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Pesquisa : D08.811.682.690.416.277 [Categoria DeCS]
Referências encontradas : 257 [refinar]
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[PMID]:29364608
[Ti] Título:[Not Available.]
[So] Source:Mikrobiologiia;85(5):609-612, 2016 Sep.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Catecol 1,2-Dioxigenase/metabolismo
Catecóis/metabolismo
Hidroxibenzoatos/farmacologia
Rhodococcus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/isolamento & purificação
Catecol 1,2-Dioxigenase/genética
Catecol 1,2-Dioxigenase/isolamento & purificação
Catecóis/química
Ativação Enzimática/efeitos dos fármacos
Ensaios Enzimáticos
Expressão Gênica
Cinética
Rhodococcus/enzimologia
Rhodococcus/genética
Frações Subcelulares/química
Frações Subcelulares/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Catechols); 0 (Hydroxybenzoates); 2ZFW40OJ7U (3-hydroxybenzoic acid); EC 1.13.11.1 (Catechol 1,2-Dioxygenase)
[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:180125
[St] Status:MEDLINE


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[PMID]:27208235
[Au] Autor:Wadke N; Kandasamy D; Vogel H; Lah L; Wingfield BD; Paetz C; Wright LP; Gershenzon J; Hammerbacher A
[Ad] Endereço:Max Planck Institute for Chemical Ecology, 07745 Jena, Germany (N.W., D.K., H.V., C.P., L.P.W., J.G., A.H.);University of Potsdam, 14476 Golm, Germany (L.L.); andDepartment of Genetics, Forestry and Agricultural Biotechnology Institute, University of Pretoria, Pretoria 0028, South Africa (B.D.W.).
[Ti] Título:The Bark-Beetle-Associated Fungus, Endoconidiophora polonica, Utilizes the Phenolic Defense Compounds of Its Host as a Carbon Source.
[So] Source:Plant Physiol;171(2):914-31, 2016 Jun.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Norway spruce (Picea abies) is periodically attacked by the bark beetle Ips typographus and its fungal associate, Endoconidiophora polonica, whose infection is thought to be required for successful beetle attack. Norway spruce produces terpenoid resins and phenolics in response to fungal and bark beetle invasion. However, how the fungal associate copes with these chemical defenses is still unclear. In this study, we investigated changes in the phenolic content of Norway spruce bark upon E. polonica infection and the biochemical factors mediating these changes. Although genes encoding the rate-limiting enzymes in Norway spruce stilbene and flavonoid biosynthesis were actively transcribed during fungal infection, there was a significant time-dependent decline of the corresponding metabolites in fungal lesions. In vitro feeding experiments with pure phenolics revealed that E. polonica transforms both stilbenes and flavonoids to muconoid-type ring-cleavage products, which are likely the first steps in the degradation of spruce defenses to substrates that can enter the tricarboxylic acid cycle. Four genes were identified in E. polonica that encode catechol dioxygenases carrying out these reactions. These enzymes catalyze the cleavage of phenolic rings with a vicinal dihydroxyl group to muconoid products accepting a wide range of Norway spruce-produced phenolics as substrates. The expression of these genes and E. polonica utilization of the most abundant spruce phenolics as carbon sources both correlated positively with fungal virulence in several strains. Thus, the pathways for the degradation of phenolic compounds in E. polonica, initiated by catechol dioxygenase action, are important to the infection, growth, and survival of this bark beetle-vectored fungus and may play a major role in the ability of I. typographus to colonize spruce trees.
[Mh] Termos MeSH primário: Ascomicetos/fisiologia
Carbono/metabolismo
Fenóis/metabolismo
Picea/microbiologia
Doenças das Plantas/microbiologia
Gorgulhos/microbiologia
[Mh] Termos MeSH secundário: Animais
Ascomicetos/patogenicidade
Catecol 1,2-Dioxigenase/genética
Catecol 1,2-Dioxigenase/metabolismo
Catecóis/química
Catecóis/metabolismo
Flavonoides/química
Flavonoides/metabolismo
Fenóis/química
Picea/química
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Resinas Vegetais/química
Resinas Vegetais/metabolismo
Estilbenos/química
Estilbenos/metabolismo
Terpenos/química
Terpenos/metabolismo
Fatores de Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Catechols); 0 (Flavonoids); 0 (Phenols); 0 (Plant Proteins); 0 (Resins, Plant); 0 (Stilbenes); 0 (Terpenes); 0 (Virulence Factors); 7440-44-0 (Carbon); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); LF3AJ089DQ (catechol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160522
[St] Status:MEDLINE
[do] DOI:10.1104/pp.15.01916


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[PMID]:26760080
[Au] Autor:Long Y; Yang S; Xie Z; Cheng L
[Ad] Endereço:a College of Life Sciences, Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) , State Key Laboratory of Virology, Wuhan University , Wuhan , China.
[Ti] Título:Cloning, expression, and characterization of catechol 1,2-dioxygenase from a phenol-degrading Candida tropicalis JH8 strain.
[So] Source:Prep Biochem Biotechnol;46(7):673-8, 2016 Oct 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The sequence cato encoding catechol 1,2-dioxygenase from Candida tropicalis JH8 was cloned, sequenced, and expressed in Escherichia coli. The sequence cato contained an ORF of 858 bp encoding a polypeptide of 285 amino acid residues. The recombinant catechol 1,2-dioxygenase exists as a homodimer structure with a subunit molecular mass of 32 KD. Recombinant catechol 1,2-dioxygenase was unstable below pH 5.0 and stable from pH 7.0 to 9.0; its optimum pH was at 7.5. The optimum temperature for the enzyme was 30°C, and it possessed a thermophilic activity within a broad temperature range. Under the optimal conditions with catechol as substrate, the Km and Vmax of recombinant catechol 1,2-dioxygenase were 9.2 µM and 0.987 µM/min, respectively. This is the first article presenting cloning and expressing in E. coli of catechol 1,2-dioxygenase from C. tropicalis and characterization of the recombinant catechol 1,2-dioxygenase.
[Mh] Termos MeSH primário: Candida tropicalis/enzimologia
Catecol 1,2-Dioxigenase/genética
Fenóis/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Candida tropicalis/metabolismo
Catecol 1,2-Dioxigenase/química
Catecol 1,2-Dioxigenase/metabolismo
Clonagem Molecular
Concentração de Íons de Hidrogênio
Cinética
Oxigenases de Função Mista/genética
Oxigenases de Função Mista/isolamento & purificação
Oxigenases de Função Mista/metabolismo
Homologia de Sequência de Aminoácidos
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phenols); EC 1.- (Mixed Function Oxygenases); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); EC 1.14.13.7 (phenol 2-monooxygenase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170331
[Lr] Data última revisão:
170331
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160114
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2015.1135449


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[PMID]:26755240
[Au] Autor:Meena SS; Sharma RS; Gupta P; Karmakar S; Aggarwal KK
[Ad] Endereço:University School of Biotechnology, Guru Gobind Singh Indraprastha University, Dwarka, New Delhi, India.
[Ti] Título:Isolation and identification of Bacillus megaterium YB3 from an effluent contaminated site efficiently degrades pyrene.
[So] Source:J Basic Microbiol;56(4):369-78, 2016 Apr.
[Is] ISSN:1521-4028
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Industrial effluents contaminated sites may serve as repositories of ecologically adapted efficient pyrene degrading bacteria. In the present study, six bacterial isolates from industrial effluents were purified using serial enrichment technique and their pyrene degrading potential on pyrene supplemented mineral salt medium was assessed. 16S rRNA sequence analysis showed that they belong to four bacterial genera, namely Acinetobacter, Bacillus, Microbacterium, and Ochrobactrum. Among these isolates, Bacillus megaterium YB3 showed considerably good growth and was further evaluated for its pyrene-degrading efficiency. B. megaterium YB3 could degrade 72.44% of 500 mg L(-1) pyrene within 7 days. GC-MS analysis of ethyl acetate extracted fractions detected two relatively less toxic metabolic intermediates of the pyrene degradation pathway. B. megaterium YB3 also tested positive for catechol 1, 2-dioxygenase and aromatic-ring-hydroxylating dioxygenase indole-indigo conversion assays. Considering the ability and efficiency of B. megaterium YB3 to degrade high pyrene content, the strain can be used as a tool to develop bioremediation technologies for the effective biodegradation of pyrene and possibly other PAHs in the environment.
[Mh] Termos MeSH primário: Bacillus megaterium/isolamento & purificação
Bacillus megaterium/metabolismo
Pirenos/metabolismo
Microbiologia do Solo
Poluentes do Solo/metabolismo
[Mh] Termos MeSH secundário: Acetatos/química
Bacillus megaterium/enzimologia
Bacillus megaterium/genética
Biodegradação Ambiental
Catecol 1,2-Dioxigenase/análise
Dioxigenases/análise
Ativação Enzimática
Índigo Carmim/metabolismo
Hidrocarbonetos Aromáticos Policíclicos/metabolismo
Pirenos/química
RNA Ribossômico 16S/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acetates); 0 (Polycyclic Aromatic Hydrocarbons); 0 (Pyrenes); 0 (RNA, Ribosomal, 16S); 0 (Soil Pollutants); 76845O8NMZ (ethyl acetate); D3741U8K7L (Indigo Carmine); EC 1.13.11.- (Dioxygenases); EC 1.13.11.1 (Catechol 1,2-Dioxygenase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170125
[Lr] Data última revisão:
170125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE
[do] DOI:10.1002/jobm.201500533


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[PMID]:26669259
[Au] Autor:Solyanikova IP; Emelyanova EV; Borzova OV; Golovleva LA
[Ad] Endereço:a FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences , Pushchino , Russia.
[Ti] Título:Benzoate degradation by Rhodococcus opacus 1CP after dormancy: Characterization of dioxygenases involved in the process.
[So] Source:J Environ Sci Health B;51(3):182-91, 2016.
[Is] ISSN:1532-4109
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The process of benzoate degradation by strain Rhodococcus opacus 1CP after a five-year dormancy was investigated and its peculiarities were revealed. The strain was shown to be capable of growth on benzoate at a concentration of up to 10 g L(-1). The substrate specificity of benzoate dioxygenase (BDO) during the culture growth on a medium with a low (200-250 mg L(-1)) and high (4 g L(-1)) concentration of benzoate was assessed. BDO of R. opacus 1CP was shown to be an extremely narrow specificity enzyme. Out of 31 substituted benzoates, only with one, 3-chlorobenzoate, its activity was higher than 9% of that of benzoate. Two dioxygenases, catechol 1,2-dioxygenase (Cat 1,2-DO) and protocatechuate 3,4-dioxygenase (PCA 3,4-DO), were identified in a cell-free extract, purified and characterized. The substrate specificity of Cat 1,2-DO isolated from cells of strain 1CP after the dormancy was found to differ significantly from that of Cat 1,2-DO isolated earlier from cells of this strain grown on benzoate. By its substrate specificity, the described Cat 1,2-DO was close to the Cat 1,2-DO from strain 1CP grown on 4-methylbenzoate. Neither activity nor inhibition by protocatechuate was observed during the reaction of Cat 1,2-DO with catechol, and catechol had no inhibitory effect on the reaction of PCA 3,4-DO with protocatechuate.
[Mh] Termos MeSH primário: Dioxigenases/metabolismo
Rhodococcus/metabolismo
[Mh] Termos MeSH secundário: Benzoatos/metabolismo
Biodegradação Ambiental
Catecol 1,2-Dioxigenase/metabolismo
Catecóis/metabolismo
Sistema Livre de Células
Clorobenzoatos/metabolismo
Hidroxibenzoatos/metabolismo
Protocatecoate-3,4-Dioxigenase/metabolismo
Rhodococcus/fisiologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzoates); 0 (Catechols); 0 (Chlorobenzoates); 0 (Hydroxybenzoates); 02UOJ7064K (3-chlorobenzoic acid); 36R5QJ8L4B (protocatechuic acid); A26GBX5SSV (4-toluic acid); EC 1.13.11.- (Dioxygenases); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); EC 1.13.11.3 (Protocatechuate-3,4-Dioxygenase); LF3AJ089DQ (catechol)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151231
[Lr] Data última revisão:
151231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151217
[St] Status:MEDLINE
[do] DOI:10.1080/03601234.2015.1108814


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[PMID]:26563518
[Au] Autor:Lin J; Milase RN
[Ad] Endereço:Discipline of Microbiology, School of Life sciences, University of KwaZulu-Natal, Westville Campus, Private Bag X54001, Durban, 4001, South Africa. linj@ukzn.ac.za.
[Ti] Título:Purification and Characterization of Catechol 1,2-Dioxygenase from Acinetobacter sp. Y64 Strain and Escherichia coli Transformants.
[So] Source:Protein J;34(6):421-33, 2015 Dec.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This study intends to purify and characterize catechol 1,2-dioxygenase (C1,2O) of phenol-degrading Acinetobacter sp. Y64 and of E. coli transformant. Acinetobacter sp. Y64 was capable of degrading 1000 mg/L of phenol within 14 ± 2 h at 30 °C, 160 rpm and pH of 7. One C1,2O of 36 kDa was purified using ammonium sulphate precipitation and Hitrap QFF column chromatograph with 49% recovery and a 10.6-fold increase in purity. Purified Y64 C1,2O had temperature and pH optimum at 37 °C and pH 7.7 respectively with the Michaelis constant of 17.53 µM and the maximal velocity of 1.95 U/mg, respectively. The presence of Fe(3+) or Fe(2+) enhanced the activity of Y64 C1,2O while other compounds such as Ca(2+), and EDTA had an inhibitory effect. 80% of C1,2O activity remained using 4-nitrocatechol as substrate while 2% remained using 3-methylcatechol compared with that using catechol. Y64 catA gene encoding C1,2O was amplified using PCR cloned into pET22b vector and expressed in Escherichia coli BL21 DE3 (pLysS) after transformation. Purified and cloned Y64 C1,2O show no significant differences in the biochemical properties. The phylogenetic tree based on the protein sequences indicates that these C1,2Os possess a common ancestry.
[Mh] Termos MeSH primário: Acinetobacter/enzimologia
Proteínas de Bactérias/isolamento & purificação
Catecol 1,2-Dioxigenase/isolamento & purificação
Proteínas Recombinantes/isolamento & purificação
[Mh] Termos MeSH secundário: Acinetobacter/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Catecol 1,2-Dioxigenase/química
Catecol 1,2-Dioxigenase/genética
Catecol 1,2-Dioxigenase/metabolismo
Clonagem Molecular
Escherichia coli/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); EC 1.13.11.1 (Catechol 1,2-Dioxygenase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151114
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-015-9637-7


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[PMID]:26489343
[Au] Autor:He QL; Liu WB; Yang HJ; Peng XX; Guan XJ; Huang SE
[Ti] Título:[Isolation, Identification of a p-tert-Butylcatechol-Degradaing Strains and Optimization for Its Degradation by Response Surface Methodology].
[So] Source:Huan Jing Ke Xue;36(7):2695-706, 2015 Jul.
[Is] ISSN:0250-3301
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:A bacterial strain YHl that used p-tert-Butylcatechol (TBC) as the sole carbon and energy source was isolated from the activated sludge of the wastewater treatment plant of a chemical factory. The strain was identified as Pseudomonas corrugate by morphological characteristics, physiological and biochemical properties, BIOLOG and the 16S rDNA sequence analysis. The degration rate of TBC was above 82% with an initial concentration of 500 mg.L-1 at 24-36°C and an initial pH of 7. 0-10. 0. Through single-factor experiments of its degradation characteristics of strain YH1, the results showed that its optimal additional carbon and nitrogen sources were sucrose and tryptone, the optimal temperature was 30°C, the optimal initial pH was 7. 0, and the optimal inoculation volume was 2%. In order to improve the TBC degradation rate, the concentrations of sucrose and tryptone and initial pH were identified as the main factors by Placket-Burman Assay. Then these factors reached their optimal region by Steepest Ascent. Finally, the optimal levels of those main factors were further optimized using Box-Behnken design and response surface analysis. The optimal conditions were as follows: sucrose concentration 3% (ρ), tryptone concentration 1. 44% (ρ), TBC concentration 400 mg.L-1, initial pH value 8. 12, inoculation amount 2. 97% (φ), temperature 30°C, training time 96 h. Under the optimal conditions mentioned above, the TBC degradation rate reached 98. 21%. Enzymology analysis and localization experiments showed that the TBC-degrading enzymes were intracellular proteins and the synthesis of catechol 1,2-dioxygenase (C12O) could be induced by TBC. Through design of specific PCR primers for the degrading enzymes, the gene encoding the catechol 1,2-dioxygenase was amplified from YHL. It was found that genes encoding TBC-degrading enzyme were located on plasmids by the plasmid detection and elimination experiments. In addition, YH1 was tolerant to high concentration of NaCl and many kinds of heavy metal ions, and resistant to multiple antibiotics. This paper provided some information for the effective treatment of complex industrial wastewater.
[Mh] Termos MeSH primário: Catecóis/metabolismo
Pseudomonas/isolamento & purificação
Esgotos/microbiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Biodegradação Ambiental
Catecol 1,2-Dioxigenase/metabolismo
Pseudomonas/classificação
Pseudomonas/metabolismo
Eliminação de Resíduos Líquidos
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Catechols); 0 (Sewage); 27213-78-1 (tert-butylcatechol); EC 1.13.11.1 (Catechol 1,2-Dioxygenase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:161018
[Lr] Data última revisão:
161018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151023
[St] Status:MEDLINE


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[PMID]:26306712
[Au] Autor:Han L; Liu P; Sun J; Wu Y; Zhang Y; Chen W; Lin J; Wang Q; Ma Y
[Ad] Endereço:Key Laboratory of Systems Microbial Biotechnology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
[Ti] Título:Engineering catechol 1, 2-dioxygenase by design for improving the performance of the cis, cis-muconic acid synthetic pathway in Escherichia coli.
[So] Source:Sci Rep;5:13435, 2015 Aug 26.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Regulating and ameliorating enzyme expression and activity greatly affects the performance of a given synthetic pathway. In this study, a new synthetic pathway for cis, cis-muconic acid (ccMA) production was reconstructed without exogenous induction by regulating the constitutive expression of the important enzyme catechol 1,2-dioxygenase (CatA). Next, new CatAs with significantly improved activities were developed to enhance ccMA production using structure-assisted protein design. Nine mutations were designed, simulated and constructed based on the analysis of the CatA crystal structure. These results showed that mutations at Gly72, Leu73 and/or Pro76 in CatA could improve enzyme activity, and the activity of the most effective mutant was 10-fold greater than that of the wild-type CatA from Acinetobacter sp. ADP1. The most productive synthetic pathway with a mutated CatA increased the titer of ccMA by more than 25%. Molecular dynamic simulation results showed that enlarging the entrance of the substrate-binding pocket in the mutants contributed to their increased enzyme activities and thus improved the performance of the synthetic pathway.
[Mh] Termos MeSH primário: Catecol 1,2-Dioxigenase/metabolismo
Escherichia coli/fisiologia
Melhoramento Genético/métodos
Transdução de Sinais/fisiologia
Ácido Sórbico/análogos & derivados
[Mh] Termos MeSH secundário: Catecol 1,2-Dioxigenase/genética
Engenharia Metabólica/métodos
Engenharia de Proteínas/métodos
Ácido Sórbico/isolamento & purificação
Ácido Sórbico/metabolismo
Biologia Sintética/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
3KD92ZL2KH (muconic acid); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); X045WJ989B (Sorbic Acid)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150827
[St] Status:MEDLINE
[do] DOI:10.1038/srep13435


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[PMID]:26020478
[Au] Autor:Lu ZY; Guo XJ; Li H; Huang ZZ; Lin KF; Liu YD
[Ad] Endereço:State Environmental Protection Key Laboratory of Environmental Risk Assessment and Control on Chemical Process, School of Resources and Environmental Engineering, East China University of Science and Technology, Shanghai 200237, China. lzy1009a@163.com.
[Ti] Título:High-throughput screening for a moderately halophilic phenol-degrading strain and its salt tolerance response.
[So] Source:Int J Mol Sci;16(6):11834-48, 2015 May 25.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:A high-throughput screening system for moderately halophilic phenol-degrading bacteria from various habitats was developed to replace the conventional strain screening owing to its high efficiency. Bacterial enrichments were cultivated in 48 deep well microplates instead of shake flasks or tubes. Measurement of phenol concentrations was performed in 96-well microplates instead of using the conventional spectrophotometric method or high-performance liquid chromatography (HPLC). The high-throughput screening system was used to cultivate forty-three bacterial enrichments and gained a halophilic bacterial community E3 with the best phenol-degrading capability. Halomonas sp. strain 4-5 was isolated from the E3 community. Strain 4-5 was able to degrade more than 94% of the phenol (500 mg · L(-1) starting concentration) over a range of 3%-10% NaCl. Additionally, the strain accumulated the compatible solute, ectoine, with increasing salt concentrations. PCR detection of the functional genes suggested that the largest subunit of multicomponent phenol hydroxylase (LmPH) and catechol 1,2-dioxygenase (C12O) were active in the phenol degradation process.
[Mh] Termos MeSH primário: Halomonadaceae/isolamento & purificação
Halomonadaceae/fisiologia
Ensaios de Triagem em Larga Escala/métodos
Fenóis/metabolismo
Tolerância a Sal
[Mh] Termos MeSH secundário: Diamino Aminoácidos/metabolismo
Proteínas de Bactérias/genética
Biodegradação Ambiental
Catecol 1,2-Dioxigenase/genética
Halomonadaceae/genética
Oxigenases de Função Mista/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids, Diamino); 0 (Bacterial Proteins); 0 (Phenols); 7GXZ3858RY (ectoine); EC 1.- (Mixed Function Oxygenases); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); EC 1.14.13.7 (phenol 2-monooxygenase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150708
[Lr] Data última revisão:
150708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150529
[St] Status:MEDLINE
[do] DOI:10.3390/ijms160611834


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[PMID]:25916475
[Au] Autor:Ontañon OM; González PS; Agostini E
[Ad] Endereço:Departamento de Biología Molecular, FCEFQyN, Universidad Nacional de Río Cuarto, Ruta 36 Km 601. CP 5800, Río Cuarto, Córdoba, Argentina, oontanon@exa.unrc.edu.ar.
[Ti] Título:Biochemical and molecular mechanisms involved in simultaneous phenol and Cr(VI) removal by Acinetobacter guillouiae SFC 500-1A.
[So] Source:Environ Sci Pollut Res Int;22(17):13014-23, 2015 Sep.
[Is] ISSN:1614-7499
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Bioremediation has emerged as an environmental friendly strategy to deal with environmental pollution. Since the majority of polluted sites contain complex mixtures of inorganic and organic pollutants, it is important to find bacterial strains that can cope with multiple contaminants. In this work, a bacterial strain isolated from tannery sediments was identified as Acinetobacter guillouiae SFC 500-1A. This strain was able to simultaneously remove high phenol and Cr(VI) concentrations, and the mechanisms involved in such process were evaluated. The phenol biodegradation was catalized by a phenol-induced catechol 1,2-dioxygenase through an ortho-cleavage pathway. Also, NADH-dependent chromate reductase activity was measured in the cytosolic fraction. The ability of this strain to reduce Cr(VI) to Cr(III) was corroborated by detection of Cr(III) in cellular biomass after the removal process. While phenol did not affect significantly the chromate reductase activity, Cr(VI) was a major disruptor of catechol dioxygenase activity. Nevertheless, this activity was high even in presence of high Cr(VI) concentrations. Our results suggest the potential application of A. guillouiae SFC 500-1A for wastewaters treatment, and the obtained data provide the insights into the removal mechanisms, dynamics, and possible limitations of the bioremediation.
[Mh] Termos MeSH primário: Acinetobacter/metabolismo
Cromo/metabolismo
Fenóis/metabolismo
Purificação da Água
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Biodegradação Ambiental
Catecol 1,2-Dioxigenase/metabolismo
Cromo/isolamento & purificação
Redes e Vias Metabólicas
Oxirredução
Oxirredutases/metabolismo
Fenóis/isolamento & purificação
Filogenia
Transporte Proteico
Águas Residuais/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Phenols); 0 (Waste Water); 0R0008Q3JB (Chromium); 18540-29-9 (chromium hexavalent ion); EC 1.- (Oxidoreductases); EC 1.13.11.1 (Catechol 1,2-Dioxygenase); EC 1.97.- (chromate reductase)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150429
[St] Status:MEDLINE
[do] DOI:10.1007/s11356-015-4571-y



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