Academic literature on the topic 'Fumarase Superfamily'

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Journal articles on the topic "Fumarase Superfamily"

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Partovi, Sarah E., Florence Mus, Andrew E. Gutknecht, et al. "Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily." Journal of Biological Chemistry 293, no. 14 (2018): 5236–46. http://dx.doi.org/10.1074/jbc.ra117.001234.

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Puthan Veetil, Vinod, Guntur Fibriansah, Hans Raj, Andy-Mark W. H. Thunnissen, and Gerrit J. Poelarends. "Aspartase/Fumarase Superfamily: A Common Catalytic Strategy Involving General Base-Catalyzed Formation of a Highly Stabilized aci-Carboxylate Intermediate." Biochemistry 51, no. 21 (2012): 4237–43. http://dx.doi.org/10.1021/bi300430j.

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Rinaldo, S., G. Giardina, M. Brunori, and F. Cutruzzolà. "N-oxide sensing and denitrification: the DNR transcription factors." Biochemical Society Transactions 34, no. 1 (2006): 185–87. http://dx.doi.org/10.1042/bst0340185.

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All denitrifiers can keep the steady-state concentrations of nitrite and nitric oxide (NO) below cytotoxic levels by controlling the expression of denitrification gene clusters by redox signalling through transcriptional regulators belonging to the CRP (cAMP receptor protein)/FNR (fumarate and nitrate reductase regulator) superfamily.
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Rinaldo, S., G. Giardina, M. Brunori, and F. Cutruzzolà. "N-oxide sensing in Pseudomonas aeruginosa: expression and preliminary characterization of DNR, an FNR–CRP type transcriptional regulator." Biochemical Society Transactions 33, no. 1 (2005): 184–86. http://dx.doi.org/10.1042/bst0330184.

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In denitrifying bacteria, the concentration of NO is maintained low by a tight control of the expression and activity of nitrite and NO reductases. Regulation involves redox-linked transcription factors, such as those belonging to the CRP-FNR (cAMP receptor protein–fumarate and nitrate reductase regulator) superfamily, which act as oxygen and N-oxide sensors. Given that few members of this superfamily have been characterized in detail, we have cloned, expressed and purified the dissimilative nitrate respiration regulator from Pseudomonas aeruginosa. To gain insights on the structural propertie
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Teague, Josiah L., John K. Barrows, Cynthia A. Baafi, and Michael W. Van Dyke. "Discovering the DNA-Binding Consensus of the Thermus thermophilus HB8 Transcriptional Regulator TTHA1359." International Journal of Molecular Sciences 22, no. 18 (2021): 10042. http://dx.doi.org/10.3390/ijms221810042.

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Transcription regulatory proteins, also known as transcription factors, function as molecular switches modulating the first step in gene expression, transcription initiation. Cyclic-AMP receptor proteins (CRPs) and fumarate and nitrate reduction regulators (FNRs) compose the CRP/FNR superfamily of transcription factors, regulating gene expression in response to a spectrum of stimuli. In the present work, a reverse-genetic methodology was applied to the study of TTHA1359, one of four CRP/FNR superfamily transcription factors in the model organism Thermus thermophilus HB8. Restriction Endonuclea
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Marastoni, Damiano, Anna I. Pisani, Gianmarco Schiavi, et al. "CSF TNF and osteopontin levels correlate with the response to dimethyl fumarate in early multiple sclerosis." Therapeutic Advances in Neurological Disorders 15 (January 2022): 175628642210921. http://dx.doi.org/10.1177/17562864221092124.

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Background: Disease activity in the first years after a diagnosis of relapsing-remitting multiple sclerosis (RRMS) is a negative prognostic factor for long-term disability. Markers of both clinical and radiological responses to disease-modifying therapies (DMTs) are advocated. Objective: The objective of this study is to estimate the value of cerebrospinal fluid (CSF) inflammatory markers at the time of diagnosis in predicting the disease activity in treatment-naïve multiple sclerosis (MS) patients exposed to dimethyl fumarate (DMF). Methods: In total, 48 RRMS patients (31 females/17 males) tr
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Giardina, Giorgio, Nicoletta Castiglione, Manuela Caruso, Francesca Cutruzzolà, and Serena Rinaldo. "The Pseudomonas aeruginosa DNR transcription factor: light and shade of nitric oxide-sensing mechanisms." Biochemical Society Transactions 39, no. 1 (2011): 294–98. http://dx.doi.org/10.1042/bst0390294.

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In response to environmental conditions, NO (nitric oxide) induces global changes in the cellular metabolism of Pseudomonas aeruginosa, which are strictly related to pathogenesis. In particular, at low oxygen tensions and in the presence of NO the denitrification alternative respiration is activated by a key regulator: DNR (dissimilative nitrate respiration regulator). DNR belongs to the CRP (cAMP receptor protein)–FNR (fumarate and nitrate reductase regulatory protein) superfamily of bacterial transcription factors. These regulators are involved in many different pathways and distinct activat
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Jardim-Messeder, Douglas, Caroline Cabreira-Cagliari, Rafael Rauber, Andreia Carina Turchetto-Zolet, Rogério Margis, and Márcia Margis-Pinheiro. "Fumarate reductase superfamily: A diverse group of enzymes whose evolution is correlated to the establishment of different metabolic pathways." Mitochondrion 34 (May 2017): 56–66. http://dx.doi.org/10.1016/j.mito.2017.01.002.

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Nonaka, Hiroshi, Gabor Keresztes, Yoshifumi Shinoda, et al. "Complete Genome Sequence of the Dehalorespiring Bacterium Desulfitobacterium hafniense Y51 and Comparison withDehalococcoides ethenogenes 195." Journal of Bacteriology 188, no. 6 (2006): 2262–74. http://dx.doi.org/10.1128/jb.188.6.2262-2274.2006.

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ABSTRACT Desulfitobacterium strains have the ability to dechlorinate halogenated compounds under anaerobic conditions by dehalorespiration. The complete genome of the tetrachloroethene (PCE)-dechlorinating strain Desulfitobacterium hafniense Y51 is a 5,727,534-bp circular chromosome harboring 5,060 predicted protein coding sequences. This genome contains only two reductive dehalogenase genes, a lower number than reported in most other dehalorespiring strains. More than 50 members of the dimethyl sulfoxide reductase superfamily and 30 paralogs of the flavoprotein subunit of the fumarate reducta
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GROGAN, Gideon. "Emergent mechanistic diversity of enzyme-catalysed β-diketone cleavage". Biochemical Journal 388, № 3 (2005): 721–30. http://dx.doi.org/10.1042/bj20042038.

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The enzymatic cleavage of C–C bonds in β-diketones is, comparatively, a little studied biochemical process, but one that has important relevance to human metabolism, bioremediation and preparative biocatalysis. In recent studies, four types of enzymes have come to light that cleave C–C bonds in the β-diketone functionality using different chemical mechanisms. OPH [oxidized poly(vinyl alcohol) hydrolase from Pseudomonas sp. strain VM15C], which cleaves nonane-4,6-dione to butyrate and pentan-2-one is a serine-triad hydrolase. Dke1 (diketone-cleaving enzyme from Acinetobacter johnsonii) is a dio
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Dissertations / Theses on the topic "Fumarase Superfamily"

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Tsai, May Yen Wei. "Structural and functional studies to determine the argininosuccinate lyase/fumarase C superfamily catalytic mechanism." 2007. http://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=742504&T=F.

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Banerjee, Sanchari. "Structural Studies on Bacterial Adenylosuccinate Lyase and Sesbania Mosaic Virus Protease." Thesis, 2014. http://etd.iisc.ac.in/handle/2005/3482.

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The three-dimensional structures of biological macromolecules and molecular assemblies are becoming increasingly important with the changing methodologies of drug discovery. The structures aid in understanding of protein function at the molecular level: be it a macromolecular assembly, a cytosolic enzyme or an intermembrane receptor molecule. X-ray crystallography is the most powerful technique to obtain the three-dimensional structures of such molecules at or near atomic resolution. With such a wide-spread importance, crystallography is an integral part of structural biology and also of the c
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Banerjee, Sanchari. "Structural Studies on Bacterial Adenylosuccinate Lyase and Sesbania Mosaic Virus Protease." Thesis, 2014. http://etd.iisc.ernet.in/2005/3482.

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The three-dimensional structures of biological macromolecules and molecular assemblies are becoming increasingly important with the changing methodologies of drug discovery. The structures aid in understanding of protein function at the molecular level: be it a macromolecular assembly, a cytosolic enzyme or an intermembrane receptor molecule. X-ray crystallography is the most powerful technique to obtain the three-dimensional structures of such molecules at or near atomic resolution. With such a wide-spread importance, crystallography is an integral part of structural biology and also of the c
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