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[PMID]:29458497
[Au] Autor:Qu JH; Zhang LJ; Fu YH; Li XD; Li HF; Tian HL
[Ad] Endereço:College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, Henan Province, PR China.
[Ti] Título:A novel genus of the class Actinobacteria, Longivirga aurantiaca gen. nov., sp. nov., isolated from lake sediment.
[So] Source:Int J Syst Evol Microbiol;68(3):942-946, 2018 Mar.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] 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 ).
[Mh] Termos MeSH primário: Actinobacteria/classificação
Sedimentos Geológicos/microbiologia
Lagos/microbiologia
Filogenia
[Mh] Termos MeSH secundário: Actinobacteria/genética
Actinobacteria/isolamento & purificação
Técnicas de Tipagem Bacteriana
Composição de Bases
Parede Celular/química
China
DNA Bacteriano/genética
Ácido Diaminopimélico/química
Ácidos Graxos/química
Peptidoglicano/química
Fosfolipídeos/química
Pigmentação
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Vitamina K 2/análogos & derivados
Vitamina K 2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] 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)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002615


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[PMID]:29188665
[Au] Autor:Zou KN; Hu M; Huang JP; Zhou HG
[Ad] 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.
[Ti] Título:[Identification of Vaginal Fluid Using Microbial Signatures].
[So] Source:Fa Yi Xue Za Zhi;32(4):254-256, 2016 Aug.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] 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.
[Mh] Termos MeSH primário: Líquidos Corporais/microbiologia
Vagina/microbiologia
[Mh] Termos MeSH secundário: Actinobacteria/classificação
Sangue/microbiologia
Fezes/microbiologia
Feminino
Genes Bacterianos
Seres Humanos
Lactobacillus/classificação
Cavidade Nasal/microbiologia
Reação em Cadeia da Polimerase
RNA Ribossômico 16S/genética
Saliva/microbiologia
Sêmen/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.04.004


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[PMID]:29362365
[Au] Autor:Zhang Y; Kastman EK; Guasto JS; Wolfe BE
[Ad] Endereço:Department of Biology, Tufts University, 200 Boston Avenue, Medford, MA, 02155, USA.
[Ti] Título:Fungal networks shape dynamics of bacterial dispersal and community assembly in cheese rind microbiomes.
[So] Source:Nat Commun;9(1):336, 2018 01 23.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Queijo/microbiologia
DNA Bacteriano/genética
Fungos/crescimento & desenvolvimento
Hifas/crescimento & desenvolvimento
Interações Microbianas/genética
Microbiota/genética
Serratia/genética
[Mh] Termos MeSH secundário: Actinobacteria/classificação
Actinobacteria/genética
Actinobacteria/crescimento & desenvolvimento
Elementos de DNA Transponíveis
Firmicutes/classificação
Firmicutes/genética
Firmicutes/crescimento & desenvolvimento
Flagelos/genética
Flagelos/ultraestrutura
Fungos/ultraestrutura
Sequenciamento de Nucleotídeos em Larga Escala
Hifas/ultraestrutura
Movimento/fisiologia
Mucor/crescimento & desenvolvimento
Mucor/ultraestrutura
Mutação
Penicillium/crescimento & desenvolvimento
Penicillium/ultraestrutura
Proteobactérias/classificação
Proteobactérias/genética
Proteobactérias/crescimento & desenvolvimento
Serratia/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Bacterial)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02522-z


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[PMID]:29318252
[Au] Autor:Carvalho ATP; Dourado DFAR; Skvortsov T; de Abreu M; Ferguson LJ; Quinn DJ; Moody TS; Huang M
[Ad] 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.
[Ti] Título:Spatial requirement for PAMO for transformation of non-native linear substrates.
[So] Source:Phys Chem Chem Phys;20(4):2558-2570, 2018 Jan 24.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Oxigenases de Função Mista/metabolismo
[Mh] Termos MeSH secundário: Acetona/análogos & derivados
Acetona/química
Acetona/metabolismo
Actinobacteria/enzimologia
Sequência de Aminoácidos
Sítios de Ligação
Biocatálise
Domínio Catalítico
Cetonas/química
Cetonas/metabolismo
Cinética
Oxigenases de Função Mista/química
Oxigenases de Função Mista/genética
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Alinhamento de Sequência
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ketones); 0 (Recombinant Proteins); 1364PS73AF (Acetone); EC 1.- (Mixed Function Oxygenases); J2G84H29AF (2-octanone); O7IZH10V9Y (1-phenyl-2-propanone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07172h


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[PMID]:29364609
[Ti] Título:[Not Available.]
[So] Source:Mikrobiologiia;85(5):613-616, 2016 Sep.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Mh] Termos MeSH primário: Actinobacteria/metabolismo
Caprolactama/análogos & derivados
Caprolactama/metabolismo
Polímeros/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Actinobacteria/isolamento & purificação
Adipatos/metabolismo
Ácido Aminocaproico/metabolismo
Caproatos/metabolismo
Meios de Cultura/química
Hidrólise
Esgotos/microbiologia
Ácido Succínico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] 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)
[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]:29364602
[Au] Autor:Danilova OV; Belova SE; Gagarinova IV; Dedysh SN
[Ti] Título:Microbial Community Composition and Methanotroph Diversity of a Subarctic Wetland in Russia.
[So] Source:Mikrobiologiia;85(5):545-554, 2016 Sep.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Água Subterrânea/microbiologia
Metano/metabolismo
Consórcios Microbianos/fisiologia
Oxigenases/genética
[Mh] Termos MeSH secundário: Acidobacteria/classificação
Acidobacteria/genética
Acidobacteria/isolamento & purificação
Acidobacteria/metabolismo
Actinobacteria/classificação
Actinobacteria/genética
Actinobacteria/isolamento & purificação
Actinobacteria/metabolismo
Alphaproteobacteria/classificação
Alphaproteobacteria/genética
Alphaproteobacteria/isolamento & purificação
Alphaproteobacteria/metabolismo
Regiões Árticas
Proteínas de Bactérias/metabolismo
Briófitas/fisiologia
Gammaproteobacteria/classificação
Gammaproteobacteria/genética
Gammaproteobacteria/isolamento & purificação
Gammaproteobacteria/metabolismo
Expressão Gênica
Líquens/fisiologia
Metano/química
Oxigenases/metabolismo
Filogenia
Planctomycetales/classificação
Planctomycetales/genética
Planctomycetales/isolamento & purificação
Planctomycetales/metabolismo
Federação Russa
Verrucomicrobia/classificação
Verrucomicrobia/genética
Verrucomicrobia/isolamento & purificação
Verrucomicrobia/metabolismo
Zonas Úmidas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.13.- (Oxygenases); EC 1.14.13.25 (methane monooxygenase); OP0UW79H66 (Methane)
[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]:28583351
[Au] Autor:Yasuda K; Sugimoto H; Hayashi K; Takita T; Yasukawa K; Ohta M; Kamakura M; Ikushiro S; Shiro Y; Sakaki T
[Ad] 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.
[Ti] Título:Protein engineering of CYP105s for their industrial uses.
[So] Source:Biochim Biophys Acta;1866(1):23-31, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Actinobacteria/genética
Substituição de Aminoácidos
Proteínas de Bactérias/química
Sistema Enzimático do Citocromo P-450/química
Mutação
Engenharia de Proteínas/métodos
[Mh] Termos MeSH secundário: Actinobacteria/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Colecalciferol/metabolismo
Sequência Conservada
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Ferredoxinas/metabolismo
Expressão Gênica
Hidroxilação
Isoenzimas
Lovastatina/análogos & derivados
Lovastatina/metabolismo
Simulação de Acoplamento Molecular
Pravastatina/biossíntese
Streptomyces/enzimologia
Streptomyces/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] 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)
[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:170607
[St] Status:MEDLINE


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[PMID]:28455615
[Au] Autor:Meng S; Wu H; Wang L; Zhang B; Bai L
[Ad] Endereço:State Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai, 200240, China.
[Ti] Título:Enhancement of antibiotic productions by engineered nitrate utilization in actinomycetes.
[So] Source:Appl Microbiol Biotechnol;101(13):5341-5352, 2017 Jul.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Actinobacteria/genética
Antibacterianos/biossíntese
Lincomicina/biossíntese
Nitratos/metabolismo
Streptomyces/genética
[Mh] Termos MeSH secundário: Actinobacteria/metabolismo
Proteínas de Transporte de Ânions/genética
Antraquinonas/metabolismo
Antibacterianos/metabolismo
Proteínas de Bactérias/genética
Regulação Bacteriana da Expressão Gênica
Nitrogênio/metabolismo
Piranos/metabolismo
Streptomyces/metabolismo
Streptomyces coelicolor/genética
Transativadores/genética
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] 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)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-017-8292-7


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[PMID]:28471358
[Au] Autor:Yasutake Y; Kameda T; Tamura T
[Ad] 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.
[Ti] 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.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):266-275, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Actinobacteria/química
Proteínas de Bactérias/química
Calcifediol/química
Colecalciferol/química
Sistema Enzimático do Citocromo P-450/química
Mutação
[Mh] Termos MeSH secundário: Actinobacteria/enzimologia
Motivos de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Calcifediol/metabolismo
Domínio Catalítico
Colecalciferol/metabolismo
Clonagem Molecular
Cristalografia por Raios X
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Ligações de Hidrogênio
Cinética
Simulação de Dinâmica Molecular
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Engenharia de Proteínas
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 1C6V77QF41 (Cholecalciferol); 9035-51-2 (Cytochrome P-450 Enzyme System); P6YZ13C99Q (Calcifediol)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17004782


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[PMID]:28471355
[Au] Autor:Wang R; Wu J; Jin DK; Chen Y; Lv Z; Chen Q; Miao Q; Huo X; Wang F
[Ad] Endereço:Wuxi Biortus Biosciences Co. Ltd, A5, 6 Dongsheng West Road, 214437 Jiangyin, Jiangsu, People's Republic of China.
[Ti] Título:Structure of NADP -bound 7ß-hydroxysteroid dehydrogenase reveals two cofactor-binding modes.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):246-252, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] 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.
[Mh] Termos MeSH primário: Actinobacteria/química
Proteínas de Bactérias/química
Hidroxiesteroide Desidrogenases/química
NADP/química
Ácido Ursodesoxicólico/química
[Mh] Termos MeSH secundário: Actinobacteria/enzimologia
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Hidroxiesteroide Desidrogenases/genética
Hidroxiesteroide Desidrogenases/metabolismo
Modelos Moleculares
NADP/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ácido Ursodesoxicólico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] 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)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17004460



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