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Academic literature on the topic 'Cataboliti'

Author: Grafiati

Published: 1 April 2023

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Journal articles on the topic "Cataboliti"

1

Kräutler, Bernhard. "Chlorophyll Breakdown – How Chemistry Has Helped to Decipher a Striking Biological Enigma." Synlett 30, no. 03 (October 31, 2018): 263–74. http://dx.doi.org/10.1055/s-0037-1611063.

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How the fall colors arise and how chlorophyll (Chl) breakdown occurs in higher plants has remained enigmatic until three decades ago. Fundamental insights into this fascinating puzzle have been gained, meanwhile, by basic contributions from plant biology and chemistry. This short review is a personal account of key advances from synthetic, mechanistic, and structural chemistry that led to the discovery of the bilin-type Chl catabolites and helped elucidate the metabolic processes that generated them from Chl.1 Introduction2 Discovery and Structure Elucidation of a First Non-Green Chl Catabolite3 Structure Elucidation of Fleetingly Existent Blue-Fluorescent Chl Catabolites4 The Red Chl Catabolite – Key Ring-Opened Tetrapyrrole Accessed by Partial Synthesis5 Synthesis of ‘Primary’ Fluorescent Chl Catabolites by Reduction of Red Chl Catabolite6 Nonfluorescent Chl Catabolites from Isomerization of Fluorescent Chl Catabolites7 Persistent Fluorescent Chl Catabolites and Blue-Luminescent Bananas8 Discovery, Structure Elucidation, and Biological Formation of Dioxobilin-Type Chl Catabolites9 Occurrence, Partial Synthesis, and Structure of Phyllochromobilins, the Colored Bilin-Type Chl Catabolites10 Conclusion and Outlook

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D’Alessandro, C., E. Colombini, G. Pasquariello, G. Sbragia, and A. Cupisti. "Compliance Alla Terapia Dietetica." Giornale di Clinica Nefrologica e Dialisi 22, no. 4 (January 31, 2018): 2–5. http://dx.doi.org/10.33393/gcnd.2010.1235.

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La terapia nutrizionale è uno dei cardini della terapia conservativa dell'Insufficienza Renale Cronica (IRC). È in grado di contrastare segni, sintomi e complicanze dell'insufficienza renale, di procrastinare l'inizio della dialisi e di mantenere lo stato nutrizionale. La dieta deve essere ridotta in proteine perché molte delle tossine e dei cataboliti ritenuti derivano dalle proteine esogene, e perché la restrizione proteica rappresenta una condizione necessaria, anche se non sufficiente, per la contestuale riduzione dell'apporto di sodio e fosforo che contribuisce agli effetti terapeutici. Altra caratteristica fondamentale della terapia dietetica è l'adeguatezza energetica. I due casi descritti rappresentano quello che spesso accade nella pratica clinica nel paziente con IRC cui viene prescritta una dieta ipoproteica, e sottolineano l'importanza del counselling dietetico per la sicurezza e l'efficacia della terapia nutrizionale nel paziente renale con o senza diabete mellito.

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Djapic, Nina. "Chlorophyll catabolism in Prunus serrulata autumnal leaves." Facta universitatis - series: Physics, Chemistry and Technology 10, no. 1 (2012): 21–26. http://dx.doi.org/10.2298/fupct1201021d.

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Chlorophyll catabolism in Prunus serrulata autumnal leaves was investigated. The amount of chlorophyll catabolites accumulated within the same plant species varies with the time of the leaf collection, seasonal climate and developmental stage of the plant. The chlorophyll catabolites found in P. serrulata autumnal leaves presented the tendency of the organism to decrease the level of photodynamically active chlorophyll before the programmed cell death. In the methanol extract several chlorophyll catabolites were identified. The results obtained by liquid - chromatography/mass spectrometry permitted the identification of the chlorophyll catabolites found in P. serrulata autumnal leaves. The analysis done revealed the chlorophyll catabolic pathway found in P. serrulata autumnal leaves.

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Campbell III, John, Gary R. Bender, and Robert E. Marquis. "Barotolerant variant of Streptococcus faecalis with reduced sensitivity to glucose catabolite repression." Canadian Journal of Microbiology 31, no. 7 (July 1, 1985): 644–50. http://dx.doi.org/10.1139/m85-121.

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Physiological characterization of the APR-11 variant of Streptococcus faecalis ATCC 9790 revealed that the variant has reduced sensitivity to glucose catabolite repression. This reduced sensitivity was indicated by the synthesis of enzymes for catabolism of lactose or arginine in cultures growing at 0.1, 40, or 70 MPa in media with levels of glucose highly repressive for the parent strain. Reduced catabolite repression appeared to be due to reduced activity of the glucose-specific, phosphotransferase system in APR-11 cells. Conversion of pyruvate to lactate or to acetate and ethanol did not appear to be altered in the variant. The APR-11 variant produced a greater final yield of biomass than the parent at all pressures tested, and its barotolerance was especially marked in media with low levels of glucose and high levels of lactose in which derepression of the lactose catabolic system was necessary for full growth. Overall, the greater barotolerance of the APR-11 strain appeared to be due to its enhanced capacity for catabolism related to its reduced sensitivity to catabolite repression by glucose.

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Cooper, T. G., R. Rai, and H. S. Yoo. "Requirement of upstream activation sequences for nitrogen catabolite repression of the allantoin system genes in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 12 (December 1989): 5440–44. http://dx.doi.org/10.1128/mcb.9.12.5440-5444.1989.

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Synthesis of the transport systems and enzymes mediating uptake and catabolism of nitrogenous compounds is sensitive to nitrogen catabolite repression. In spite of the widespread occurrence of the control process, little is known about its mechanism. We have previously demonstrated that growth of cells on repressive nitrogen sources results in a dramatic decrease in the steady-state levels of mRNA encoded by the allantoin and arginine catabolic pathway genes and of the transport systems associated with allantoin metabolism. The present study identified the upstream activation sequences in the 5'-flanking regions of the allantoin system genes as the cis-acting sites through which nitrogen catabolite repression is exerted.

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Cooper, T. G., R. Rai, and H. S. Yoo. "Requirement of upstream activation sequences for nitrogen catabolite repression of the allantoin system genes in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 12 (December 1989): 5440–44. http://dx.doi.org/10.1128/mcb.9.12.5440.

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Synthesis of the transport systems and enzymes mediating uptake and catabolism of nitrogenous compounds is sensitive to nitrogen catabolite repression. In spite of the widespread occurrence of the control process, little is known about its mechanism. We have previously demonstrated that growth of cells on repressive nitrogen sources results in a dramatic decrease in the steady-state levels of mRNA encoded by the allantoin and arginine catabolic pathway genes and of the transport systems associated with allantoin metabolism. The present study identified the upstream activation sequences in the 5'-flanking regions of the allantoin system genes as the cis-acting sites through which nitrogen catabolite repression is exerted.

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Bahar, Masoud, John de Majnik, Margaret Wexler, Judith Fry, Philip S. Poole, and Peter J. Murphy. "A Model for the Catabolism of Rhizopine in Rhizobium leguminosarum Involves a Ferredoxin Oxygenase Complex and the Inositol Degradative Pathway." Molecular Plant-Microbe Interactions® 11, no. 11 (November 1998): 1057–68. http://dx.doi.org/10.1094/mpmi.1998.11.11.1057.

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Rhizopines are nodule-specific compounds that confer an intraspecies competitive nodulation advantage to strains that can catabolize them. The rhizopine (3-O-methyl-scyllo-inosamine, 3-O-MSI) catabolic moc gene cluster mocCABRDE(F) in Rhizobium leguminosarum bv. viciae strain 1a is located on the Sym plasmid. MocCABR are homologous to the mocCABR gene products from Sinorhizobium meliloti. MocD and MocE contain motifs corresponding to a TOL-like oxygenase and a [2Fe-2S] Rieske-like ferredoxin, respectively. The mocF gene encodes a ferredoxin reductase that would complete the oxygenase system, but is not essential for rhizopine catabolism. We propose a rhizopine catabolic model whereby MocB transports rhizopine into the cell and MocDE and MocF (or a similar protein elsewhere in the genome), under the regulation of MocR, act in concert to form a ferredoxin oxygenase system that demethylates 3-O-MSI to form scyllo-inosamine (SI). MocA, an NAD(H)-dependent dehydrogenase, and MocC continue the catabolic process. Compounds formed then enter the inositol catabolic pathway.

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Platt, Thomas G., James D. Bever, and Clay Fuqua. "A cooperative virulence plasmid imposes a high fitness cost under conditions that induce pathogenesis." Proceedings of the Royal Society B: Biological Sciences 279, no. 1734 (November 23, 2011): 1691–99. http://dx.doi.org/10.1098/rspb.2011.2002.

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Harbouring a plasmid often imposes a fitness cost on the bacterial host. Motivated by implications for public health, the majority of studies on plasmid cost are focused on elements that impart antibiotic resistance. Plasmids, however, can provide a wide range of ecologically important phenotypes to their bacterial hosts—such as virulence, specialized catabolism and metal resistance. The Agrobacterium tumefaciens tumour-inducing (Ti) plasmid confers both the ability to infect dicotyledonous plants and to catabolize the metabolites that plants produce as a result of being infected. We demonstrate that this virulence and catabolic plasmid imposes a measurable fitness cost on host cells under resource-limiting, but not resource replete, environmental conditions. Additionally, we show that the expression of Ti-plasmid-borne pathogenesis genes necessary to initiate cooperative pathogenesis is extremely costly to the host cell. The benefits of agrobacterial pathogenesis stem from the catabolism of public goods produced by infected host plants. Thus, the virulence-plasmid-dependent costs we demonstrate constitute costs of cooperation typically associated with the ability to garner the benefits of cooperation. Interestingly, genotypes that harbour derived opine catabolic plasmids minimize this trade-off, and are thus able to freeload upon the pathogenesis initiated by other individuals.

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Berthon, Céline, Michaela Fontenay, Selim Corm, Isabelle Briche, Michel Lhermitte, and Bruno Quesnel. "Metabolites of Tryptophan Catabolism Are Elevated in Sera of Patients with Myelodysplastic Syndromes and Inhibit Hematopoietic Progenitor Amplification." Blood 120, no. 21 (November 16, 2012): 3843. http://dx.doi.org/10.1182/blood.v120.21.3843.3843.

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Abstract Abstract 3843 Introduction: Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine, which blocks T-cell activation and induces immunosuppression. Kynurenine itself is converted by downstream enzymes into secondary catabolites that also have toxic effects on T cells. Tryptophan catabolism is elevated in many cancers, including acute myeloid leukemia (AML). However, tryptophan catabolites that are downstream of kynurenine have never been investigated in hematological malignancies. Methods: We evaluated the serum levels of primary and secondary tryptophan catabolites in a cohort of patients with myelodysplastic syndromes (MDS). Sera were isolated from 132 adult MDS patients after informed consent was obtained in accordance with the Helsinki Declaration. The levels of tryptophan, kynurenine, kynurenic acid, 3-hydroxykynurenine, 3-hydroxyanthranilic acid, and anthranilic acid in the sera were quantified using HPLC. For erythroid cell expansion, CD34+ cells were collected and isolated from the mononuclear cell fractions of cytapheresis products from 3 healthy donors and cultured in liquid medium under erythroid conditions with tryptophan catabolites. Results: The MDS patients showed significantly lower levels of tryptophan and higher levels of kynurenine, kynurenic acid, 3-hydroxyanthranilic acid, and anthranilic acid compared with the healthy controls. We also compared the kynurenine and tryptophan levels in the MDS patients with our previous cohort of 112 patients with primary AML. The kynurenine/tryptophan ratios were significantly higher in the MDS patients (median 0.0468 vs. 0.0676). The tryptophan catabolites correlated with cytopenia; higher kynurenine levels were associated with lower hemoglobin levels and higher blast counts and were associated with presence of dysgranulopoiesis. Lower tryptophan levels were found in patients with platelet transfusion dependency. Kynurenic acid levels were higher in patients with dysmegakaryopoiesis. High 3-hydroxyanthranilic and kynurenic acid levels were associated with severe thrombopenia below 20 G/L. IPSS score, cytogenetic, and WHO diagnosis did not associated with any tryptophan catabolite level. The tryptophan catabolites inhibited progenitor expansion during the in vitro culture of hematopoietic cells and reduced the numbers of granulocytes and erythroblasts. Conclusions: Thus, MDS patients are characterized by high tryptophan catabolism resulting in elevated primary and secondary metabolites, which both have inhibitory effects on hematopoiesis. These results suggest that IDO or TDO inhibitors should be investigated in MDS. Disclosures: No relevant conflicts of interest to declare.

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Cunningham, T. S., and T. G. Cooper. "Expression of the DAL80 gene, whose product is homologous to the GATA factors and is a negative regulator of multiple nitrogen catabolic genes in Saccharomyces cerevisiae, is sensitive to nitrogen catabolite repression." Molecular and Cellular Biology 11, no. 12 (December 1991): 6205–15. http://dx.doi.org/10.1128/mcb.11.12.6205-6215.1991.

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We have cloned the negative regulatory gene (DAL80) of the allantoin catabolic pathway, characterized its structure, and determined the physiological conditions that control DAL80 expression and its influence on the expression of nitrogen catabolic genes. Disruption of the DAL80 gene demonstrated that it regulates multiple nitrogen catabolic pathways. Inducer-independent expression was observed for the allantoin pathway genes DAL7 and DUR1,2, as well as the UGA1 gene required for gamma-aminobutyrate catabolism in the disruption mutant. DAL80 transcription was itself highly sensitive to nitrogen catabolite repression (NCR), and its promoter contained 12 sequences homologous to the NCR-sensitive UASNTR. The deduced DAL80 protein structure contains zinc finger and coiled-coil motifs. The DAL80 zinc finger motif possessed high homology to the transcriptional activator proteins required for expression of NCR-sensitive genes in fungi and the yeast GLN3 gene product required for functioning of the NCR-sensitive DAL UASNTR. It was also homologous to the three GATAA-binding proteins reported to be transcriptional activators in avian and mammalian tissues. The latter correlations raise the possibility that both positive and negative regulators of allantoin pathway transcription may bind to similar sequences.

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Dissertations / Theses on the topic "Cataboliti"

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Tongyoo, Narongchai. "Physical and functional analysis of genes from the cam catabolic plasmid encoding probable steps in the catabolism of camphor." Thesis, University College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.397983.

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Chou, Han Ting. "L-Lysine Decarboxylase and Cadaverine Gamma-Glutamylation Pathways in Pseudomonas Aeruginosa PAO1." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/biology_diss/103.

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In comparison to other Pseudomonas, P. aeruginosa grows poorly in L-lysine as a sole source of nutrient while fast growth mutants can be obtained. The proposed catabolic pathway involves lysine decarboxylation to cadaverine and its subsequent degradation through g-glutamylation pathway to d-aminovalerate and glutarate. The lysine decarboxylase A (ldcA) gene, previously identified as a member of the ArgR regulon of L-arginine metabolism, was found essential for L-lysine catabolism. The ldcA gene encodes a decarboxylase which takes L-lysine but not L-arginine as substrate. Contrarily, the ldcA expression was inducible by L-arginine but not by L-lysine. This peculiar arginine control on lysine utilization was also noted from uptake experiments. The lack of lysine-responsive control on lysine catabolism and its tight connection to arginine regulatory network provided an explanation of lysine as poor nutrient for P. aeruginosa. Catabolism of cadaverine, a product from lysine decarboxylation, was investigated and compared to that of putrescine, another diamine of similar biochemical properties that is derived from arginine and ornithine. While the g-glutamylation pathway was first reported in E. coli for putrescine utilization, an expanded version of this pathway was found in P. aeruginosa with redundant enzymes for polyamine degradation. The PauR protein was identified as a transcriptional repressor of genes for the catabolism of putrescine and cadaverine, as well as their corresponding downstream metabolites, g-aminobutyrate (GABA) and d-aminovalerate (AMV). PauR shows distinct dimer configuration after glutaraldehyde crosslinkage, and possible conformational changes could be triggered by the presence of putrescine and cadaverine, but not GABA. A newly identified ABC transport system, encoded by the agtABCD operon, was found important for the uptake of GABA and AMV; and expression of which is controlled by the AgtSR two-component system. The CbrAB two-component system was proposed to regulate the catabolite repression control protein Crc through a small RNA CrcZ. A consensus CbrB recognition sequence was proposed based on the conserved palindromic nucleotide sequence in the upstream activating sequence of the crcZ promoter. Genetic studies indicated utilization of arginine, lysine and diamines (but not histidine, GABA and AMV) might be under CbrAB regulation through the CbrAB/CrcZ/Crc system in P. aeruginosa.

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Madhushani, W. K. Anjana. "Multiple regulatory inputs for hierarchical control of phenol catabolism by Pseudomonas putida." Doctoral thesis, Umeå universitet, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet), 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-106878.

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Metabolically versatile bacteria have evolved diverse strategies to adapt to different environmental niches and respond to fluctuating physico-chemical parameters. In order to survive in soil and water habitats, they employ specific and global regulatory circuits to integrate external and internal signals to counteract stress and optimise their energy status. One strategic endurance mechanism is the ability to choose the most energetically favourable carbon source amongst a number on offer. Pseudomonas putida strains possess large genomes that underlie much of their ability to use diverse carbon sources as growth substrates. Their metabolic potential is frequently expanded by possession of catabolic plasmids to include the ability to grow at the expense of seemingly obnoxious carbon sources such as phenols. However, this ability comes with a metabolic price tag. Carbon source repression is one of the main regulatory networks employed to subvert use of these expensive pathways in favour of alternative sources that provide a higher metabolic gain. This thesis identifies some of the key regulatory elements and factors used by P. putida to supress expression of plasmid-encoded enzymes for degradation of phenols until they are beneficial. I first present evidence for a newly identified DNA and RNA motif within the regulatory region of the gene encoding the master regulator of phenol catabolism – DmpR. The former of these motifs functions to decrease the number of transcripts originating from the dmpR promoter, while the latter mediates a regulatory checkpoint for translational repression by Crc – the carbon repression control protein of P. putida. The ability of Crc to form repressive riboprotein complexes with RNA is shown to be dependent on the RNA chaperone protein Hfq – a co-partnership demonstrated to be required for many previously identified Crc-targets implicated in hierarchical assimilation of different carbon sources in P. putida. Finally, I present evidence for a model in which Crc and Hfq co-target multiple RNA motifs to bring about a two-tiered regulation to subvert catabolism of phenols in the face of preferred substrates – one at the level of the regulator DmpR and another at the level of translation of the catabolic enzymes.

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Dantas, Hugo Miguel Campelo. "Engineering hexuronic acid catabolism." Master's thesis, Universidade de Aveiro, 2013. http://hdl.handle.net/10773/11776.

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Metabolic engineering is an emerging field targeted to the improvement of pathways for the production of high-value compounds. Citrus peel is produced at an estimated 15,000,000 t per year worldwide and its disposal causes environmental problems. The main constituent of citrus peel is D-galacturonic acid. The aim of this project is to convert D-galacturonic acid to useful chemicals using genetically engineered moulds. Aspergillus niger was chosen since it is naturally a good consumer of D-galacturonic acid and produces the enzymes required for citrus peel hydrolysis. In the present study, engineered Aspergillus niger strains were used where (i) the gaaB coding for L-galactonate dehydrogenase was deleted (ΔgaaB) and (ii) the gaaB was deleted and the gaaA coding for D-galacturonate reductase was overexpressed (ΔgaaB-gaaA). These strains were used for solid-state and submerged state fermentation to convert orange peel to L-galactonate in a consolidate process. The strains were able to convert up to 87 % of Dgalacturonic acid to L-galactonate by solid-state fermentation. Another pathway that was studied was the eukaryotic D-Glucuronic acid pathway. In this pathway is a ddecarboxylase that converts 3-keto-L-gulonate to L-xylulose. The reaction is poorly characterized and the gene not known. It was tried to assay this activity in a coupled enzyme assay. In this assay Lgulonic acid is the initial substrate, an NAD-dependent L-gulonate-3-dehydrogenase (GDH) that produces the substrate for the decarboxylase. Lxylulose reductase is then detected by an NADPH-dependent L-xylulose reductase from Aspergillus niger (lxrA). To follow the reaction NADPH was monitored at 340 nm. To avoid the interference of NADH that also absorbs at 340 nm Thio-NAD+ was used for the dehydrogenase. Active GDH and lxrA were prepared and the assay tested with ammonium sulfate precipitates from bovine liver extract. A 3-keto-L-gulonate decarboxylase activity could not be detected.
A engenharia metabólica é uma área emergente que visa o aperfeiçoamento de vias metabólicas para produção de compostos valiosos. A produção mundial de casca de frutos cítricos é estimada em 15,000,000 de toneladas por ano, e o seu descarte causa problemas ambientais. O principal constituinte da casca de frutos cítricos é o ácido D-galacturónico. O objetivo deste projeto é converter o ácido D-galacturónico noutros químicos proveitosos, utilizando para tal bolores geneticamente modificados. Aspergillus niger foi escolhido por ser naturalmente um bom consumidor do ácido Dgalacturónico e produtor das enzimas necessárias à hidrólise de casca de frutos cítricos. No presente trabalho, estirpes de Aspergillus niger foram geneticamente modificados onde (i) o gene gaaB que codifica para a L-galactonato desidratase foi deletado (ΔgaaB) e (ii) o gene gaaB foi deletado e o gene gaaA que codifica para a D-galacturonato reductase se encontrava sobreexpresso (ΔgaaB-gaaA). Estas estirpes foram utilizadas para fermentação submersa e em estado sólido para converter casca de laranja em L-galactonato num processo consolidado. As estirpes foram capazes de converter, até 87 %, de ácido D-galacturónico em L-galactonato por fermentação em estado sólido. Outra via metabólica estudada foi a via eucariota do ácido glucurónico. Nesta via metabólica é uma descarboxilase que converte o 3-ceto-L-gulonato em Lxilulose. A reação ainda não está claramente caracterizada e o gene não é conhecido. Um teste enzimático acoplado foi realizado de forma a testar a sua atividade. Neste ensaio o ácido L-gulónico é o substrato inicial, uma Lgulonato- 3-desidrogenase NAD-dependente (GDH) que produz o substrato para a descarboxilase. A L-xilulose reductase é então detetada por uma Lxilulose reductase NADPH-dependente de Aspergillus niger (lxrA). Para seguir a reação, o NADPH foi monitorizado a 340 nm. Para evitar a interferência do NADH que também absorve a 340 nm, Tio-NAD+ foi usado para a desidrogenase. GDH e lxrA ativas foram preparadas e o ensaio testado com precipitados sulfato de amónio de extrato de fígado bovino. A atividade da 3-ceto-Lgulonato descarboxilase não foi detetada.

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Stankiewicz, Margaret J. "Oxidative catabolism of tetrahydropterins." Thesis, Aston University, 1989. http://publications.aston.ac.uk/12531/.

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Mixed labelled folic acid was administerd to rats. Exposure to N2O was used to give an insight into the major route of scission within the monoglutamate pool, results suggest that THF formed during transport from the gut lumen to the plasma is the major route of scission within the gut. Peroxides in corn oil and arising as a result of lipid peroxidation and autoxidation increase catabolism of the monoglutamate pool and decrease incorporation of administered folates into the polyglutamate pool. It is suggested that peroxides may oxidise B12 resulting in inhibition of methionine synthetase, this results in diminished polyglutamation and increased urinary excretion of 5 CH3THF. Fats undergo peroxidation within tissues, the resulting peroxides increase catabolism of the polyglutamate pool. It is suggested that the NBT assay may reflect polyglutamate breakdown. Antioxidants such as vitamin E (and DES) decrease catabolism of the monoglutamate pool. Administration of DES resulted in changes similar to those observed during malignancy, it is suggested that these changes may precede the onset of tumour development. Vitamin E elevates brain DHPR activity. Since lowered DHPR levels and disturbed THB metabolism have been observed in aging and Down's syndrome it is proposed that vitamin E therapy may prove beneficial in situations where oxidative stress is increased. Brain DHPR activity was increased on administration of peroxides suggesting that in situations of oxidative stress (which may result in increased catabolism of THB) the salvage pathway may be stimulated and loss of THB minimised. N2O exposure had no effect on THB metabolism suggesting that the stimulatory role of 5 CH3THF is due to its role as a methyl donor.

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Crabbe, T. B. "Studies on the adenylate cyclase and HMGCoA reductase of the yeast Saccharomyces cerevisiae." Thesis, University of Liverpool, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233812.

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Birch, D. J. "Carbon catabolite repression in the yeast Saccharomyces cerevisiae." Thesis, University of Liverpool, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.372682.

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Jones, Melissa Kaye. "Inositol catabolism in Drosophila melanogaster." Thesis, California State University, Long Beach, 2014. http://pqdtopen.proquest.com/#viewpdf?dispub=1527384.

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myo-Inositoloxygenase (MIOX) catalyzes the first step in myo-inositol catabolism. MIOX has not been annotated in Drosophila melanogaster, but the protein encoded by the CG6910 gene is similar to the mouse MIOX protein. CG6910 "knocked-down" expression was explored using RNAi. "Knock-down" flies did not survive on inositol defined media, indicating that CG6910 encodes MIOX. Survival of these flies on sucrose defined media suggest that MIOX is not essential for development. Biochemical assays demonstrated that D. melanogaster has MIOX activity. Computational analyses revealed potential miRNA sites, and that a number of essential components are conserved. MIOX genes found in other drosopholids are highly similar to D. melanogaster MIOX, and analyses of the syntenic regions concur with established evolution. Western blot analyses showed differential expression amongst D. melanogaster from different geographic locations and between species. These studies may contribute to understanding the role of inositol catabolism in fruit fly development and diabetes.

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Brummett, Adam Eugene. "Enzymology of microbial dimethylsulfoniopropionate catabolism." Diss., University of Iowa, 2017. https://ir.uiowa.edu/etd/5430.

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The biosynthesis of DMSP by phytoplankton and algae has wide ranging impact on marine organisms. Release of DMSP and uptake by marine bacteria leads to the eventual catabolism of this osmolyte. Enzymatic breakdown of DMSP leads to acrylate and volatile DMS production, which is fluxed into the atmosphere. When DMS enters the atmosphere it undergoes oxidation, acting as nucleation sites for water. The nucleation of water, and the subsequent cloud formation increases the albedo and reflects solar radiation. Global climate has therefore been hypothesized to be dependent upon DMSP breakdown to DMS. The enzymatic production of acrylate is also of interest for industrial applications. Only six enzymes are known to act as a DMSP-lyase, causing the production of DMS. These enzymes are still being discovered, and until recently there was very limited analysis of the biochemical requirements for catalysis. The work presented here investigates these requirements and the structural properties that permit the elimination reaction yielding DMS.

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Kandasamy, Dineshkumar. "Study on yeast enzymes Urc1p and Urc4p in a novel uracil catabolism pathway (URC)." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-185013.

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Purine and pyrimidine bases are the central precursors of DNA and RNA and theirintracellular concentration is balanced by three pathways- de novo, salvage and catabolicpathways. Uracil catabolism pathway has been found in several bacteria and in some fungi(including yeast). Seven genes, URC1-7 have been found to be involved in this novelpathway. There are two “unknown genes” in the yeast Lachancea (Saccharomyces) kluyveri,namelyURC1 and URC4, which play a central role in this pathway and their exact functionremains a mystery.In this project, two S. kluyveri genes, URC1&URC4, were over-expressed in the bacterialsystem and successfully purified. Our preliminary functional assay showed that uridinemonophosphate (UMP) is a likely substrate for Urc1p at pH7, 25ºC. It was shown clearly thatboth uracil and uridine were not the substrate for Urc1p. We tried to phosphorylatechemically synthesized ribosylurea using Drosophila melanogaster deoxyribonucleosidekinase and compared the activity between phosphorylated and non- phosphorylated RU atdifferent conditions. Phosphorylated ribosylurea seemed to be a likely substrate for Urc4p atpH7, 37ºC. Keywords: Uridine monophosphate (UMP), ribosylurea (RU), uracil catabolism.

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Books on the topic "Cataboliti"

1

Suzuki, Koichi, and Judith S. Bond, eds. Intracellular Protein Catabolism. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0335-0.

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Revhaug, Arthur, ed. Acute Catabolic State. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-48801-6.

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1950-, Revhaug A., ed. Acute catabolic state. Berlin: Springer, 1996.

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Rojas, A. E. Carvajal de. Carbon catabolism in streptomyces venezuelae. Manchester: UMIST, 1995.

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McVitty, Rosalind Shirley. In vitro studies of folate catabolism. [S.l: The Author], 1997.

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Beck, Susan Anne. Catabolic factors in tumour-induced cachexia. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1989.

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Floderus, Eugenie. Aminopeptidases and arginine catabolism in oral streptococci. [Stockholm: Karolinska Institute, Dept. of Oral Microbiology], 1990.

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Floderus, Eugenie. Aminopeptidases and arginine catabolism in oral straptococci. Stockholm: Kongl. Carolinska Medico Chirurgiska Institutet, 1990.

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International Symposium on Intracellular Protein Catabolism (6th 1986 Büchenberg (Magdeburg, Germany)). Intracellular protein catabolism: Abstracts of the 6th symposium. Edited by Aurich H, Kirschke Heidrun, Wiederanders Bernd, Proteolysis Group in Halle, and Biochemische Gesellschaft der Deutschen Demokratischen Republik. Halle, Saale: Martin-Luther-Universität Halle-Wittenberg, 1986.

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Engel, Norbert G. Chlorophyll catabolism in algae and higher plants: A chemical approach. Freiburg (Schweiz): Department of Chemistry, Universität Freiburg (Schwiez), 2001.

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Book chapters on the topic "Cataboliti"

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Itoh, Yoshifumi, Takayuki Nishijyo, and Yuji Nakada. "Histidine Catabolism and Catabolite Regulation." In Pseudomonas, 371–95. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6097-7_13.

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Gooch, Jan W. "Catabolite Activation." In Encyclopedic Dictionary of Polymers, 880. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13328.

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Gooch, Jan W. "Catabolite Repression." In Encyclopedic Dictionary of Polymers, 880. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13329.

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Peretó, Juli. "Catabolism." In Encyclopedia of Astrobiology, 397. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_244.

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Abbasi, Adeel, Francis DeRoos, José Artur Paiva, J. M. Pereira, Brian G. Harbrecht, Donald P. Levine, Patricia D. Brown, et al. "Catabolism." In Encyclopedia of Intensive Care Medicine, 504. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-00418-6_1317.

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Kalmar, Jayne M., Brigid M. Lynch, Christine M. Friedenreich, Lee W. Jones, A. N. Bosch, Alessandro Blandino, Elisabetta Toso, et al. "Catabolism." In Encyclopedia of Exercise Medicine in Health and Disease, 176. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2203.

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Peretó, Juli. "Catabolism." In Encyclopedia of Astrobiology, 262. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_244.

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Gooch, Jan W. "Catabolism." In Encyclopedic Dictionary of Polymers, 880. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13327.

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Peretó, Juli. "Catabolism." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_244-2.

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Kalmar, Jayne M., Brigid M. Lynch, Christine M. Friedenreich, Lee W. Jones, A. N. Bosch, Alessandro Blandino, Elisabetta Toso, et al. "Catabolic." In Encyclopedia of Exercise Medicine in Health and Disease, 176. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2202.

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Conference papers on the topic "Cataboliti"

1

Sugimoto, Megumi, Eijiro Maeda, and Toshiro Ohashi. "Modulation of Traction Forces of Isolated Tenocytes by Substrate Stiffness." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53818.

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Mechanical stimuli are important to maintenance of homeostasis in many connective tissues including tendons and ligaments. Application of cyclic tensile loading in a physiological range has been demonstrated to possess anabolic and anti-catabolic effects on tenocyte metabolism [1,2], whereas the loading falling outside the range induced upregulations of tenocyte catabolism [3]. One of mechanotransduction signaling pathways of tenocytes is mediated via cytoskeletal elements [4]. It has been demonstrated that cytoskeletal tension within tenocytes regulated anabolic and catabolic gene expressions in a reciprocal manner [4]. However, the precise relationship between cell metabolism and internal tension within cytoskeletons has not been studied.

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Smith, Lynelle P., Lucas M. Harrell, Jessica L. Christenson, Benjamin Bitler, Jill Slansky, and Jennifer K. Richer. "Abstract 5137: Tryptophan catabolism in ovarian cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5137.

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Armstrong, AD, A. Malur, AG Malur, BP Barna, MS Kavuru, and MJ Thomassen. "PPARγ Deficiency in Alveolar Macrophages Disrupts Surfactant Catabolism." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a6281.

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Amba, Vineeth. "Catabolism of Indole-3-Carbil in Arabidopsis thaliana." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1046514.

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Riesenberg, Brian, Elizabeth Hunt, Megan Tennant, Katie Hurst, Alex Andrews, Lee Leddy, David Neskey, et al. "1044 Proteasome mediated protein catabolism fuels antitumor immunity." In SITC 37th Annual Meeting (SITC 2022) Abstracts. BMJ Publishing Group Ltd, 2022. http://dx.doi.org/10.1136/jitc-2022-sitc2022.1044.

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Marozkina, Nadzeya, Talissa Altes, Eduardo de Lange, Douglas Curran-Everett, Denise Thompson-Batt, Suzy A. Comhair, Serpil C. Erzurum, W. G. Teague, and Benjamin Gaston. "S-Nitrosoglutathione (GSNO) Catabolic Enzymes In Severe Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2566.

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Maidhof, Robert, Neena Rajan, and Nadeen O. Chahine. "Effect of Inflammation on the Osmotic Response of Nucleus Pulposus Cells." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80358.

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Intervertebral disc (IVD) degeneration is accompanied by elevated levels of pro-inflammatory cytokines, particularly IL-1β and TNF-α [1]. Disc cells from the nucleus pulposus (NPs) respond to cytokine stimulation with increased catabolic breakdown of the tissue, resulting in a positive feedback of disc integrity loss and further inflammation [2]. Previous studies by our group have examined the response of NP cells to Toll-Like Receptor-4 (TLR-4) activation through stimulation with lipopolysaccharide (LPS). TLR-4 is a pattern recognition receptor that is activated in innate immunity and by polysaccharide fragments from degenerated proteoglycans. TLR-4 activation by LPS results in stimulation of multiple cytokines by NP cells [3]. Moreover, we have shown that in vivo LPS injection results in catabolic changes in the IVD, including matrix breakdown, decrease in biomechanical properties and loss of disc height [4]. However, the specific cellular mechanisms for these catabolic changes remain to be elucidated.

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Malur, Anagha, Anna D. Baker, Barbara P. Barna, Shobha Ghosh, Mani S. Kavuru, Achut G. Malur, and Mary J. Thomassen. "Targeted PPAR³ Deficiency In Alveolar Macrophages Disrupts Surfactant Catabolism." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2463.

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BIRBIR, Meral, and Pinar CAGLAYAN. "A Review on Catabolic Activity of Microorganisms in Leather Industry." In The 7th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2018. http://dx.doi.org/10.24264/icams-2018.vi.3.

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Kruglova, M. N., Y. A. Chugunova, A. A. Samkov, N. N. Volchenko, and A. A. Khudokormov. "Correlation between the diversity of xenobiotic catabolism genes in Rhodococcus and phytotoxicity of imidazolinone and organophosphate herbicide biotransformation products." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.131.

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Rhodococcus strains with a wide spectrum of catabolic genes, have provided a more marked reduction of toxicity of imidazolinone. In the case of glyphosate, the opposite strain-specific pattern is found.

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Reports on the topic "Cataboliti"

1

Lessie, T. G. Genomic plasticity and catabolic potential of Pseudomonas cepacia. Office of Scientific and Technical Information (OSTI), April 1996. http://dx.doi.org/10.2172/224251.

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Stutzenberger, Fred. Regulation of Catabolic Enzyme Biosynthesis in Thermomonospora curvata. Fort Belvoir, VA: Defense Technical Information Center, March 1988. http://dx.doi.org/10.21236/ada197244.

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Daniel Gage. Molecular characterization of catabolite repression by succinate in the nodulating bacterium Sinorhizobium meliloti. Office of Scientific and Technical Information (OSTI), September 2006. http://dx.doi.org/10.2172/891983.

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Parke, D., and L. N. Ornston. Organization and control of genes encoding catabolic enzymes in Rhizobiaceae. Office of Scientific and Technical Information (OSTI), March 1993. http://dx.doi.org/10.2172/6754773.

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Wilmore, Douglas W. A Program for the Study of Skeletal Muscle Catabolism Following Physical Trauma. Fort Belvoir, VA: Defense Technical Information Center, November 1989. http://dx.doi.org/10.21236/ada216569.

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Parke, D., and L. N. Ornston. Organization and control of genes encoding catabolic enzymes in Rhizobiaceae. Final report. Office of Scientific and Technical Information (OSTI), December 1997. http://dx.doi.org/10.2172/763956.

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Parke, D., and L. N. Ornston. Organization and control of genes encoding catabolic enzymes in Rhizobiaceae. Progress report, March 1993. Office of Scientific and Technical Information (OSTI), March 1993. http://dx.doi.org/10.2172/10134071.

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Porter, Carl W. Activation of Polymine Catabolism as a Novel Strategy for Treating and/or Preventing Human Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada455145.

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Yoon, Jong M., Jerald L. Schnoor, Benoit Van Aken, Laura B. Brentner, Sachiyo Tanaka, and Brittany Flokstra. Identification of Metabolic Routes and Catabolic Enzymes Involved in Phytoremediation of the Nitro- Substituted Explosives TNT, RDX, and HMX. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada476298.

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Stern, David, and Gadi Schuster. Manipulating Chloroplast Gene Expression: A Genetic and Mechanistic Analysis of Processes that Control RNA Stability. United States Department of Agriculture, June 2004. http://dx.doi.org/10.32747/2004.7586541.bard.

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New potential for engineering chloroplasts to express novel traits has stimulated research into relevant techniques and genetic processes, including plastid transformation and gene regulation. This BARD-funded research dealt with the mechanisms that influence chloroplast RNA accumulation, and thus gene expression. Previous work on cpRNA catabolism has elucidated a pathway initiated by endonucleolytic cleavage, followed by polyadenylation and exonucleolytic degradation. A major player in this process is the nucleus-encoded exoribo-nuclease/polymerase polynucleotide phosphorylase (PNPase). Biochemical characterization of PNPase has revealed a modular structure that controls its RNA synthesis and degradation activities, which in turn are responsive to the phosphate (P) concentration. During the funding period, new insights emerged into the molecular mechanism of RNA metabolism in the chloroplast and cyanobacteria, suggesting strategies for improving agriculturally-important plants or plants with novel introduced traits.

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