonas donghuensis HYST, while strain CCOS 865T shared 99.0 % similarity with Pseudomonas putida DSM 291T and lower similarity with other P. putida group type strains. Based on multilocus sequence analysis, the two strains were genotypically distinct from each other, each forming a separate clade. Strains CCOS 864T and CCOS 865T were Gram-stain-negative, motile and rod-shaped, growing at a temperature range of 4-37 °C. Strain CCOS 864T could be phenotypically distinguished from P. putida group species by the combination of gelatinase-positive reaction and positive growth on N-acetyl-d-glucosamine, p-hydroxyphenylacetic acid and inosine but lack of fluorescein production on King's B medium, while strain CCOS 865T could be distinguished from P. putida group species by the combination of positive growth with saccharic acid and negative growth with p-hydroxyphenylacetic acid and l-pyroglutamic acid. The major polar lipid for both strains was phosphatidylethanolamine; the major quinone was ubiquinone Q-9. DNA-DNA hybridization and average nucleotide identities confirmed the novel species status for the two strains. The DNA G+C contents of CCOS 864T and CCOS 865T were 62.1 and 63.8 mol%, respectively. The phenotypic, phylogenetic and DNA-DNA relatedness data support the suggestion that CCOS 864T and CCOS 865T represent two novel Pseudomonas species. The names Pseudomonas wadenswilerensis sp. nov. (type strain CCOS 864T=LMG 29327T) and Pseudomonas reidholzensis sp. nov. (type strain CCOS 865T=LMG 29328T) are proposed.
[Mh] Termos MeSH primário: Florestas
Filogenia
Pseudomonas/classificação
Microbiologia do Solo
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
DNA Bacteriano/genética
Ácidos Graxos/química
Tipagem de Sequências Multilocus
Hibridização de Ácido Nucleico
Fosfatidiletanolaminas/química
Pseudomonas/genética
Pseudomonas/isolamento & purificação
Pseudomonas putida
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Suíça
Ubiquinona/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phosphatidylethanolamines); 0 (RNA, Ribosomal, 16S); 1339-63-5 (Ubiquinone); 39382-08-6 (phosphatidylethanolamine); MGW7TYF2DQ (ubiquinone 9)
[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:170819
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002035


  9 / 3857 MEDLINE  
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[PMID]:28772002
[Au] Autor:Roth S; Funk I; Hofer M; Sieber V
[Ad] Endereço:Technical University of Munich, Chair of Chemistry of Biogenic Resources, Schulgasse 16, 94315, Straubing, Germany.
[Ti] Título:Chemoenzymatic Synthesis of a Novel Borneol-Based Polyester.
[So] Source:ChemSusChem;10(18):3574-3580, 2017 Sep 22.
[Is] ISSN:1864-564X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Terpenes are a class of natural compounds that have recently moved into the focus as a bio-based resource for chemical production, owing to their abundance, their mostly cyclic structures, and the presence of olefin or single hydroxy groups. To apply this raw material in new industrial fields, a second hydroxy group is inserted into borneol by cytochrome P450cam (CYP101) enzymes in a whole-cell catalytic biotransformation with Pseudomonas putida KT2440. Next, a semi-continuous batch system was developed to produce 5-exo-hydroxyborneol with a final concentration of 0.54 g L . The bifunctional terpene was then used for the synthesis of a bio-based polyester by a solvent-free polycondensation reaction. The resulting polymer showed a glass transition temperature of around 70 °C and a molecular weight in the range of 2000-4000 g mol (M ). These results show that whole-cell catalytic biotransformation of terpenes could lead to bio-based, higher-functionalized monomers, which might be basic raw materials for different fields of application, such as biopolymers.
[Mh] Termos MeSH primário: Bornanos/química
Cânfora 5-Mono-Oxigenase/metabolismo
Poliésteres/química
Poliésteres/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Biotransformação
Engenharia Genética
Polimerização
Pseudomonas putida/citologia
Pseudomonas putida/enzimologia
Pseudomonas putida/genética
Pseudomonas putida/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bornanes); 0 (Polyesters); EC 1.14.15.1 (Camphor 5-Monooxygenase); L88RA8N5EG (isoborneol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1002/cssc.201701146


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[PMID]:28683916
[Au] Autor:Bearne SL; St Maurice M
[Ad] Endereço:Dalhousie University, Halifax, NS, Canada. Electronic address: sbearne@dal.ca.
[Ti] Título:A Paradigm for CH Bond Cleavage: Structural and Functional Aspects of Transition State Stabilization by Mandelate Racemase.
[So] Source:Adv Protein Chem Struct Biol;109:113-160, 2017.
[Is] ISSN:1876-1623
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mandelate racemase (MR) from Pseudomonas putida catalyzes the Mg -dependent, 1,1-proton transfer reaction that racemizes (R)- and (S)-mandelate. MR shares a partial reaction (i.e., the metal ion-assisted, Brønsted base-catalyzed proton abstraction of the α-proton of carboxylic acid substrates) and structural features ((ß/α) ß-barrel and N-terminal α + ß capping domains) with a vast group of homologous, yet functionally diverse, enzymes in the enolase superfamily. Mechanistic and structural studies have developed this enzyme into a paradigm for understanding how enzymes such as those of the enolase superfamily overcome kinetic and thermodynamic barriers to catalyze the abstraction of an α-proton from a carbon acid substrate with a relatively high pK value. Structural studies on MR bound to intermediate/transition state analogues have delineated those structural features that MR uses to stabilize transition states and enhance reaction rates of proton abstraction. Kinetic, site-directed mutagenesis, and structural studies have also revealed that the phenyl ring of the substrate migrates through the hydrophobic cavity within the active site during catalysis and that the Brønsted acid-base catalysts (Lys 166 and His 297) may be utilized as binding determinants for inhibitor recognition. In addition, structural studies on the adduct formed from the irreversible inhibition of MR by 3-hydroxypyruvate revealed that MR can form and deprotonate a Schiff-base with 3-hydroxypyruvate to yield an enol(ate)-aldehyde adduct, suggesting a possible evolutionary link between MR and the Schiff-base forming aldolases. As the archetype of the enolase superfamily, mechanistic and structural studies on MR will continue to enhance our understanding of enzyme catalysis and furnish insights into the evolution of enzyme function.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Racemases e Epimerases/metabolismo
[Mh] Termos MeSH secundário: Bactérias/química
Bactérias/metabolismo
Domínio Catalítico
Cinética
Ácidos Mandélicos/química
Ácidos Mandélicos/metabolismo
Modelos Moleculares
Pseudomonas putida/química
Pseudomonas putida/enzimologia
Pseudomonas putida/metabolismo
Racemases e Epimerases/química
Especificidade por Substrato
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Mandelic Acids); EC 5.1.- (Racemases and Epimerases); EC 5.1.2.2 (mandelate racemase); NH496X0UJX (mandelic acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE



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