Base de dados : MEDLINE
Pesquisa : B03.510.024.049.537.775 [Categoria DeCS]
Referências encontradas : 2260 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 226 ir para página                         

  1 / 2260 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
[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


  2 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28745867
[Au] Autor:DeLorenzo DM; Henson WR; Moon TS
[Ad] Endereço:Department of Energy, Environmental and Chemical Engineering, Washington University in St. Louis , St. Louis, Missouri 63130, United States.
[Ti] Título:Development of Chemical and Metabolite Sensors for Rhodococcus opacus PD630.
[So] Source:ACS Synth Biol;6(10):1973-1978, 2017 Oct 20.
[Is] ISSN:2161-5063
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rhodococcus opacus PD630 is a nonmodel, Gram-positive bacterium that possesses desirable traits for biomass conversion, including consumption capabilities for lignocellulose-based sugars and toxic lignin-derived aromatic compounds, significant triacylglycerol accumulation, relatively rapid growth rate, and genetic tractability. However, few genetic elements have been directly characterized in R. opacus, limiting its application for lignocellulose bioconversion. Here, we report the characterization and development of genetic tools for tunable gene expression in R. opacus, including: (1) six fluorescent reporters for quantifying promoter output, (2) three chemically inducible promoters for variable gene expression, and (3) two classes of metabolite sensors derived from native R. opacus promoters that detect nitrogen levels or aromatic compounds. Using these tools, we also provide insights into native aromatic consumption pathways in R. opacus. Overall, this work expands the ability to control and characterize gene expression in R. opacus for future lignocellulose-based fuel and chemical production.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Rhodococcus/genética
[Mh] Termos MeSH secundário: Lignina/metabolismo
Nitrogênio/metabolismo
Regiões Promotoras Genéticas/genética
Rhodococcus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9005-53-2 (Lignin); N762921K75 (Nitrogen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1021/acssynbio.7b00192


  3 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27771781
[Au] Autor:Müller CA; Weingartner AM; Dennig A; Ruff AJ; Gröger H; Schwaneberg U
[Ad] Endereço:Institute of Biotechnology, RWTH Aachen University, Worringerweg 3, 52074, Aachen, Germany.
[Ti] Título:A whole cell biocatalyst for double oxidation of cyclooctane.
[So] Source:J Ind Microbiol Biotechnol;43(12):1641-1646, 2016 Dec.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A novel whole cell cascade for double oxidation of cyclooctane to cyclooctanone was developed. The one-pot oxidation cascade requires only a minimum of reaction components: resting E. coli cells in aqueous buffered medium (=catalyst), the target substrate and oxygen as environmental friendly oxidant. Conversion of cyclooctane was catalysed with high efficiency (50% yield) and excellent selectivity (>94%) to cyclooctanone. The reported oxidation cascade represents a novel whole cell system for double oxidation of non-activated alkanes including an integrated cofactor regeneration. Notably, two alcohol dehydrogenases from Lactobacillus brevis and from Rhodococcus erythropolis with opposite cofactor selectivities and one monooxygenase P450 BM3 were produced in a coexpression system in one single host. The system represents the most efficient route with a TTN of up to 24363 being a promising process in terms of sustainability as well.
[Mh] Termos MeSH primário: Álcool Desidrogenase/química
Proteínas de Bactérias/química
Ciclo-Octanos/química
Oxigenases de Função Mista/química
[Mh] Termos MeSH secundário: Álcool Desidrogenase/biossíntese
Proteínas de Bactérias/metabolismo
Biocatálise
Reatores Biológicos
Evolução Molecular Direcionada
Escherichia coli/genética
Escherichia coli/metabolismo
Lactobacillus brevis/enzimologia
Oxigenases de Função Mista/biossíntese
Oxirredução
Rhodococcus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cyclooctanes); EC 1.- (Mixed Function Oxygenases); EC 1.1.1.1 (Alcohol Dehydrogenase); KKZ3KBS654 (cyclooctane)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  4 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28726102
[Au] Autor:Maksimova YG; Gorbunova AN; Demakov VA
[Ad] Endereço:Institute of Ecology and Genetics of Microorganisms, Ural Branch, Russian Academy of Sciences, Perm, 614081, Russia. maks@iegm.ru.
[Ti] Título:Stereoselective biotransformation of phenylglycine nitrile by heterogeneous biocatalyst based on immobilized bacterial cells and enzyme preparation.
[So] Source:Dokl Biochem Biophys;474(1):183-185, 2017 May.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:We studied the effect of a heterogeneous environment on the stereoselectivity of transformation of racemic phenylglycine nitrile. Immobilized biocatalysts were prepared by adhesion of Pseudomonas fluorescens C2 cells on carbon-containing supports and covalent crosslinking of nitrile hydratase and amidase of Rhodococcus rhodochrous 4-1 to activated chitosan as well as by the method of cross-linked aggregates. At a reaction duration of 20 h, the ratio of phenylglycine stereoisomers changes depending on the presence of support in medium. The highest optical purity of the product (enantiomeric excess of L-phenylglycine solution, 98%) is achieved when enzyme aggregates of nitrile hydratase and amidase cross-linked with 0.1% glutaraldehyde are used as a biocatalyst.
[Mh] Termos MeSH primário: Acetonitrilos/química
Acetonitrilos/metabolismo
Amidoidrolases/metabolismo
Biocatálise
Hidroliases/metabolismo
Pseudomonas/citologia
[Mh] Termos MeSH secundário: Amidoidrolases/química
Aderência Bacteriana
Biotransformação
Células Imobilizadas/citologia
Hidroliases/química
Hidrólise
Rhodococcus/enzimologia
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetonitriles); 0 (phenylglycine nitrile); EC 3.5.- (Amidohydrolases); EC 3.5.1.4 (amidase); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.- (nitrile hydratase)
[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:170721
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672917030139


  5 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28696117
[Au] Autor:Marques SM; Dunajova Z; Prokop Z; Chaloupkova R; Brezovsky J; Damborsky J
[Ad] Endereço:Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment RECETOX, Faculty of Science, Masaryk University , Kamenice 5/A13, 625 00 Brno, Czech Republic.
[Ti] Título:Catalytic Cycle of Haloalkane Dehalogenases Toward Unnatural Substrates Explored by Computational Modeling.
[So] Source:J Chem Inf Model;57(8):1970-1989, 2017 Aug 28.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The anthropogenic toxic compound 1,2,3-trichloropropane is poorly degradable by natural enzymes. We have previously constructed the haloalkane dehalogenase DhaA31 by focused directed evolution ( Pavlova, M. et al. Nat. Chem. Biol. 2009 , 5 , 727 - 733 ), which is 32 times more active than the wild-type enzyme and is currently the most active variant known against that substrate. Recent evidence has shown that the structural basis responsible for the higher activity of DhaA31 was poorly understood. Here we have undertaken a comprehensive computational study of the main steps involved in the biocatalytic hydrolysis of 1,2,3-trichloropropane to decipher the structural basis for such enhancements. Using molecular dynamics and quantum mechanics approaches we have surveyed (i) the substrate binding, (ii) the formation of the reactive complex, (iii) the chemical step, and (iv) the release of the products. We showed that the binding of the substrate and its transport through the molecular tunnel to the active site is a relatively fast process. The cleavage of the carbon-halogen bond was previously identified as the rate-limiting step in the wild-type. Here we demonstrate that this step was enhanced in DhaA31 due to a significantly higher number of reactive configurations of the substrate and a decrease of the energy barrier to the S 2 reaction. C176Y and V245F were identified as the key mutations responsible for most of those improvements. The release of the alcohol product was found to be the rate-limiting step in DhaA31 primarily due to the C176Y mutation. Mutational dissection of DhaA31 and kinetic analysis of the intermediate mutants confirmed the theoretical observations. Overall, our comprehensive computational approach has unveiled mechanistic details of the catalytic cycle which will enable a balanced design of more efficient enzymes. This approach is applicable to deepen the biochemical knowledge of a large number of other systems and may contribute to robust strategies in the development of new biocatalysts.
[Mh] Termos MeSH primário: Biocatálise
Simulação por Computador
Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Hidrolases/química
Hidrolases/genética
Cinética
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Mutação
Rhodococcus/enzimologia
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.- (Hydrolases); EC 3.8.1.5 (haloalkane dehalogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00070


  6 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28688759
[Au] Autor:Eschapasse E; Hussenet C; Bergeron A; Lebeaux D
[Ad] Endereço:Service de pneumologie, institut du thorax, hôpital G.-et-R.-Laënnec, CHU de Nantes, 44093 Nantes, France.
[Ti] Título:[Respiratory infections caused by slow-growing bacteria: Nocardia, Actinomyces, Rhodococcus].
[Ti] Título:Infections respiratoires à bactéries à croissance lente : Nocardia, Actinomyces, Rhodococcus..
[So] Source:Rev Mal Respir;34(6):661-671, 2017 Jun.
[Is] ISSN:1776-2588
[Cp] País de publicação:France
[La] Idioma:fre
[Ab] Resumo:INTRODUCTION: Pneumonia caused by slow-growing bacteria is rare but sometimes severe. STATE OF THE ART: These infections share many similarities such as several differential diagnoses, difficulties to identify the pathogen, the importance of involving the microbiologist in the diagnostic investigation and the need for prolonged antibiotic treatment. However, major differences distinguish them: Nocardia and Rhodococcus infect mainly immunocompromised patients while actinomycosis also concerns immunocompetent patients; the severity of nocardioses is related to their hematogenous spread while locoregional extension by contiguity makes the gravity of actinomycosis. PROSPECTIVE: For these diseases, molecular diagnostic tools are essential, either to obtain a species identification and guide treatment in the case of nocardiosis or to confirm the diagnosis from a biological sample. Treatment of these infections is complex due to: (1) the limited data in the literature; (2) the need for prolonged treatment of several months; (3) the management of toxicities and drug interactions for the treatment of Nocardia and Rhodococcus. CONCLUSION: Close cooperation between pneumonologists, infectious disease specialists and microbiologists is essential for the management of these patients.
[Mh] Termos MeSH primário: Actinomyces
Nocardia
Infecções Respiratórias/microbiologia
Rhodococcus
[Mh] Termos MeSH secundário: Actinomyces/crescimento & desenvolvimento
Actinomyces/isolamento & purificação
Infecções por Actinomycetales/diagnóstico
Infecções por Actinomycetales/microbiologia
Infecções por Actinomycetales/terapia
Actinomicose/diagnóstico
Actinomicose/microbiologia
Actinomicose/terapia
Bactérias/crescimento & desenvolvimento
Bactérias/isolamento & purificação
Diagnóstico Diferencial
Seres Humanos
Hospedeiro Imunocomprometido
Nocardia/crescimento & desenvolvimento
Nocardia/isolamento & purificação
Nocardiose/diagnóstico
Nocardiose/microbiologia
Nocardiose/terapia
Pneumonia/diagnóstico
Pneumonia/microbiologia
Pneumonia/terapia
Infecções Respiratórias/epidemiologia
Infecções Respiratórias/patologia
Infecções Respiratórias/terapia
Rhodococcus/crescimento & desenvolvimento
Rhodococcus/isolamento & purificação
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170710
[St] Status:MEDLINE


  7 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28686600
[Au] Autor:Ott L; Hacker E; Kunert T; Karrington I; Etschel P; Lang R; Wiesmann V; Wittenberg T; Singh A; Varela C; Bhatt A; Sangal V; Burkovski A
[Ad] Endereço:Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
[Ti] Título:Analysis of Corynebacterium diphtheriae macrophage interaction: Dispensability of corynomycolic acids for inhibition of phagolysosome maturation and identification of a new gene involved in synthesis of the corynomycolic acid layer.
[So] Source:PLoS One;12(7):e0180105, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Corynebacterium diphtheriae is the causative agent of diphtheria, a toxin mediated disease of upper respiratory tract, which can be fatal. As a member of the CMNR group, C. diphtheriae is closely related to members of the genera Mycobacterium, Nocardia and Rhodococcus. Almost all members of these genera comprise an outer membrane layer of mycolic acids, which is assumed to influence host-pathogen interactions. In this study, three different C. diphtheriae strains were investigated in respect to their interaction with phagocytic murine and human cells and the invertebrate infection model Caenorhabditis elegans. Our results indicate that C. diphtheriae is able to delay phagolysosome maturation after internalization in murine and human cell lines. This effect is independent of the presence of mycolic acids, as one of the strains lacked corynomycolates. In addition, analyses of NF-κB induction revealed a mycolate-independent mechanism and hint to detrimental effects of the different strains tested on the phagocytic cells. Bioinformatics analyses carried out to elucidate the reason for the lack of mycolates in one of the strains led to the identification of a new gene involved in mycomembrane formation in C. diphtheriae.
[Mh] Termos MeSH primário: Corynebacterium diphtheriae/genética
Difteria/microbiologia
Interações Hospedeiro-Patógeno/genética
Macrófagos/microbiologia
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Caenorhabditis elegans/microbiologia
Linhagem Celular
Corynebacterium diphtheriae/metabolismo
Corynebacterium diphtheriae/patogenicidade
Difteria/genética
Difteria/patologia
Seres Humanos
Macrófagos/metabolismo
Macrófagos/patologia
Camundongos
Mycobacterium/genética
Ácidos Micólicos/metabolismo
NF-kappa B/genética
Nocardia/genética
Fagossomos/microbiologia
Rhodococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mycolic Acids); 0 (NF-kappa B); 18951-35-4 (corynomycolic acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180105


  8 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28657620
[Au] Autor:Singh SP; Guha S; Bose P
[Ad] Endereço:Department of Civil Engineering, Indian Institute of Technology, Kanpur-208016, India. pbose@iitk.ac.in sguha@iitk.ac.in.
[Ti] Título:Impact of the composition of the bacterial population and additional carbon source on the pathway and kinetics of degradation of endosulfan isomers.
[So] Source:Environ Sci Process Impacts;19(7):964-974, 2017 Jul 19.
[Is] ISSN:2050-7895
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Abiotic and bacterial degradation is presented for the two isomers α- and ß- of the organochlorine pesticide endosulfan, denoted as ES-1 and ES-2, respectively. Biodegradation studies were conducted with two indigenous species Pseudomonas putida (P. putida) and Rhodococcus sp. Both ES isomers rapidly hydrolyzed in water at pH ≥ 7 but the hydrolysis was inhibited in the presence of biomass. The pesticide partitioned onto the biomass making it unavailable for abiotic hydrolytic reaction. Spontaneous temperature dependent abiotic conversion of ES-2 to ES-1 was reported in the presence of dual air-water phases but was not observed in the abiotic aqueous phase. Biodegradation experiments with pure isomers showed a small amount of interconversion (∼5%) in either direction and ruled out any preferential interconversion of the ES-2 isomer to ES-1 or vice versa. Both the species were shown to degrade ES-2 at a higher rate compared to ES-1 which may lead to enrichment of ES-1 in agricultural fields in short-term following application of the pesticide. P. putida degraded both the ES isomers through oxidative and hydrolytic pathways while the Rhodococcus sp. used only the hydrolytic pathway. Since ES-S (product of the oxidative pathway) is orders of magnitude more toxic than the parent isomers, the short term toxicity of a field following the application of the pesticide may increase if the composition of the indigenous bacterial population is such that the oxidative pathway is preferred over the hydrolytic one. The presence of an additional carbon source increased the rates of degradation of both the isomers but the enhancement was greater for the degradation rate of ES-2 than ES-1.
[Mh] Termos MeSH primário: Carbono/química
Endossulfano/análise
Inseticidas/análise
Pseudomonas putida/crescimento & desenvolvimento
Rhodococcus/crescimento & desenvolvimento
Poluentes do Solo/análise
[Mh] Termos MeSH secundário: Aerobiose
Biodegradação Ambiental
Biomassa
Endossulfano/química
Glucose/química
Hidrólise
Inseticidas/química
Isomerismo
Cinética
Modelos Teóricos
Poluentes do Solo/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insecticides); 0 (Soil Pollutants); 7440-44-0 (Carbon); IY9XDZ35W2 (Glucose); OKA6A6ZD4K (Endosulfan)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1039/c7em00154a


  9 / 2260 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28644864
[Au] Autor:Lan Y; Zhang X; Liu Z; Zhou L; Shen R; Zhong X; Cui W; Zhou Z
[Ad] Endereço:Key Laboratory of Industrial Biotechnology (Ministry of Education), School of Biotechnology, Jiangnan University, Wuxi, China.
[Ti] Título:Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.
[So] Source:PLoS One;12(6):e0179833, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitrile hydratase (NHase) from Rhodococcus rhodochrous J1 is widely used for industrial production of acrylamide and nicotinamide. However, the two types of NHases (L-NHase and H-NHase) from R. rhodochrous J1 were only slightly expressed in E. coli by routine methods, which limits the comprehensive and systematic characterization of the enzyme properties. We successfully expressed the two types of recombinant NHases in E. coli by codon-optimization, engineering of Ribosome Binding Site (RBS) and spacer sequences. The specific activity of the purified L-NHase and H-NHase were 400 U/mg and 234 U/mg, respectively. The molecular mass of L-NHase and H-NHase was identified to be 94 kDa and 504 kDa, respectively, indicating that the quaternary structure of the two types of NHases was the same as those in R. rhodochrous J1. H-NHase exhibited higher substrate and product tolerance than L-NHase. Moreover, higher activity and shorter culture time were achieved in recombinant E. coli, and the whole cell catalyst of recombinant E. coli harboring H-NHase has equivalent efficiency in tolerance to the high-concentration product relative to that in R. rhodochrous J1. These results indicate that biotransformation of nitrile by R. rhodochrous J1 represents a potential alternative to NHase-producing E. coli.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Hidroliases/genética
Hidroliases/metabolismo
Rhodococcus/enzimologia
Rhodococcus/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/síntese química
Proteínas de Bactérias/isolamento & purificação
Sítios de Ligação/genética
Biotransformação
Códon
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática
Escherichia coli/enzimologia
Expressão Gênica
Engenharia Genética
Hidroliases/síntese química
Hidroliases/isolamento & purificação
RNA Mensageiro/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Codon); 0 (RNA, Messenger); 0 (Recombinant Proteins); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.- (nitrile hydratase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179833


  10 / 2260 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28642093
[Au] Autor:Guevara G; Heras LFL; Perera J; Llorens JMN
[Ad] Endereço:Department of Biochemistry and Molecular Biology I, Universidad Complutense de Madrid, 28040, Madrid, Spain.
[Ti] Título:Functional characterization of 3-ketosteroid 9α-hydroxylases in Rhodococcus ruber strain chol-4.
[So] Source:J Steroid Biochem Mol Biol;172:176-187, 2017 Sep.
[Is] ISSN:1879-1220
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 3-Ketosteroid-9α-Hydroxylase, also known as KshAB [androsta-1,4-diene-3,17-dione, NADH:oxygen oxidoreductase (9α-hydroxylating); EC 1.14.13.142)], is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with a 3-ketosteroid-Δ -dehydrogenase activity (KstD), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9α-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9α-hydroxy-4-androsten-3,17-dione (9OHAD) or 9α-hydroxy-1,4-androstadiene-3,17-dione (9OHADD), respectively. The redundancy of these enzymes in the actinobacterial genomes results in a serious difficulty for metabolic engineering this catabolic pathway to obtain intermediates of industrial interest. In this work, we have identified three homologous kshA genes and one kshB gen in different genomic regions of R. ruber strain Chol-4. We present a set of data that helps to understand their specific roles in this strain, including: i) description of the KshAB enzymes ii) construction and characterization of ΔkshB and single, double and triple ΔkshA mutants in R. ruber iii) growth studies of the above strains on different substrates and iv) genetic complementation and biotransformation assays with those strains. Our results show that KshA2 isoform is needed for the degradation of steroid substrates with short side chain, while KshA3 works on those molecules with longer side chains. KshA1 is a more versatile enzyme related to the cholic acid catabolism, although it also collaborates with KshA2 or KshA3 activities in the catabolism of steroids. Accordingly to what it is described for other Rhodococcus strains, our results also suggest that the side chain degradation is KshAB-independent.
[Mh] Termos MeSH primário: Androstenos/metabolismo
Proteínas de Bactérias/metabolismo
Colesterol/metabolismo
Oxigenases de Função Mista/metabolismo
Subunidades Proteicas/metabolismo
Rhodococcus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Oxigenases de Função Mista/genética
Mutação
Fases de Leitura Aberta
Filogenia
Subunidades Proteicas/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Rhodococcus/classificação
Rhodococcus/genética
Rhodococcus/isolamento & purificação
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Esgotos/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Androstenes); 0 (Bacterial Proteins); 0 (Isoenzymes); 0 (Protein Subunits); 0 (Recombinant Proteins); 0 (Sewage); 97C5T2UQ7J (Cholesterol); EC 1.- (Mixed Function Oxygenases)
[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:170624
[St] Status:MEDLINE



página 1 de 226 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

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