Relevant bibliographies by topics / Ktedonobacter racemifer

Academic literature on the topic 'Ktedonobacter racemifer'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Ktedonobacter racemifer"

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Tomazini, Atilio, Sadhana Lal, Riffat Munir, Matthew Stott, Bernard Henrissat, Igor Polikarpov, Richard Sparling, and David B. Levin. "Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability." Canadian Journal of Microbiology 64, no. 12 (December 2018): 992–1003. http://dx.doi.org/10.1139/cjm-2018-0336.

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The phylum Chloroflexi is phylogenetically diverse and is a deeply branching lineage of bacteria that express a broad spectrum of physiological and metabolic capabilities. Members of the order Ktedonobacteriales, including the families Ktedonobacteriaceae, Thermosporotrichaceae, and Thermogemmatisporaceae, all have flexible aerobic metabolisms capable of utilizing a wide range of carbohydrates. A number of species within these families are considered cellulolytic and are capable of using cellulose as a sole carbon and energy source. In contrast, Ktedonobacter racemifer, the type strain of the order, does not appear to possess this cellulolytic phenotype. In this study, we confirmed the ability of Thermogemmatispora sp. strain T81 to hydrolyze cellulose, determined the whole-genome sequence of Thermogemmatispora sp. T81, and using comparative bioinformatics analyses, identified genes encoding putative carbohydrate-active enzymes (CAZymes) in the Thermogemmatispora sp. T81, Thermogemmatispora onikobensis, and Ktedonobacter racemifer genomes. Analyses of the Thermogemmatispora sp. T81 genome identified 64 CAZyme gene sequences belonging to 57 glycoside hydrolase families. The genome of Thermogemmatispora sp. T81 encodes 19 genes for putative extracellular CAZymes, similar to the number of putative extracellular CAZymes identified in T. onikobensis (17) and K. racemifer (17), despite K. racemifer not possessing a cellulolytic phenotype. These results suggest that these members of the order Ktedonobacteriales may use a broader range of carbohydrate polymers than currently described.
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Yabe, Shuhei, Yoshifumi Aiba, Yasuteru Sakai, Masaru Hazaka, and Akira Yokota. "Thermosporothrix hazakensis gen. nov., sp. nov., isolated from compost, description of Thermosporotrichaceae fam. nov. within the class Ktedonobacteria Cavaletti et al. 2007 and emended description of the class Ktedonobacteria." International Journal of Systematic and Evolutionary Microbiology 60, no. 8 (August 1, 2010): 1794–801. http://dx.doi.org/10.1099/ijs.0.018069-0.

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We isolated from compost an aerobic, thermophilic, Gram-stain-positive, spore-forming bacterium that formed branched vegetative and aerial mycelia. This strain, designated SK20-1T, grew at 31–58 °C, with optimum growth at 50 °C, while no growth was observed below 28 or above 60 °C. The pH range for growth was 5.4–8.7, with optimum growth at pH 7.0, while no growth was observed below pH 5.0 or above pH 9.1. Strain SK20-1T was able to hydrolyse polysaccharides such as cellulose, xylan and chitin. The DNA G+C content was 54.0 mol%. The major fatty acid was iso-C17 : 0 and the major menaquinone was MK-9(H2). The cell wall contained glutamic acid, serine, alanine and ornithine in a molar ratio of 1.00 : 1.07 : 2.64 : 0.83. The polar lipids consisted of phosphatidylinositol, phosphatidylinositol mannosides, phosphatidylglycerol, diphosphatidylglycerol and an unknown glycolipid. Cell-wall sugars were rhamnose and mannose. Detailed phylogenetic analysis based on 16S rRNA gene sequences indicated that strain SK20-1T belongs to the class Ktedonobacteria, and that the strain is most closely related to Ktedonobacter racemifer SOSP1-21T (88.5 %). On the basis of its phenotypic features and phylogenetic position, we propose that SK20-1T represents a novel genus and species, Thermosporothrix hazakensis gen. nov., sp. nov., within the new family Thermosporotrichaceae fam. nov. The type strain of Thermosporothrix hazakensis is strain SK20-1T (=JCM 16142T =ATCC BAA-1881T). In addition, we propose an emended description of the class Ktedonobacteria to classify the class in the phylum Chloroflexi.
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Chang, Yun-juan, Miriam Land, Loren Hauser, Olga Chertkov, Tijana Glavina Del Rio, Matt Nolan, Alex Copeland, et al. "Non-contiguous finished genome sequence and contextual data of the filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1-21T)." Standards in Genomic Sciences 5, no. 1 (October 1, 2011): 97–111. http://dx.doi.org/10.4056/sigs.2114901.

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Munday, Samuel D., Natasha K. Maddigan, Rosemary J. Young, and Stephen G. Bell. "Characterisation of two self-sufficient CYP102 family monooxygenases from Ktedonobacter racemifer DSM44963 which have new fatty acid alcohol product profiles." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 6 (June 2016): 1149–62. http://dx.doi.org/10.1016/j.bbagen.2016.01.023.

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Klein, Joshua G., Yang Wu, Bashkim Kokona, and Louise K. Charkoudian. "Widening the bottleneck: Heterologous expression, purification, and characterization of the Ktedonobacter racemifer minimal type II polyketide synthase in Escherichia coli." Bioorganic & Medicinal Chemistry 28, no. 20 (October 2020): 115686. http://dx.doi.org/10.1016/j.bmc.2020.115686.

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Maddigan, Natasha K., and Stephen G. Bell. "The self-sufficient CYP102 family enzyme, Krac9955, from Ktedonobacter racemifer DSM44963 acts as an alkyl- and alkyloxy-benzoic acid hydroxylase." Archives of Biochemistry and Biophysics 615 (February 2017): 15–21. http://dx.doi.org/10.1016/j.abb.2016.12.014.

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7

Yabe, Shuhei, Yu Zheng, Chiung-mei Wang, Yasuteru Sakai, Keietsu Abe, Akira Yokota, Stefano Donadio, Linda Cavaletti, and Paolo Monciardini. "Reticulibacter mediterranei gen. nov., sp. nov., within the new family Reticulibacteraceae fam. nov., and Ktedonospora formicarum gen. nov., sp. nov., Ktedonobacter robiniae sp. nov., Dictyobacter formicarum sp. nov. and Dictyobacter arantiisoli sp. nov., belonging to the class Ktedonobacteria." International Journal of Systematic and Evolutionary Microbiology 71, no. 7 (July 23, 2021). http://dx.doi.org/10.1099/ijsem.0.004883.

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The aerobic, Gram-positive, mesophilic Ktedonobacteria strains, Uno17T, SOSP1-1T, 1-9T, 1-30T and 150040T, formed mycelia of irregularly branched filaments, produced spores or sporangia, and numerous secondary metabolite biosynthetic gene clusters. The five strains grew at 15–40 °C (optimally at 30 °C) and pH 4.0–8.0 (optimally at pH 6.0–7.0), and had 7.21–12.67 Mb genomes with 49.7–53.7 mol% G+C content. They shared MK9(H2) as the major menaquinone and C16 : 1-2OH and iso-C17 : 0 as the major cellular fatty acids. Phylogenetic and phylogenomic analyses showed that Uno17T and SOSP1-9T were most closely related to members of the genus Dictyobacter , with 94.43–96.21 % 16S rRNA gene similarities and 72.16–81.56% genomic average nucleotide identity. The strain most closely related to SOSP1-1T and SOSP1-30T was Ktedonobacter racemifer SOSP1-21T, with 91.33 and 98.84 % 16S rRNA similarities, and 75.13 and 92.35% average nucleotide identities, respectively. Strain 150040T formed a distinct clade within the order Ktedonobacterales , showing <90.47 % 16S rRNA gene similarity to known species in this order. Based on these results, we propose: strain 150040T as Reticulibacter mediterranei gen. nov., sp. nov. (type strain 150 040T=CGMCC 1.17052T=BCRC 81202T) within the family Reticulibacteraceae fam. nov. in the order Ktedonobacterales ; strain SOSP1-1T as Ktedonospora formicarum gen. nov., sp. nov. (type strain SOSP1-1T=CGMCC 1.17205T=BCRC 81203T) and strain SOSP1-30T as Ktedonobacter robiniae sp. nov. (type strain SOSP1-30T=CGMCC 1.17733T=BCRC 81205T) within the family Ktedonobacteraceae ; strain Uno17T as Dictyobacter arantiisoli sp. nov. (type strain Uno17T=NBRC 113155T=BCRC 81116T); and strain SOSP1-9T as Dictyobacter formicarum sp. nov. (type strain SOSP1-9T=CGMCC 1.17206T=BCRC 81204T) within the family Dictyobacteraceae .
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Dissertations / Theses on the topic "Ktedonobacter racemifer"

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Munday, Samuel David. "Investigations and applications of self-sufficient cytochrome P450 monooxygenases." Thesis, 2016. http://hdl.handle.net/2440/100734.

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The cytochrome P450 superfamily catalyses the oxidation of a vast array of organic molecules. Most commonly, this oxidation process ensues by the insertion of a single oxygen atom from dioxygen into an unreactive C-H bond. There is a high degree of interest for this reaction type in conventional synthesis, but it is difficult to achieve high levels of selectivity and is often performed under harsh conditions. CYP102A1 or P450Bm3 from Bacillus megaterium however, can perform this oxidative process under physiological conditions and so researchers have a strong interest in exploiting the potential benefits of this enzyme. The natural substrates of P450Bm3 are fatty acids but this thesis will address both modern and classical techniques to improve catalytic performance with a variety of non-natural substrates. The first two results chapters of this thesis (Chapters 3 and 4) describe the effect of decoy molecules on non-natural substrate oxidation with the aim of improving rates of product formation while maintaining the selectivity of the enzyme. Analysis of the oxidation of these substrates by wild-type P450Bm3 and the variant KT2 showed substantial increases in product formation rate while maintaining the regioselectivity. As a rigorous test of regioselectivity, a selection of xylenes were used that have previously been shown to generate multiple products upon P450Bm3 oxidation. Retention of enantioselectivity was also assessed by using prochiral substrates that have stereocentres introduced upon P450Bm3 oxidation. Chiral chromatography analysis of these turnovers showed that in most cases, the enantioselectivity of the enzyme was either maintained or marginally improved. Knowing that xylenes give a range of oxidation products upon P450Bm3 activity, a wider range of disubsituted benzene compounds were also analysed (Chapter 5). These substrates were chosen to resemble potential xenobiotic compounds in order to assess what metabolites may be produced by P450Bm3 and therefore other P450 systems. These substrates were analysed with several P450Bm3 variants and significantly improved rates of product formation were observed, enabling identification of the likely metabolites. Chapter 6 describes an investigation into two potential CYP102 family members from the bacterium Ktedonobacter racemifer DSM44963 (Krac0936 and Krac9955). Their sequenced genes show similarities to P450Bm3, which encouraged the investigation of a range of fatty acid substrates with these two enzymes. Although their product distributions differed, both Krac0936 and Krac9955 were active with straight-chain saturated and unsaturated fatty acids.
Thesis (M.Phil.) -- University of Adelaide, School of Physical Sciences, 2016.
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