Relevant bibliographies by topics / Thiamin pyrophosphate

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Academic literature on the topic 'Thiamin pyrophosphate'

Author: Grafiati
Published: 4 June 2021
Last updated: 27 January 2023

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Journal articles on the topic "Thiamin pyrophosphate"

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Strobbe, Simon, Jana Verstraete, Christophe Stove, and Dominique Van Der Straeten. "Metabolic engineering provides insight into the regulation of thiamin biosynthesis in plants." Plant Physiology 186, no. 4 (2021): 1832–47. http://dx.doi.org/10.1093/plphys/kiab198.

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Abstract Thiamin (or thiamine) is a water-soluble B-vitamin (B1), which is required, in the form of thiamin pyrophosphate, as an essential cofactor in crucial carbon metabolism reactions in all forms of life. To ensure adequate metabolic functioning, humans rely on a sufficient dietary supply of thiamin. Increasing thiamin levels in plants via metabolic engineering is a powerful strategy to alleviate vitamin B1 malnutrition and thus improve global human health. These engineering strategies rely on comprehensive knowledge of plant thiamin metabolism and its regulation. Here, multiple metabolic
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Hironaka, R., and G. C. Kozub. "Thiamin supplementation of beef cattle diets." Canadian Journal of Animal Science 71, no. 4 (1991): 1261–64. http://dx.doi.org/10.4141/cjas91-151.

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Thiamin supplementation at 10 mg kg−1 of barley-based all-concentrate diets fed to slow- or fast-gaining 250-kg steers or of diets with 10.9 or 11.8% crude protein did not increase rate of gain. The thiamin pyrophosphate (TPP) effect was lower in supplemented than in non-supplemented steers (P < 0.05), indicating that supplementation increased the thiamin level in the blood. Key words: Steers, thiamin, TPP effect
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Lonsdale, Derrick. "Dietary intake and thiamin pyrophosphate response." American Journal of Clinical Nutrition 55, no. 1 (1992): 139. http://dx.doi.org/10.1093/ajcn/55.1.139.

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Nichols, H. K., and T. K. Basu. "Thiamin status of the elderly: dietary intake and thiamin pyrophosphate response." Journal of the American College of Nutrition 13, no. 1 (1994): 57–61. http://dx.doi.org/10.1080/07315724.1994.10718372.

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Subramanya, Sandeep B., Veedamali S. Subramanian, V. Thillai Sekar, and Hamid M. Said. "Thiamin uptake by pancreatic acinar cells: effect of chronic alcohol feeding/exposure." American Journal of Physiology-Gastrointestinal and Liver Physiology 301, no. 5 (2011): G896—G904. http://dx.doi.org/10.1152/ajpgi.00308.2011.

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Thiamin is important for normal function of pancreatic acinar cells, but little is known about its mechanism of uptake and about the effect of chronic alcohol use on the process. We addressed these issues using freshly isolated rat primary and rat-derived cultured AR42J pancreatic acinar cells as models. Results showed thiamin uptake by both primary and cultured AR42J pancreatic acinar cells to be via a specific carrier-mediated mechanism and that both of the thiamin transporters 1 and 2 (THTR-1 and THTR-2) are expressed in these cells. Chronic alcohol feeding of rats was found to lead to a si
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Sabui, Subrata, Veedamali S. Subramanian, Rubina Kapadia, and Hamid M. Said. "Adaptive regulation of pancreatic acinar mitochondrial thiamin pyrophosphate uptake process: possible involvement of epigenetic mechanism(s)." American Journal of Physiology-Gastrointestinal and Liver Physiology 313, no. 5 (2017): G448—G455. http://dx.doi.org/10.1152/ajpgi.00192.2017.

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The essentiality of thiamin stems from its roles as a cofactor [mainly in the form of thiamin pyrophosphate (TPP)] in critical metabolic reactions including oxidative energy metabolism and reduction of cellular oxidative stress. Like other mammalian cells, pancreatic acinar cells (PAC) obtain thiamin from their surroundings and convert it to TPP; mitochondria then take up TPP by a carrier-mediated process that involves the mitochondrial TPP (MTPP) transporter (MTPPT; product of SLC25A19 gene). Previous studies have characterized different physiological/biological aspects of the MTPP uptake pro
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Shigeoka, S., and Y. Nakano. "The effect of thiamin on the activation of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in Euglena gracilis." Biochemical Journal 292, no. 2 (1993): 463–67. http://dx.doi.org/10.1042/bj2920463.

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The effect of thiamin on thiamin pyrophosphate-dependent 2-oxoglutarate (2-OG) decarboxylase activity in Euglena gracilis was investigated. The total activity of 2-OG decarboxylase in thiamin-sufficient cells in 3 times that in thiamin-deficient cells. The addition of thiamin to thiamin-deficient cells causes the total enzyme and holoenzyme activities to increase and reach similar levels to that in thiamin-sufficient cells. Cycloheximide and chloramphenicol, inhibitors of protein synthesis, have no effect on the total enzyme activity. Immunochemical titration and determination of 2-OG decarbox
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Melnick, Jonathan S., K. Ingrid Sprinz, Jason J. Reddick, Cynthia Kinsland, and Tadhg P. Begley. "An efficient enzymatic synthesis of thiamin pyrophosphate." Bioorganic & Medicinal Chemistry Letters 13, no. 22 (2003): 4139–41. http://dx.doi.org/10.1016/j.bmcl.2003.07.026.

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Lonsdale, Derrick. "Three Case Reports to Illustrate Clinical Applications in the Use of Erythrocyte Transketolase." Evidence-Based Complementary and Alternative Medicine 4, no. 2 (2007): 247–50. http://dx.doi.org/10.1093/ecam/nel089.

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Non-caloric nutrients (NCN) are extremely numerous and it is more than obvious that they work in a team relationship. These vitally important interactions are, for the most part, poorly understood. These brief case reports illustrate this in the therapeutic use of thiamin in a clinical setting. The initially abnormal erythrocyte transketolase activity (TKA) and/or the thiamin pyrophosphate effect (TPPE), indicating intracellular cofactor deficiency, usually improves with thiamin administration. Biochemical correction of the abnormality is, however, invariably dependent on the provision of othe
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HOLZER, H., and C. GUBLER. "Thiamin Pyrophosphate: Catalytic Mechanism, Role in Protein Turnover." Journal of Nutritional Science and Vitaminology 38, Special (1992): 287–91. http://dx.doi.org/10.3177/jnsv.38.special_287.

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Dissertations / Theses on the topic "Thiamin pyrophosphate"

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Iqbal, Amjid. "Synthesis and evaluation of thiamin diphosphate analogues." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.607797.

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Thomson, Andrew Campbell. "Macrocyclic thiazolium salts as models for thiamin pyrophosphate-dependent enzymes." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614841.

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Tunc, Meral. "The molecular genetic regulation of thiamin biosynthesis in plants." abstract and full text PDF (free order & download UNR users only), 2008. http://0-gateway.proquest.com.innopac.library.unr.edu/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3307578.

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Nguyen, Trinh Doan Thi. "Thiamine pyrophosphate riboswitches in Chlamydomonas reinhardtii : understanding their nature to generate tools for biotechnology." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708526.

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Erixon, Karl Magnus. "Synthesis and evaluation of thiamine pyrophosphate analogues." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611168.

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Aljuaid, Bandar. "Identification and analysis of Arabidopsis thiamine pyrophosphate transporters." Thesis, University of Essex, 2017. http://repository.essex.ac.uk/19430/.

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Thiamine pyrophosphate (TPP) serves as a cofactor in universal metabolic pathways, including glycolysis, the pentose phosphate pathway (PPP) and the tricarboxylic acid cycle; moreover, it is essential for the proper functioning of all organisms. Recently, several steps of the plant thiamine biosynthetic pathway have been characterised, and a mechanism of feedback regulation for thiamine biosynthesis via riboswitching has been unravelled. In plants, thiamine is made in the chloroplasts and then transferred to the cytosol to generate the active form of thiamine, TPP. The mitochondria and chlorop
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Chen, Yang-Ting(Percival Yang Ting). "Structural insights into conformationally-gated reactions catalyzed by thiamine pyrophosphate-dependent enzymes." Thesis, Massachusetts Institute of Technology, 2019. https://hdl.handle.net/1721.1/122450.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2019<br>Vita. Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>Thiamine pyrophosphate (TPP)-dependent enzymes utilize TPP as a biological carbanion to initiate reactions on substrates with carbonyl carbon(s), such as pyruvate and 2-oxoglutarate, two central metabolites. This thesis presents structural analyses of three TPP-dependent enzymes. Most interestingly, each mechanism of three proteins studied contains a gated step that is drastically accelerated by 3-5 orders of magnitudes t
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Sopaci, Saziye Betul. "Microorganism Mediated Stereoselective Bio-oxidation And Bio-hydrogenation Reactions And Thiamine Pyrophosphate Dependent Enzyme Catalyzed Enantioselective Acyloin Reactions." Phd thesis, METU, 2009. http://etd.lib.metu.edu.tr/upload/2/12610516/index.pdf.

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In this study various microbial and enzymatic methods developed for enantioselective acyloin synthesis for preparation of some pharmaceutically important intermediates. By performing Aspergillus flavus (MAM 200120) mediated biotransformation, enantioselective bio-oxidation of meso-hydrobenzoin was achieved with a high ee value (76%). Racemic form of hydrobenzoin was also employed for the same bio-oxidation process and this bioconversion was resulted in accumulation of meso form (&gt<br>90% yield) confirming the suggested mechanism of oxidation-reduction sequence of hydrobenzoin. Wieland-Miesch
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Chabrière, Eric. "Etude structurale de la pyruvate:ferrédoxine oxydoréductase de Desulfovibrio africanus par cristallographie des rayons X : vers une meilleure connaissance du mécanisme réactionnel du cofacteur thiamine pyrophosphate." Université Joseph Fourier (Grenoble), 1999. http://www.theses.fr/1999GRE10094.

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Les pyruvate : ferredoxine oxydoreductases (pfor) sont des enzymes qui, chez la plupart des organismes anaerobes, catalysent la decarboxylation oxydative du pyruvate en utilisant le cofacteur thiamine pyrophosphate, suivant la reaction : pyruvate + coa-sh acetyl-coa + co 2 + 2e + h + dans cette these, nous expliquons comment nous avons resolu, par cristallographie, la premiere structure tridimensionnelle d'une pfor, celle de desulfovibrio africanus, une bacterie sulfato-reductrice anaerobe. Nous montrons aussi comment l'analyse de cette structure a apporte une meilleure comprehension du mecani
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Garcia, Assuero Faria. "Thi1, uma proteína envolvida na síntese de tiamina em Arabidopsis thaliana: análises estruturais do mutante Thi1 (A140V)." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-04102011-161654/.

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A forma ativa da vitamina B1, tiamina pirofosfato (TPP), é um cofator indispensável para certas enzimas que atuam no metabolismo de carboidratos e aminoácidos. Sua biossíntese se dá pela formação independente de suas partes componentes pirimidina e tiazol. Em procariotos a via de síntese para vitamina B1 já foi esclarecida, entretanto em eucariotos ainda existem ainda algumas lacunas a serem preenchidas. Em Arabidopsis thaliana a proteína Thi1 é possivelmente a responsável pela síntese do motivo tiazólico, uma vez que um composto relacionado a TPP foi encontrado em sua estrutura. Neste trabalh
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Books on the topic "Thiamin pyrophosphate"

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Alfred, Schellenberger, Schowen Richard L, Martin-Luther-Universität Halle-Wittenberg, and Biochemische Gesellschaft der Deutschen Demokratischen Republik., eds. Thiamin pyrophosphate biochemistry. CRC Press, 1988.

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International Meeting on the Function of Thiamin Diphosphate Enzymes (1990 Blaubeuren, Germany). Biochemistry and physiology of thiamin diphosphate enzymes: Proceedings of the International Meeting on the Function of Thiamin Diphosphate Enzymes, held in Blaubeuren, October 1990. VCH, 1991.

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Dünkelmann, Pascal. Entwicklung eines Donor/Akzeptor-Konzeptes für die asymmetrische Synthese unsymmetrischer Benzoine mit Hilfe ThDP-abhängiger Enzyme. Forschungszentrum Jülich GmbH, Zentralbibliothek, 2005.

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(Editor), Frank Jordan, and Mulchand S. Patel (Editor), eds. Thiamine: Catalytic Mechanisms in Normal and Disease States (Oxidative Stress and Disease). CRC, 2003.

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Patel, Mulchand S., and Frank Jordan. Thiamine: Catalytic Mechanisms in Normal and Disease States. Taylor & Francis Group, 2003.

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Patel, Mulchand S., and Frank Jordan. Thiamine: Catalytic Mechanisms in Normal and Disease States. Taylor & Francis Group, 2003.

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Frank, Jordan, and Patel Mulchand S, eds. Thiamine: Catalytic mechanisms in normal and disease states. Marcel Dekker, 2004.

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Patel, Mulchand S., and Frank Jordan. Thiamine: Catalytic Mechanisms in Normal and Disease States. Taylor & Francis Group, 2003.

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Patel, Mulchand S., and Frank Jordan. Thiamine: Catalytic Mechanisms in Normal and Disease States. Taylor & Francis Group, 2003.

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Patel, Mulchand S., and Frank Jordan. Thiamine: Catalytic Mechanisms in Normal and Disease States. Taylor & Francis Group, 2003.

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Book chapters on the topic "Thiamin pyrophosphate"

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Foulon, Veerle, Minne Casteels, Guy P. Mannaerts, Bruce D. Gelb, and Paul P. VanVeldhoven. "Thiamine Pyrophosphate: an essential Cofactor in the Mammalian Metabolism of 3-methyl-branched Fatty Acids." In Advances in Experimental Medicine and Biology. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9072-3_39.

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"Thiamin Pyrophosphate." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_16923.

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Casteels, Minne, Veerle Foulon, Guy Mannaerts, and Paul Van Veldhoven. "Thiamine Pyrophosphate." In Thiamine. CRC Press, 2003. http://dx.doi.org/10.1201/9780203913420.ch29.

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"Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea." In Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, edited by Scott B. Brown, John D. Fitzsimons, Vince P. Palace, and Lenore Vandenbyllaardt. American Fisheries Society, 1998. http://dx.doi.org/10.47886/9781888569087.ch3.

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&lt;em&gt;Abstract&lt;/em&gt;.—Reproductive success and vitamin B&lt;sub&gt;1 &lt;/sub&gt;(thiamine pyrophosphate, thiamine monophosphate, and free thiamine) concentrations were assessed in feral female lake trout &lt;em&gt;Salvelinus namaycush &lt;/em&gt;from Lake Ontario and Lake Manitou. We monitored fertilization success, survival to hatch, incidence of blue-sac disease, other anomalies, and lake trout early mortality syndrome (EMS). Fertilization and hatching success were high, whereas mortality from blue-sac disease and other anomalies was low in egg batches from both lakes. There was no mortality from EMS in families from Lake Manitou. However, EMS occurred after hatching in the offspring of 48% of the females collected from Lake Ontario. We measured thiamine in liver, red blood cells, eggs, and developing embryos. Relative to fish collected in reference lakes, females in Lake Ontario had depressed hepatic, red blood cell, and egg thiamine concentrations. Although more extensive investigation of thiamine balance is required, it may be possible to use red blood cell thiamine pyrophosphate as a predictive index for EMS susceptibility in offspring. Total thiamine concentrations in developing embryos declined by 50% between fertilization and swim-up. Free thiamine reserves declined most rapidly, whereas levels of thiamine pyrophosphate increased between the eyed embryo and hatch stages. A high proportion (67%) of lake trout families in which the initial egg free thiamine reserves or embryonic concentrations of thiamine pyrophosphate levels were &lt;0.8 nmol/g exhibited EMS. Below this threshold (0.8 nmol/g), the occurrence of EMS was variable (0–100%) and only weakly related to free thiamine concentrations (&lt;em&gt;r&lt;/em&gt;&lt;sup&gt;2&lt;/sup&gt; = 0.32, &lt;EM&gt;P&lt;/EM&gt; = 0.014). This observation implies the possibility of additional interactions with other factors.
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"Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea." In Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, edited by Scott B. Brown, Dale C. Honeyfield, and Lenore Vandenbyllaardt. American Fisheries Society, 1998. http://dx.doi.org/10.47886/9781888569087.ch8.

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&lt;em&gt;Abstract&lt;/em&gt;.—Thiamine pyrophosphate, thiamine monophosphate, and thiamine were measured by reversed phase high-performance liquid chromatography in tissues of lake trout &lt;em&gt;Salvelinus namaycush &lt;/em&gt;and alewife &lt;em&gt;Alosa pseudoharengus&lt;/em&gt;. Mean assay sensitivity for thiamine and its phosphates was 0.012 pmol. Average recoveries of low and high doses of thiamine compounds added to tissue samples ranged from 91.4 to 104.5%. Average coefficients of variation for between assay reproducibility ranged from 4.8 to 12.8%. The predominant form of vitamin B&lt;sub&gt;1 &lt;/sub&gt;was unesterified thiamine in eggs and plasma of lake trout. Thiamine pyrophosphate was the predominant form in red blood cells, liver, muscle, and kidney. The stability of thiamine forms in fish tissues was temperature and species dependent. Thiamine levels were markedly depressed in lake trout collected from Lake Ontario relative to levels in fish captured from Lake 468 at the Experimental Lakes Area in northwestern Ontario.
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"Thiamin(pyrophosphat) und Thiamintriphosphat." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_313642.

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"Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea." In Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, edited by Dale C. Honeyfield, Kofi Fynn-Aikins, John D. Fitzsimons, and Jennifer A. Mota. American Fisheries Society, 1998. http://dx.doi.org/10.47886/9781888569087.ch18.

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&lt;em&gt;Abstract&lt;/em&gt;.—Dietary amprolium, a thiamine antagonist, was fed to lake trout &lt;em&gt;Salvelinus namaycush &lt;/em&gt;broodstock from April to October before spawning to determine its effect on egg and tissue concentrations of thiamine, thiamine monophosphate, and thiamine pyrophosphate. The thiamine concentration of eggs from fish fed no amprolium was 61.8 nmol/g, whereas the concentration of thiamine in fish fed 0.05 and 0.10% amprolium was 4.02 and 1.71 nmol/g (&lt;EM&gt;P &lt;/EM&gt;&lt; 0.01), respectively. In lake trout fed 0.10% amprolium beginning in August, egg free thiamine concentration was reduced to 11.6 nmol/g. No sign of early mortality syndrome was observed in sac fry from eggs in this study, which suggests that thiamine concentrations in the egg were not low enough to be below a critical threshold or that factors other than thiamine are involved in early mortality syndrome.
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"Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea." In Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, edited by Ying Q. Ji, Joseph J. Warthesen, and Ira R. Adelman. American Fisheries Society, 1998. http://dx.doi.org/10.47886/9781888569087.ch11.

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&lt;em&gt;Abstract&lt;/em&gt;.—Juvenile and adult lake trout &lt;em&gt;Salvelinus namaycush &lt;/em&gt;that were fed semipurified, thiaminedeficient diets or alewives &lt;em&gt;Alosa pseudoharengus &lt;/em&gt;containing thiaminase, a thiamine-destroying enzyme, showed no overt symptoms of thiamine deficiency. Growth rates and ovulation rates were similar among all treatments. However, liver thiamine pyrophosphate (TPP), a biochemical indicator of impending thiamine deficiency, in juvenile lake trout fed thiamine-deficient diets was reduced to 35 pmol/ g compared with 59 pmol/g in control groups. Blood TPP in adult female lake trout fed alewives was one-third of that in controls fed a commercial diet. Adult lake trout from Lake Michigan had blood TPP levels similar to those of fish fed the alewife diet in the laboratory. Lake Superior lake trout had TPP levels similar to those of fish fed the control diet in the laboratory. Thiamine synthesis occurred in the intestine of lake trout. At least 81% of thiamine in the posterior intestine was synthesized, presumably by bacteria, when a &lt;sup&gt;14&lt;/sup&gt;C-labeled thiamine diet was force-fed to lake trout. Thiamine had a long retention time in the lake trout: at 27 weeks after fish were injected with radioactive thiamine, blood cells retained 11% of the radioactivity that was present at 2 d and liver tissue retained 34% of the 2-d level. Lack of self-sustaining lake trout reproduction by Lake Michigan fish may be related to their lower blood thiamine levels. Thiamine deficiency may cause early mortality syndrome, which is common in Lake Michigan but not Lake Superior fish with higher blood thiamine levels.
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"Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea." In Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, edited by Dale C. Honeyfield, John G. Hnath, Jim Copeland, Konrad Dabrowski, and Jozef H. Blom. American Fisheries Society, 1998. http://dx.doi.org/10.47886/9781888569087.ch14.

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&lt;em&gt;Abstract.—&lt;/em&gt;Muscle and egg samples from returning adult female Lake Michigan coho salmon &lt;em&gt;Oncorhynchus kisutch &lt;/em&gt;were collected for thiamine analysis. Three groups of five females having low (2.5%), medium (42.4%), or high (92.6%) mean fry survival were selected for this study. Egg and muscle samples were collected at spawning and analyzed by high-performance liquid chromatography analysis for free thiamine, thiamine monophosphate (TP), and thiamine pyrophosphate (TPP). Egg concentrations of ascorbic acid, iron, zinc, magnesium, and potassium were measured. Twenty-five contaminants were also measured in muscle tissue of adult females. Total thiamine levels in eggs were similar between the medium and high survival groups but significantly lower in the low survival group. Eggs from the high and medium survival groups had higher levels of free thiamine and TP (&lt;EM&gt;P &lt;/EM&gt;&lt; 0.01) than eggs from the low survival group. There were no significant differences among the three groups in egg TPP. Muscle concentrations of TPP, TP, and total thiamine were similar among the three survival groups (&lt;EM&gt;P &lt;/EM&gt;&gt; 0.10). Correlations between fry survival and egg free thiamine (&lt;em&gt;r &lt;/em&gt;= 0.61) and TP (&lt;em&gt;r &lt;/em&gt;= 0.52) were observed. Fry survival was not correlated with adult muscle concentration of any form of thiamine or contaminant measured. Among the three groups, no differences in egg concentration were found for ascorbic acid, dehydroascorbic acid, iron, magnesium, zinc, and potassium. This research supports the hypothesis that low egg thiamine is an important factor in early mortality syndrome.
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Frey, Perry A., and Adrian D. Hegeman. "Decarboxylation and Carboxylation." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0012.

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Decarboxylation is an essential process in catabolic metabolism of essentially all nutrients that serve as sources of energy in biological cells and organisms. The most widely known biological process leading to decarboxylation is the metabolism of glucose, in which all of the carbon in the molecule is oxidized to carbon dioxide by way of the glycolytic pathway, the pyruvate dehydrogenase complex, and the tricarboxylic acid cycle. The decarboxylation steps take place in thiamine pyrophosphate (TPP)–dependent α-ketoacid dehydrogenase complexes and isocitrate dehydrogenase. The latter enzyme does not require a coenzyme, other than the cosubstrate NAD+. Many other decarboxylations require coenzymes such as pyridoxal-5'-phosphate (PLP) or a pyruvoyl moiety in the peptide chain. Biological carboxylation is the essential process in the fixation of carbon dioxide by plants and of bicarbonate by animals, plants, and bacteria. Carboxylation by enzymes requires the action of biotin or a divalent metal cofactor, and it requires ATP when the carboxylating agent is the bicarbonate ion. The most prevalent enzymatic carboxylation is that of ribulose bisphosphate carboxylase (rubisco), which is responsible for carbon dioxide fixation in plants. The basic chemistry of decarboxylation is illustrated by mechanisms A to D in fig. 8-1. The mechanisms all require some means of accommodation for the electrons from the cleavage of the bond linking the carboxylate group to the α-carbon. In mechanism A, an electron sink at the β-carbon provides a haven for two electrons. Acetoacetate decarboxylase functions by this mechanism (see chap. 1), as well as PLP- and TPP-dependent decarboxylases (see chap. 3). In mechanism B, a leaving group at the β-carbon departs with two electrons. Mevalonate-5-diphosphate decarboxylate functions by mechanism B and is discussed in a later section. In mechanism C, a leaving group replaces the α-carbon and departs with a pair of electrons. A biological example is formate dehydrogenase, in which the leaving group is a hydride that is transferred to NAD+. In mechanism D, a free radical center is created adjacent to the α-carbon and potentiates the homolytic scission of the bond to the carboxylate group. Mechanism D requires secondary electron transfer processes to create the radical center and quench the formyl radical.
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