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Journal articles on the topic 'Thiamin pyrophosphate'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 January 2023

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Williams, K., P. N. Lowe, and P. F. Leadlay. "Purification and characterization of pyruvate: ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis." Biochemical Journal 246, no. 2 (1987): 529–36. http://dx.doi.org/10.1042/bj2460529.

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The pyruvate: ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis is an extrinsic protein bound to the hydrogenosomal membrane. It has been solubilized and purified to homogeneity, principally by salting-out chromatography on Sepharose 4B. Low recoveries of active enzyme were caused by inactivation by O2 and the irreversible loss of thiamin pyrophosphate. It is a dimeric enzyme of overall Mr 240,000 and subunit Mr 120,000. The enzyme contains, per mol of dimer, 7.3 +/- 0.3 mol of iron and 5.9 +/- 0.9 mol of acid-labile sulphur, suggesting the presence of two [4Fe-4S] c

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12

Sabui, Subrata, Jose M. Romero, and Hamid M. Said. "Developmental maturation of the colonic uptake process of the microbiota-generated thiamin pyrophosphate." American Journal of Physiology-Gastrointestinal and Liver Physiology 320, no. 5 (2021): G829—G835. http://dx.doi.org/10.1152/ajpgi.00067.2021.

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The colonic carrier-mediated uptake process of the microbiota-generated and phosphorylated form of vitamin B1, i.e., thiamin pyrophosphate, undergoes ontogenic changes that parallel the development of the gut microbiota (and their ability to generate vitamins) during early stages of life.

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13

Subramanian, Veedamali S., Sandeep B. Subramanya, Hidekazu Tsukamoto, and Hamid M. Said. "Effect of chronic alcohol feeding on physiological and molecular parameters of renal thiamin transport." American Journal of Physiology-Renal Physiology 299, no. 1 (2010): F28—F34. http://dx.doi.org/10.1152/ajprenal.00140.2010.

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The renal thiamin reabsorption process plays an important role in regulating thiamin body homeostasis and involves both thiamin transporters-1 and -2 (THTR1 and THTR2). Chronic alcohol use is associated with thiamin deficiency. Although a variety of factors contribute to the development of this deficiency, effects of chronic alcohol use on renal thiamin transport have not been thoroughly examined. We addressed this issue by examining the effect of chronic alcohol feeding of rats with liquid diet on physiological and molecular parameters of renal thiamin transport. Chronic alcohol feeding cause

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14

Gans, D. A., and A. E. Harper. "Thiamin status of incarcerated and nonincarcerated adolescent males: dietary intake and thiamin pyrophosphate response." American Journal of Clinical Nutrition 53, no. 6 (1991): 1471–75. http://dx.doi.org/10.1093/ajcn/53.6.1471.

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15

Williams, K. P., P. F. Leadlay, and P. N. Lowe. "Inhibition of pyruvate:ferredoxin oxidoreductase from Trichomonas vaginalis by pyruvate and its analogues. Comparison with the pyruvate decarboxylase component of the pyruvate dehydrogenase complex." Biochemical Journal 268, no. 1 (1990): 69–75. http://dx.doi.org/10.1042/bj2680069.

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Pyruvate:ferredoxin oxidoreductase and the pyruvate dehydrogenase multi-enzyme complex both catalyse the CoA-dependent oxidative decarboxylation of pyruvate but differ in size, subunit composition and mechanism. Comparison of the pyruvate:ferredoxin oxidoreductase from the protozoon Trichomonas vaginalis and the pyruvate dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex shows that both are inactivated by incubation with pyruvate under aerobic conditions in the absence of co-substrates. However, only the former is irreversibly inhibited by incubation with hydroxypyr

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16

Hawkins, Christopher F., Adolfo Borges, and Richard N. Perham. "A common structural motif in thiamin pyrophosphate-binding enzymes." FEBS Letters 255, no. 1 (1989): 77–82. http://dx.doi.org/10.1016/0014-5793(89)81064-6.

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17

Reed, George H., Stephen W. Ragsdale, and Steven O. Mansoorabadi. "Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1824, no. 11 (2012): 1291–98. http://dx.doi.org/10.1016/j.bbapap.2011.11.010.

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18

Müri, R. M., J. von Overbeck, J. Furrer, and P. E. Ballmer. "Thiamin deficiency in HIV-positive patients: evaluation by erythrocyte transketolase activity and thiamin pyrophosphate effect." Clinical Nutrition 18, no. 6 (1999): 375–78. http://dx.doi.org/10.1016/s0261-5614(99)80019-3.

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19

Keith, Mary, Shirley Quach, Mavra Ahmed, et al. "Thiamin supplementation does not improve left ventricular ejection fraction in ambulatory heart failure patients: a randomized controlled trial." American Journal of Clinical Nutrition 110, no. 6 (2019): 1287–95. http://dx.doi.org/10.1093/ajcn/nqz192.

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ABSTRACT Background Thiamin, a water-soluble B-complex vitamin, functions as a coenzyme in macronutrient oxidation and in the production of cellular ATP. Data suggest that thiamin depletion occurs in heart failure (HF). Therefore, thiamin supplementation in HF patients may improve cardiac function. Objective We sought to determine whether oral thiamin supplementation improves left ventricular ejection fraction (LVEF), exercise tolerance, and quality of life among patients with HF and reduced LVEF. Methods In this prospective, multicenter, double-blind, placebo-controlled randomized trial, elig

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20

Essama-Tjani, Jeanne Chantal, Jean-Claude Guilland, Françoise Fuchs, Marie Lombard, and Dominique Richard. "Changes in Thiamin, Riboflavin, Niacin, beta-carotene, Vitamins C, A, D and E Status of French Elderly Subjects during the First Year of Institutionalization." International Journal for Vitamin and Nutrition Research 70, no. 2 (2000): 54–64. http://dx.doi.org/10.1024/0300-9831.70.2.54.

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Vitamin status was assessed in 26 recently institutionalized elderly subjects by combining dietary and biochemical measurements of thiamin, riboflavin, niacin, beta-carotene, vitamins C, A, D and E at admission (P1), and 1.5 (P2), 3.0 (P3), 4.5 (P4), 6.0 (P5), 12 (P6) months later. At admission, except for vitamin A, mean vitamin intakes were lower than the 1992 French Recommended Dietary Allowance. Thiamin, vitamins C, A and E status seemed nearly satisfactory as less than one-fourth of the population sample had blood values lower than the cut-off point for thiamin (erythrocyte thiamin pyroph

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21

Kennedy, Lindsey, Heather Francis, and Gianfranco Alpini. "Impact of prevailing thiamin levels on thiamin pyrophosphate uptake in pancreatic acinar cells: do the shuttle!" American Journal of Physiology-Gastrointestinal and Liver Physiology 313, no. 5 (2017): G373—G375. http://dx.doi.org/10.1152/ajpgi.00256.2017.

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22

Subramanian, Veedamali S., Svetlana M. Nabokina, Yaping Lin-Moshier, Jonathan S. Marchant, and Hamid M. Said. "Mitochondrial Uptake of Thiamin Pyrophosphate: Physiological and Cell Biological Aspects." PLoS ONE 8, no. 8 (2013): e73503. http://dx.doi.org/10.1371/journal.pone.0073503.

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23

Nosaka, Kazuto, Mari Onozuka, Hiroyuki Konno, et al. "Genetic regulation mediated by thiamin pyrophosphate-binding motif inSaccharomyces cerevisiae." Molecular Microbiology 58, no. 2 (2005): 467–79. http://dx.doi.org/10.1111/j.1365-2958.2005.04835.x.

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24

Miranda-Ríos, Juan. "The THI-box Riboswitch, or How RNA Binds Thiamin Pyrophosphate." Structure 15, no. 3 (2007): 259–65. http://dx.doi.org/10.1016/j.str.2007.02.001.

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25

Park, Joo-Heon, Pieter C. Dorrestein, Huili Zhai, Cynthia Kinsland, Fred W. McLafferty, and Tadhg P. Begley. "Biosynthesis of the Thiazole Moiety of Thiamin Pyrophosphate (Vitamin B1)†." Biochemistry 42, no. 42 (2003): 12430–38. http://dx.doi.org/10.1021/bi034902z.

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26

Sato, Akiko, Shinji Sato, Go Omori, and Keiichi Koshinaka. "Effects of Thiamin Restriction on Exercise-Associated Glycogen Metabolism and AMPK Activation Level in Skeletal Muscle." Nutrients 14, no. 3 (2022): 710. http://dx.doi.org/10.3390/nu14030710.

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This study aimed to investigate the direct influence of a decrease in the cellular thiamin level, before the onset of anorexia (one of the symptoms of thiamin deficiency) on glycogen metabolism and the AMP-activated protein kinase (AMPK) activation levels in skeletal muscle at rest and in response to exercise. Male Wistar rats were classified as the control diet (CON) group or the thiamin-deficient diet (TD) group and consumed the assigned diets for 1 week. Skeletal muscles were taken from the rats at rest, those that underwent low-intensity swimming (LIS), or high-intensity intermittent swimm

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27

Dodi, K., M. Louloudi, G. Malandrinos та N. Hadjiliadis. "Metal complexes with 2-(α-hydroxy-benzyl) thiamin pyrophosphate (HBTPP). Models for metal binding of thiamin enzymes". Journal of Inorganic Biochemistry 73, № 1-2 (1999): 41–47. http://dx.doi.org/10.1016/s0162-0134(98)10089-2.

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28

SCHELLENBERGER, A. "Thiamin Pyrophosphate Binding Mechanism and the Function of the Aminopyrimidine Part." Journal of Nutritional Science and Vitaminology 38, Special (1992): 392–96. http://dx.doi.org/10.3177/jnsv.38.special_392.

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29

Subramanian, Veedamali S., Svetlana M. Nabokina, Yaping Lin-Moshier, Jonathan S. Marchant, and Hamid M. Said. "Correction: Mitochondrial Uptake of Thiamin Pyrophosphate: Physiological and Cell Biological Aspects." PLOS ONE 12, no. 10 (2017): e0186541. http://dx.doi.org/10.1371/journal.pone.0186541.

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30

Strumilo, Slawomir, Jan Czerniecki, and Pawel Dobrzyn. "Regulatory Effect of Thiamin Pyrophosphate on Pig Heart Pyruvate Dehydrogenase Complex." Biochemical and Biophysical Research Communications 256, no. 2 (1999): 341–45. http://dx.doi.org/10.1006/bbrc.1999.0321.

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31

GIBSON, D. M., J. J. KENNELLY, and F. X. AHERNE. "THE PERFORMANCE AND THIAMIN STATUS OF PIGS FED SULFUR DIOXIDE TREATED HIGH-MOISTURE BARLEY." Canadian Journal of Animal Science 67, no. 3 (1987): 841–54. http://dx.doi.org/10.4141/cjas87-087.

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High-moisture barley (HMB) was ensiled or treated with 1% (wt/wt) liquid sulfur dioxide (SO2). Forty-five weanling pigs were allocated to five dietary treatments for 28 d. Diets consisted of: (1) dry barley, diet mixed every 28 d; (2) ensiled HMB, diet mixed daily; (3) SO2-treated HMB, diet mixed every 28 d; (4) SO2-treated HMB, diet mixed daily; (5) SO2-treated HMB, diet mixed daily and supplemented with thiamin. All diets contained 47% barley on a dry matter (DM) basis. Pigs fed diets 2 and 4 continued on test to 85 kg; diets formulated after 28 d contained 75% barley (DM basis). Feed intake

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32

Talwar, Dinesh, Helen Davidson, Josephine Cooney, and Denis St. JO’Reilly. "Vitamin B1 Status Assessed by Direct Measurement of Thiamin Pyrophosphate in Erythrocytes or Whole Blood by HPLC: Comparison with Erythrocyte Transketolase Activation Assay." Clinical Chemistry 46, no. 5 (2000): 704–10. http://dx.doi.org/10.1093/clinchem/46.5.704.

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Abstract Background: The concentration of thiamin diphosphate (TDP) in erythrocytes is a useful index of thiamin status. We describe an HPLC method for TDP and its results in patients at risk of thiamin deficiency. Methods: We used reversed-phase HPLC with postcolumn derivatization with alkaline potassium ferricyanide and fluorescence detection. Samples were deproteinized and injected directly onto a C18 column. TDP concentrations in erythrocytes were compared with those in whole blood. Reference intervals for erythrocyte TDP (n = 147; 79 males and 68 females; mean age, 54 years) and whole blo

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33

Yoshioka, T., and T. Uematsu. "Formation of N-hydroxy-N-arylacetamides from nitroso aromatic compounds by the mammalian pyruvate dehydrogenase complex." Biochemical Journal 290, no. 3 (1993): 783–90. http://dx.doi.org/10.1042/bj2900783.

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Bovine, human and porcine heart mitochondria and isolated porcine heart pyruvate dehydrogenase complex (PDHC) pyruvate-dependently form N-hydroxy-N-arylacetamides from nitroso aromatic compounds, including carcinogenic 4-biphenyl and 2-fluorenyl derivatives. The PDHC-catalysed formation of N-hydroxyacetanilide (N-OH-AA) from nitrosobenzene (NOB), through a Ping Pong mechanism, is optimum at pH 6.8 and is accelerated by thiamin pyrophosphate, but is inhibited by thiamin thiazolone pyrophosphate and ATP. Km pyruvate in the reaction is independent of pH over the range tested, whereas KmNOB increa

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34

Anandam, Kasin Yadunandam, Subrata Sabui, Morgan M. Thompson, Sreya Subramanian, and Hamid M. Said. "Enterohemorrhagic Escherichia coli infection inhibits colonic thiamin pyrophosphate uptake via transcriptional mechanism." PLOS ONE 14, no. 10 (2019): e0224234. http://dx.doi.org/10.1371/journal.pone.0224234.

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35

Rosado-Souza, Laise, Sebastian Proost, Michael Moulin, et al. "Appropriate Thiamin Pyrophosphate Levels Are Required for Acclimation to Changes in Photoperiod." Plant Physiology 180, no. 1 (2019): 185–97. http://dx.doi.org/10.1104/pp.18.01346.

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36

Trebukhina, Raisa V., Yurij M. Ostrovsky, Vladimir S. Shapot, Georgij N. Mikhaltsevich, and Veniamin N. Tumanov. "Turnover of [14C]thiamin and activities of thiamin pyrophosphate‐dependent enzymes in tissues of mice with ehrlich ascites carcinoma." Nutrition and Cancer 6, no. 4 (1985): 260–73. http://dx.doi.org/10.1080/01635588509513832.

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37

Whitfield, Kyly C., Setareh Shahab-Ferdows, Hou Kroeun, et al. "Macro- and Micronutrients in Milk from Healthy Cambodian Mothers: Status and Interrelations." Journal of Nutrition 150, no. 6 (2020): 1461–69. http://dx.doi.org/10.1093/jn/nxaa070.

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ABSTRACT Background Except for low thiamin content, little is known about vitamins or macronutrients in milk from Cambodian mothers, and associations among milk nutrients. Objectives We measured fat-soluble vitamins (FSVs) and water-soluble vitamins (WSVs), and macronutrients, and explored internutrient associations in milk from Cambodian mothers. Methods Milk from women (aged 18–45 y, 3–27 wk postpartum, n = 68) who participated in a thiamin-fortification trial were analyzed for vitamins B-2 (riboflavin, FAD), B-3 (nicotinamide), B-5, B-6 (pyridoxal, pyridoxine), B-7, B-12, A, E [α-tocopherol

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38

Casteels, M., M. Sniekers, P. Fraccascia, G. P. Mannaerts, and P. P. Van Veldhoven. "The role of 2-hydroxyacyl-CoA lyase, a thiamin pyrophosphate-dependent enzyme, in the peroxisomal metabolism of 3-methyl-branched fatty acids and 2-hydroxy straight-chain fatty acids." Biochemical Society Transactions 35, no. 5 (2007): 876–80. http://dx.doi.org/10.1042/bst0350876.

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2-Hydroxyphytanoyl-CoA lyase (abbreviated as 2-HPCL), renamed to 2-hydroxyacyl-CoA lyase (abbreviated as HACL1), is the first peroxisomal enzyme in mammals that has been found to be dependent on TPP (thiamin pyrophosphate). It was discovered in 1999, when studying α-oxidation of phytanic acid. HACL1 has an important role in at least two pathways: (i) the degradation of 3-methyl-branched fatty acids like phytanic acid and (ii) the shortening of 2-hydroxy long-chain fatty acids. In both cases, HACL1 catalyses the cleavage step, which involves the splitting of a carbon–carbon bond between the fir

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39

Srinivasan, Padmanabhan, Svetlana Nabokina, and Hamid M. Said. "Chronic alcohol exposure affects pancreatic acinar mitochondrial thiamin pyrophosphate uptake: studies with mouse 266-6 cell line and primary cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 309, no. 9 (2015): G750—G758. http://dx.doi.org/10.1152/ajpgi.00226.2015.

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Thiamin is essential for normal metabolic activity of all mammalian cells, including those of the pancreas. Cells obtain thiamin from their surroundings and enzymatically convert it into thiamin pyrophosphate (TPP) in the cytoplasm; TPP is then taken up by mitochondria via a specific carrier the mitochondrial TPP transporter (MTPPT; product of the SLC25A19 gene). Chronic alcohol exposure negatively impacts the health of pancreatic acinar cells (PAC), but its effect on physiological/molecular parameters of MTPPT is not known. We addressed this issue using mouse pancreatic acinar tumor cell line

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40

Shigeoka, Shigeru, Toshio Onishi, Kozi Maeda, Yoshihisa Nakano, and Shozaburo Kitaoka. "Occurrence of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in mitochondria of Euglena gracilis." FEBS Letters 195, no. 1-2 (1986): 43–47. http://dx.doi.org/10.1016/0014-5793(86)80126-0.

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41

Anandam, Kasin Yadunandam, Padmanabhan Srinivasan, Veedamali S. Subramanian, and Hamid M. Said. "Molecular mechanisms involved in the adaptive regulation of the colonic thiamin pyrophosphate uptake process." American Journal of Physiology-Cell Physiology 313, no. 6 (2017): C655—C663. http://dx.doi.org/10.1152/ajpcell.00169.2017.

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A considerable amount of the thiamin generated by gut microbiota exists in the form of thiamin pyrophosphate (TPP). We have previously shown that human colonocytes possess an efficient carrier-mediated uptake process for TPP that involves the SLC44A4 system and this uptake process is adaptively regulated by prevailing extracellular TPP level. Little is known about the molecular mechanisms that mediate this adaptive regulation. We addressed this issue using human-derived colonic epithelial NCM460 cells and mouse colonoids as models. Maintaining NCM460 cells in the presence of a high level of TP

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42

Bocobza, Samuel E., Sergey Malitsky, Wagner L. Araújo, et al. "Orchestration of Thiamin Biosynthesis and Central Metabolism by Combined Action of the Thiamin Pyrophosphate Riboswitch and the Circadian Clock in Arabidopsis." Plant Cell 25, no. 1 (2013): 288–307. http://dx.doi.org/10.1105/tpc.112.106385.

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43

O'Fallon, J. V., and B. P. Chew. "Characterization of a retinylmonophosphatase in the plasma membrane of mouse brain." Biochemical Journal 237, no. 3 (1986): 625–30. http://dx.doi.org/10.1042/bj2370625.

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Retinylmonophosphatase (RMPase) activity in mouse brain paralleled the subcellular distribution of the plasma-membrane marker Na+ + K+-dependent ATPase. The enzyme had a pH optimum between 5.5 and 7.0. The enzyme demonstrated linear kinetics with respect to time and both protein and substrate concentrations. RMPase was saturated by low retinyl monophosphate (RMP) concentrations and exhibited an apparent Km of 4.6 microM. The enzyme did not require MgCl2 for activity, and in fact assays were routinely run in the presence of 10 mM-Na2EDTA. In general, detergents inhibited the enzyme, with 0.05%

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44

Nakazawa, Masami, Shigeo Takenaka, Mitsuhiro Ueda, Hiroshi Inui, Yoshihisa Nakano, and Kazutaka Miyatake. "Pyruvate:NADP+ oxidoreductase is stabilized by its cofactor, thiamin pyrophosphate, in mitochondria of Euglena gracilis." Archives of Biochemistry and Biophysics 411, no. 2 (2003): 183–88. http://dx.doi.org/10.1016/s0003-9861(02)00749-x.

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Jikrona, Rafi, Suharjono Suharjono, and Abraham Ahmad. "THIAMINE SUPPLEMENT THERAPY IMPROVES EJECTION FRACTION VALUE IN STAGE II HEART FAILURE PATIENTS." Folia Medica Indonesiana 53, no. 2 (2017): 139. http://dx.doi.org/10.20473/fmi.v53i2.6358.

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Thiamine, also called vitamin B1, is a water soluble vitamin that is involved in the formation of ATP in cells. The active metabolite of thiamine is a co-enzyme thiamine pyrophosphate (TPP) that plays an active role in carbohydrate metabolism and the formation of amino acid binding conjugates. Directly, thiamine may increase energy production in heart muscle cells through such mechanism, whereas in conditions of heart failure, a decrease in the contractility of heart muscle may be found. Therefore, thiamine supplementation is needed in stage II heart failure patients due to long-term use of fu

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KOLOBOVA, Elena, Alina TUGANOVA, Igor BOULATNIKOV, and Kirill M. POPOV. "Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites." Biochemical Journal 358, no. 1 (2001): 69–77. http://dx.doi.org/10.1042/bj3580069.

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The enzymic activity of the mammalian pyruvate dehydrogenase complex is regulated by the phosphorylation of three serine residues (sites 1, 2 and 3) located on the E1 component of the complex. Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (PDK1, PDK2, PDK3 and PDK4) differ in their abilities to phosphorylate the enzyme. PDK1 can phosphorylate all three sites, whereas PDK2, PDK3 and PDK4 each phosphorylate only site 1 and site 2. Although PDK2 phosphorylates site 1 and 2, it incorporates less phosphate in

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Masumoto, Toshiro, R. W. Hardy, and E. Casillas. "Comparison of Transketolase Activity and Thiamin Pyrophosphate Levels in Erythrocytes and Liver of Rainbow Trout (Salmo gairdneri) as Indicators of Thiamin Status." Journal of Nutrition 117, no. 8 (1987): 1422–26. http://dx.doi.org/10.1093/jn/117.8.1422.

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Laber, B., and N. Amrhein. "Metabolism of 1-aminoethylphosphinate generates acetylphosphinate, a potent inhibitor of pyruvate dehydrogenase." Biochemical Journal 248, no. 2 (1987): 351–58. http://dx.doi.org/10.1042/bj2480351.

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The alanine analogue 1-aminoethylphosphinate [H3C-CH(NH2)-PO2H2] effectively inhibited anthocyanin synthesis in buckwheat hypocotyls and caused an increase in the concentrations of alanine and alanine-derived metabolites. Aminotransferase inhibitors partially alleviated the effects of the analogue. 1-Aminoethylphosphinate did not affect the growth of Klebsiella pneumoniae under anaerobic conditions, but under aerobic conditions it inhibited growth and caused the massive excretion of pyruvate. The analogue inhibited the pyruvate dehydrogenase complex in vitro in the presence of an aminotransfer

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Gathercole, P. S., P. G. Thiel, and J. H. S. Hofmeyr. "Inhibition of pyruvate dehydrogenase complex by moniliformin." Biochemical Journal 233, no. 3 (1986): 719–23. http://dx.doi.org/10.1042/bj2330719.

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The mechanism for the inhibition of pyruvate dehydrogenase complex from bovine heart by moniliformin was investigated. Thiamin pyrophosphate proved to be necessary for the inhibitory action of moniliformin. The inhibition reaction was shown to be time-dependent and to follow first-order and saturation kinetics. Pyruvate protected the pyruvate dehydrogenase complex against moniliformin inactivation. Extensive dialysis of the moniliformin-inactivated complex only partially reversed inactivation. Moniliformin seems to act by inhibition of the pyruvate dehydrogenase component of the enzyme complex

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Ali, M. Showkat, Bhami C. Shenoy, Devayani Eswaran, Laura A. Andersson, Thomas E. Roche, and Mulchand S. Patel. "Identification of the Tryptophan Residue in the Thiamin Pyrophosphate Binding Site of Mammalian Pyruvate Dehydrogenase." Journal of Biological Chemistry 270, no. 9 (1995): 4570–74. http://dx.doi.org/10.1074/jbc.270.9.4570.

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