Base de dados : MEDLINE
Pesquisa : B03.510.460.400.400.049 [Categoria DeCS]
Referências encontradas : 2890 [refinar]
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  1 / 2890 MEDLINE  
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PMID:29458497
Autor:Qu JH; Zhang LJ; Fu YH; Li XD; Li HF; Tian HL
Endereço:College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, Henan Province, PR China.
Título:A novel genus of the class Actinobacteria, Longivirga aurantiaca gen. nov., sp. nov., isolated from lake sediment.
Fonte:Int J Syst Evol Microbiol; 68(3):942-946, 2018 Mar.
ISSN:1466-5034
País de publicação:England
Idioma:eng
Resumo:A novel actinobacterial strain, designated X5 , was isolated from the sediment of Taihu Lake in China and was subjected to a polyphasic taxonomic characterization. The strain formed orange-red colonies comprising aerobic, Gram-stain-negative, rod-shaped cells on R2A agar. Phylogenetic analysis based on the 16S rRNA gene sequences revealed that the organism was closely related to the genus Sporichthya and consistently formed a distinct clade along with the members of this genus. The closest phylogenetic neighbour was Sporichthya polymorpha NBRC 12702 with 93.7 % 16S rRNA gene sequence similarity. The major fatty acids (>10 %) were iso-C16 : 0 (18.7 %), C18 : 1ω9c (18.6 %) and C17 : 1ω8c (14.0 %). The genomic DNA G+C content was 74.4 mol%. The organism contained menaquinone MK-8(H2), MK-9(H4) and an unidentified menaquinone. Polar lipids were composed of phosphatidylglycerol, an unidentified lipid, two unidentified phospholipids and two unidentified aminolipids. The whole-cell sugars contained ribose, xylose, mannose, glucose and galactose. The cell-wall peptidoglycan contained ll-diaminopimelic acid. Based on the physiological, biochemical and chemotaxonomic data, the organism is proposed to represent a novel genus and species, for which the name Longivirga aurantiaca gen. nov., sp. nov. is proposed. The type strain is X5 (=CGMCC 4.7317 =NBRC 112237 ).
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Peptidoglycan); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-38-6 (vitamin MK 8); 583-93-7 (Diaminopimelic Acid)


  2 / 2890 MEDLINE  
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PMID:29188665
Autor:Zou KN; Hu M; Huang JP; Zhou HG
Endereço:Shanghai Key Laboratory of Crime Scene Evidence, Key Laboratory of Forensic Evidence and Science Technology, Ministry of Public Security, Institute of Forensic Science, Shanghai Public Security Bureau, Shanghai 200083, China.
Título:[Identification of Vaginal Fluid Using Microbial Signatures].
Fonte:Fa Yi Xue Za Zhi; 32(4):254-256, 2016 Aug.
ISSN:1004-5619
País de publicação:China
Idioma:chi
Resumo:OBJECTIVES: To investigate the specific microbial signatures in vaginal fluid. METHODS: Vaginal fluid (16 samples), saliva (16 samples), feces (16 samples), semen (8 samples), peripheral blood (8 samples), urine (5 samples), and nasal secretion (4 samples) were collected respectively. The genes of , , , , and were amplified. PCR production was detected via a 3130xl Genetic Analyzer. RESULTS: The detected number of , , , , and were 15, 5, 8, 14, and 3 in all vaginal fluid samples, respectively. and existed specifically in vaginal fluid. CONCLUSIONS: There is a potential application value to detect and for the identification of vaginal fluid.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (RNA, Ribosomal, 16S)


  3 / 2890 MEDLINE  
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PMID:29362365
Autor:Zhang Y; Kastman EK; Guasto JS; Wolfe BE
Endereço:Department of Biology, Tufts University, 200 Boston Avenue, Medford, MA, 02155, USA.
Título:Fungal networks shape dynamics of bacterial dispersal and community assembly in cheese rind microbiomes.
Fonte:Nat Commun; 9(1):336, 2018 01 23.
ISSN:2041-1723
País de publicação:England
Idioma:eng
Resumo:Most studies of bacterial motility have examined small-scale (micrometer-centimeter) cell dispersal in monocultures. However, bacteria live in multispecies communities, where interactions with other microbes may inhibit or facilitate dispersal. Here, we demonstrate that motile bacteria in cheese rind microbiomes use physical networks created by filamentous fungi for dispersal, and that these interactions can shape microbial community structure. Serratia proteamaculans and other motile cheese rind bacteria disperse on fungal networks by swimming in the liquid layers formed on fungal hyphae. RNA-sequencing, transposon mutagenesis, and comparative genomics identify potential genetic mechanisms, including flagella-mediated motility, that control bacterial dispersal on hyphae. By manipulating fungal networks in experimental communities, we demonstrate that fungal-mediated bacterial dispersal can shift cheese rind microbiome composition by promoting the growth of motile over non-motile community members. Our single-cell to whole-community systems approach highlights the interactive dynamics of bacterial motility in multispecies microbiomes.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nome de substância:0 (DNA Transposable Elements); 0 (DNA, Bacterial)


  4 / 2890 MEDLINE  
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PMID:29318252
Autor:Carvalho ATP; Dourado DFAR; Skvortsov T; de Abreu M; Ferguson LJ; Quinn DJ; Moody TS; Huang M
Endereço:School of Chemistry and Chemical Engineering, Queen's University, David Keir Building, Stranmillis Road, Belfast BT9 5AG, Northern Ireland, UK. m.huang@qub.ac.uk.
Título:Spatial requirement for PAMO for transformation of non-native linear substrates.
Fonte:Phys Chem Chem Phys; 20(4):2558-2570, 2018 Jan 24.
ISSN:1463-9084
País de publicação:England
Idioma:eng
Resumo:Phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenases family, and therefore it is an ideal candidate for the synthesis of industrially relevant ester or lactone compounds. However, its limited substrate scope has largely limited its industrial applications. Linear substrates are interesting from an industrial point of view, it is thus necessary to identify the essential spatial requirement for achieving high conversions for non-native linear substrates. Here using molecular dynamics simulations, we compared the conversion of a non-native linear substrate 2-octanone and the native substrate phenylacetone, catalyzed by the WT enzyme and a quadruple variant P253F/G254A/R258M/L443F that exhibits significantly improved activity towards 2-octanone. We uncovered that a remarkable movement of L289 is crucial for a reshaping of the active site of the quadruple variant so as to prevent the aliphatic substrate from moving away from the C4a-peroxyflavin, thus enabling it to keep a catalytically relevant pose during the oxygenation process. By performing steady-state kinetic analysis of two single-mutation variants at position 258, we further validated that the L289 reposition is attributed to the combined effect of quadruple mutations. In order to further explore the substrate scope of PAMO we also studied the binding of cyclopentanone and 2-phenylcyclohexanone, which are the typical substrates of CPMO in group I and CHMO in group III, respectively. Our study provides fundamental atomic-level insights in rational engineering of PAMO for wide applications in industrial biocatalysis, in particular, in the biotransformation of long-chain aliphatic oils into potential biodiesels.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Ketones); 0 (Recombinant Proteins); 1364PS73AF (Acetone); EC 1.- (Mixed Function Oxygenases); J2G84H29AF (2-octanone); O7IZH10V9Y (1-phenyl-2-propanone)


  5 / 2890 MEDLINE  
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PMID:29364609
Título:[Not Available.]
Fonte:Mikrobiologiia; 85(5):613-616, 2016 Sep.
ISSN:0026-3656
País de publicação:Russia (Federation)
Idioma:rus
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (6-oxohexanoic acid); 0 (Adipates); 0 (Caproates); 0 (Culture Media); 0 (Polymers); 0 (Sewage); 25038-54-4 (nylon 6); 6879X594Z8 (Caprolactam); 72-89-9 (Acetyl Coenzyme A); 76A0JE0FKJ (adipic acid); AB6MNQ6J6L (Succinic Acid); U6F3787206 (Aminocaproic Acid)


  6 / 2890 MEDLINE  
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PMID:29364602
Autor:Danilova OV; Belova SE; Gagarinova IV; Dedysh SN
Título:Microbial Community Composition and Methanotroph Diversity of a Subarctic Wetland in Russia.
Fonte:Mikrobiologiia; 85(5):545-554, 2016 Sep.
ISSN:0026-3656
País de publicação:Russia (Federation)
Idioma:eng
Resumo:This study assessed the microbial diversity, activity, and composition of methane-oxidizing communities of a subarctic wetland in Russia,with mosaic cover of Sphagnum mosses and lichens of the genera Cladonia and Cetraria. Potential methane-oxidizing activity of peat sampled from lichen-dominated wetland sites was higher than that in the sites dominated by Sphagnum mosses. In peat from lichendominated sites, major bacterial groups identified by high-throughput sequencing of the 16S rRNA genes were the Acidobacteria (35.4-41.2% of total 16S rRNA gene reads), Alphaproteobacteria (19.1-24.2%), Gammaproteobacteria (7.9-11.1%), Actinobacteria (5.5-13.2%), Planctomycetes (7.2-9.5%), and Verrucomicrobia (5.1-9.5%). The distinctive feature of this community was high proportion of Subdivision 2 Acidobacteria, which are not char- acteristic for boreal Sphagnum peat bogs. Methanotrophic community composition was determined by mo- lecular analysis of the pmoA gene encoding particulate methane monooxygenase. Most (-80%) of all pmoA gene fragments revealed in peat from lichen-dominated sites belonged to the phylogenetic lineage represented by a microaerobic spiral-shaped methanotroph, "Candidatus Methylospira mobilis." Members of the genus Methylocystis, which are typical inhabitants of boreal Sphagnum peat bogs, represented only a minor group of indigenous methanotrophs. The specific feature of a methanotrophic community in peat from lichen-dominated sites was the presence of uncultivated USCa (Upland Soil Cluster alpha) methanotrophs, which are typical for acidic upland soils showing atmospheric methane oxidation. The methanotrophic community composition in lichen-dominated sites of a tundra wetland, therefore, was markedly different from that in bo- real Sphagnum peat bogs.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); EC 1.13.- (Oxygenases); EC 1.14.13.25 (methane monooxygenase); OP0UW79H66 (Methane)


  7 / 2890 MEDLINE  
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PMID:28583351
Autor:Yasuda K; Sugimoto H; Hayashi K; Takita T; Yasukawa K; Ohta M; Kamakura M; Ikushiro S; Shiro Y; Sakaki T
Endereço:Department of Pharmaceutical Engineering, Faculty of Engineering, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan; Department of Biotechnology, Faculty of Engineering, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
Título:Protein engineering of CYP105s for their industrial uses.
Fonte:Biochim Biophys Acta; 1866(1):23-31, 2018 01.
ISSN:0006-3002
País de publicação:Netherlands
Idioma:eng
Resumo:Cytochrome P450 enzymes belonging to the CYP105 family are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales. In this review, we focused on the protein engineering of P450s belonging to the CYP105 family for industrial use. Two Arg substitutions to Ala of CYP105A1 enhanced its vitamin D 25- and 1α-hydroxylation activities by 400 and 100-fold, respectively. The coupling efficiency between product formation and NADPH oxidation was largely improved by the R84A mutation. The quintuple mutant Q87W/T115A/H132L/R194W/G294D of CYP105AB3 showed a 20-fold higher activity than the wild-type enzyme. Amino acids at positions 87 and 191 were located at the substrate entrance channel, and that at position 294 was located close to the heme group. Semi-rational engineering of CYP105A3 selected the best performing mutant, T85F/T119S/V194N/N363Y, for producing pravastatin. The T119S and N363Y mutations synergistically had remarkable effects on the interaction between CYP105A3 and putidaredoxin. Although wild-type CYP105AS1 hydroxylated compactin to 6-epi-pravastatin, the quintuple mutant I95T/Q127R/A180V/L236I/A265N converted almost all compactin to pravastatin. Five amino acid substitutions by two rounds of mutagenesis almost completely changed the stereo-selectivity of CYP105AS1. These results strongly suggest that the protein engineering of CYP105 enzymes greatly increase their industrial utility. 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.
Tipo de publicação: JOURNAL ARTICLE; REVIEW
Nome de substância:0 (Bacterial Proteins); 0 (Ferredoxins); 0 (Isoenzymes); 1C6V77QF41 (Cholecalciferol); 1UQM1K0W9X (mevastatin); 57087-75-9 (putidaredoxin); 9035-51-2 (Cytochrome P-450 Enzyme System); 9LHU78OQFD (Lovastatin); EC 1.14.- (P450SU1 protein, Streptomyces griseolus); KXO2KT9N0G (Pravastatin)


  8 / 2890 MEDLINE  
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PMID:28455615
Autor:Meng S; Wu H; Wang L; Zhang B; Bai L
Endereço:State Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai, 200240, China.
Título:Enhancement of antibiotic productions by engineered nitrate utilization in actinomycetes.
Fonte:Appl Microbiol Biotechnol; 101(13):5341-5352, 2017 Jul.
ISSN:1432-0614
País de publicação:Germany
Idioma:eng
Resumo:Nitrate is necessary for primary and secondary metabolism of actinomycetes and stimulates the production of a few antibiotics, such as lincomycin and rifamycin. However, the mechanism of this nitrate-stimulating effect was not fully understood. Two putative ABC-type nitrate transporters were identified in Streptomyces lincolnensis NRRL2936 and verified to be involved in lincomycin biosynthesis. With nitrate supplementation, the transcription of nitrogen assimilation genes, nitrate-specific ABC1 transporter genes, and lincomycin exporter gene lmrA was found to be enhanced and positively regulated by the global regulator GlnR, whose expression was also improved. Moreover, heterologous expression of ABC2 transporter genes in Streptomyces coelicolor M145 resulted in an increased actinorhodin production. Further incorporation of a nitrite-specific transporter gene nirC, as in nirC-ABC2 cassette, led to an even higher actinorhodin production. Similarly, the titers of salinomycin, ansamitocin, lincomycin, and geldanamycin were increased with the integration of this cassette to Streptomyces albus BK3-25, Actinosynnema pretiosum ATCC31280, S. lincolnensis LC-G, and Streptomyces hygroscopicus XM201, respectively. Our work expanded the nitrate-stimulating effect to many antibiotic producers by utilizing the nirC-ABC2 cassette for enhanced nitrate utilization, which could become a general tool for titer increase of antibiotics in actinomycetes.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Anion Transport Proteins); 0 (Anthraquinones); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (GlnR protein, Streptomyces coelicolor); 0 (NirC protein, Bacteria); 0 (Nitrates); 0 (Pyrans); 0 (Trans-Activators); 62UXS86T64 (salinomycin); BOD072YW0F (Lincomycin); G4HH387T6Z (actinorhodin); N762921K75 (Nitrogen)


  9 / 2890 MEDLINE  
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PMID:28471358
Autor:Yasutake Y; Kameda T; Tamura T
Endereço:Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517, Japan.
Título:Structural insights into the mechanism of the drastic changes in enzymatic activity of the cytochrome P450 vitamin D hydroxylase (CYP107BR1) caused by a mutation distant from the active site.
Fonte:Acta Crystallogr F Struct Biol Commun; 73(Pt 5):266-275, 2017 May 01.
ISSN:2053-230X
País de publicação:United States
Idioma:eng
Resumo:Cytochromes P450 (P450s) are haem-containing enzymes that catalyze medically and industrially important oxidative reactions, and many P450s have been subjected to directed evolution and site-directed mutagenesis to improve their activity and substrate specificity. Nonetheless, in most cases the mechanism that leads to drastic changes in specific activity after the introduction of an amino-acid substitution distant from the active-site pocket is unclear. Here, two crystal structures of inactive mutants of the P450 vitamin D hydroxylase (Vdh), Vdh-F106V and Vdh-L348M, which were obtained in the course of protein-engineering experiments on Vdh, are reported. The overall structures of these mutants show an open conformation similar to that of wild-type Vdh (Vdh-WT), whereas a rearrangement of the common main-chain hydrogen bonds is observed in the CD-loop (residues 102-106), resulting in a more compactly folded CD-loop relative to that of Vdh-WT. The previously reported structures of Vdh-WT and of the highly active Vdh-T107A and Vdh-K1 mutants have a more stretched CD-loop, with partial formation of 3 -helix-type hydrogen bonds, both in the open and closed states. Molecular-dynamics simulations also showed that the frequency of the 3 -helix is significantly reduced in Vdh-F106V and Vdh-L348M. The closed conformation is crucial for substrate and ferredoxin binding to initiate the catalytic reaction of Vdh. Therefore, it is implied that the small local structural changes observed in this study might disrupt the conformational transition from the open to the closed state, thereby leading to a complete loss of vitamin D hydroxylase activity.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); 0 (Recombinant Proteins); 1C6V77QF41 (Cholecalciferol); 9035-51-2 (Cytochrome P-450 Enzyme System); P6YZ13C99Q (Calcifediol)


  10 / 2890 MEDLINE  
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PMID:28471355
Autor:Wang R; Wu J; Jin DK; Chen Y; Lv Z; Chen Q; Miao Q; Huo X; Wang F
Endereço:Wuxi Biortus Biosciences Co. Ltd, A5, 6 Dongsheng West Road, 214437 Jiangyin, Jiangsu, People's Republic of China.
Título:Structure of NADP -bound 7ß-hydroxysteroid dehydrogenase reveals two cofactor-binding modes.
Fonte:Acta Crystallogr F Struct Biol Commun; 73(Pt 5):246-252, 2017 May 01.
ISSN:2053-230X
País de publicação:United States
Idioma:eng
Resumo:In mammals, bile acids/salts and their glycine and taurine conjugates are effectively recycled through enterohepatic circulation. 7ß-Hydroxysteroid dehydrogenases (7ß-HSDHs; EC 1.1.1.201), including that from the intestinal microbe Collinsella aerofaciens, catalyse the NADPH-dependent reversible oxidation of secondary bile-acid products to avoid potential toxicity. Here, the first structure of NADP bound to dimeric 7ß-HSDH is presented. In one active site, NADP adopts a conventional binding mode similar to that displayed in related enzyme structures. However, in the other active site a unique binding mode is observed in which the orientation of the nicotinamide is different. Since 7ß-HSDH has become an attractive target owing to the wide and important pharmaceutical use of its product ursodeoxycholic acid, this work provides a more detailed template to support rational protein engineering to improve the enzymatic activities of this useful biocatalyst, further improving the yield of ursodeoxycholic acid and its other applications.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); 0 (Recombinant Proteins); 53-59-8 (NADP); 724L30Y2QR (Ursodeoxycholic Acid); EC 1.1.- (Hydroxysteroid Dehydrogenases); EC 1.1.1.- (7 beta-hydroxysteroid dehydrogenase)



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