Friedrich, W. Thiamin (Vitamin B1, aneurin). in: Hanbuch der Vitamine, Urban & Schwarzenberg, München, Vien, Baltimore, 1987, 240–258.
 Hohmann, S. and Meacock, P.A. Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation. Biochim. Biophys. Acta 1385 (1998) 201–219.
 Nosaka, K. Recent progress in understanding thiamin biosynthesis and its genetic regulation in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 72 (2006) 30–40. http://dx.doi.org/10.1007/s00253-006-0464-9 [CrossRef]
 Lai, E.C. RNA sensors and riboswitches: self-regulating messages. Curr. Biol. 13 (2003) 285–291. http://dx.doi.org/10.1016/S0960-9822(03)00203-3 [CrossRef]
 Bettendorff, L. A non-cofactor role of thiamine derivatives in excitable cells? Arch. Physiol. Biochem. 104 (1996) 745–751. http://dx.doi.org/10.1076/apab.104.6.745.12916 [CrossRef]
 Lakaye, B., Wirtzfeld, B., Wins, P., Grisar, T. and Bettendorff, L. Thiamine triphosphate, a new signal required for optimal growth of Escherichia coli during amino acid starvation. J. Biol. Chem. 279 (2004) 17142–17147. http://dx.doi.org/10.1074/jbc.M313569200 [CrossRef]
 Machado, C.R., Praekelt, U.M., Costa de Oliveira, R.L., Barbosa, A.C.C., Byrne, K.L., Meacock, P.A. and Menck, C.F.M. Dual role for yeast THI4 gene in thiamine biosynthesis and DNA damage tolerance. J. Mol. Biol. 273 (1997) 114–121. http://dx.doi.org/10.1006/jmbi.1997.1302 [CrossRef]
 Medina-Silva, R., Barros, M.P., Galhardo, R.S., Netto, L.S., Colepicolo, P. and Menck, C.F. Heat stress promotes mitochondrial instability and oxidative responses in yeast deficient in thiazole biosynthesis. Res. Microbiol. 157 (2005) 275–281. http://dx.doi.org/10.1016/j.resmic.2005.07.004 [CrossRef]
 Ahn, I-P., Kim, S. and Lee, Y-H. Vitamin B1 functions as an activator of plant disease resistance. Plant Physiol. 138 (2005) 1505–1515. http://dx.doi.org/10.1104/pp.104.058693 [CrossRef]
 Begley, T., Downs, D., Ealick S., McLafferty, F., Van Loon, D., Taylor, S., Campobasso, N., Chiu, J., Kinsland, C., Reddick, J. and Xi, J. Thiamin biosynthesis in prokaryotes. Arch. Microbiol. 171 (1999) 293–300. http://dx.doi.org/10.1007/s002030050713 [CrossRef]
 Chatterjee, A., Jurgenson, C.T., Schroeder, F.C., Ealick, S.E. and Begley, T.P. Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate. J. Am. Chem. Soc. 14 (2007) 2914–2922. http://dx.doi.org/10.1021/ja067606t [CrossRef]
 Nosaka, K., Nishimura, H., Kawasaki, Y., Tsujihara, T. and Iwashima, A. Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae. J. Biol. Chem. 269 (1994) 30510–3-516.
 Zeidler, J., Sayer, B.G. and Spenser, I.D. Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid. J. Am. Chem. Soc. 125 (2003) 13094–13105. http://dx.doi.org/10.1021/ja030261j [CrossRef]
 Kawasaki, Y., Onozuka, M., Mizote, T. and Nosaka, K. Biosynthesis of hydroxymethylpyrimidine pyrophosphate in Saccharomyces cerevisiae. Curr. Genet. 47 (2005) 156–162. http://dx.doi.org/10.1007/s00294-004-0557-x [CrossRef]
 Nosaka, K., Kaneko, Y., Nishimura, H. and Iwashima, A. Isolation and characterization of a thiamin pyrophosphokinase gene, THI80, from Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 17440–17447.
 Enjo, F., Nosaka, K., Ogata, M., Iwashima, A. and Nishimura, H. Isolation and characterization of a thiamin transport gene, THI10, from Saccharomyces cerevisiae. J. Biol. Chem. 272 (1997) 19165–19170. http://dx.doi.org/10.1074/jbc.272.31.19165 [CrossRef]
 Jurgenson, C.T., Chatterjee, A., Begley, T.P. and Ealick, S.E. Structural insights into the function of the thiamine biosynthetic enzyme Thi4 from Saccharomyces cerevisiae. Biochemistry 45 (2006) 11061–11070. http://dx.doi.org/10.1021/bi061025z [CrossRef]
 Faou, P. and Tropschug, M. Neurospora crassa CyPBP37: a cytosolic stress protein that is able to replace yeast Thi4p function in the synthesis of vitamin B1. J. Mol. Biol. 344 (2004) 1147–1157. http://dx.doi.org/10.1016/j.jmb.2004.09.097 [CrossRef]
 Wightman, R. and Meacock, P.A. The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine. Microbiology 149 (2003) 1447–1460. http://dx.doi.org/10.1099/mic.0.26194-0 [CrossRef]
 Haas, A.L., Laun, N.P. and Begley, T.P. Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities. Bioorg. Chem. 33 (2005) 338–344. http://dx.doi.org/10.1016/j.bioorg.2005.04.001 [CrossRef]
 Llorente, B., Fairhead, C. and Dujon, B. Genetic redundancy and gene fusion in the genome of the baker’s yeast Saccharomyces cerevisiae: functional characterization of a three-member gene family involved in the thiamine biosynthetic pathway. Mol. Microbiol. 32 (1999) 1140–1152. http://dx.doi.org/10.1046/j.1365-2958.1999.01412.x [CrossRef]
 Nosaka, K., Kaneko, Y., Nishimura, H. and Iwashima, A. A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast. FEMS Microbiol. Lett. 51 (1989) 55–59. http://dx.doi.org/10.1016/0378-1097(89)90077-3 [CrossRef]
 Marobbio, C.M., Vozza, A., Harding, M., Bissaccia, F., Palmieri, F. and Walker, J.E. Identification and reconstitution of the yeast mitochondrial transporter for thiamine pyrophosphate. EMBO J. 21 (2002) 5653–5661. http://dx.doi.org/10.1093/emboj/cdf583 [CrossRef]
 Nosaka, K., Onozuka, M., Konno, H., Kawasaki, Y., Nishimura H., Sano, M. and Akaji, K. Genetic regulation mediated by thiamin pyrophosphate-binding motif in Saccharomyces cerevisiae. Mol. Microbiol. 58 (2005) 467–479. http://dx.doi.org/10.1111/j.1365-2958.2005.04835.x [CrossRef]
 Mojzita D. and Hohmann, S. Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces cerevisiae. Mol. Gen. Genomics 276 (2006) 147–161. http://dx.doi.org/10.1007/s00438-006-0130-z [CrossRef]
 Baker, L.J., Dorocke, J.A., Harris, R.A. and Timm, D.E. The crystal structure of yeast thiamin pyrophosphokinase. Structure 9 (2001) 539–546. http://dx.doi.org/10.1016/S0969-2126(01)00615-3 [CrossRef]
 Voskoboyev, A.I. and Ostrovsky, Y.M. Thiamin pyrophosphokinase: structure, properties, and role in thiamin metabolism. Ann. N. Y. Acad. Sci. 378 (1982) 161–176. http://dx.doi.org/10.1111/j.1749-6632.1982.tb31195.x [CrossRef]
 Kawasaki, Y. Copurification of hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase of Saccharomyces cerevisiae: characterization of hydroxyethylthiazole kinase as a bifunctional enzyme in the thiamine biosynthetic pathway. J. Bacteriol. 175 (1993) 5153–5158.
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The genes and enzymes involved in the biosynthesis of thiamin and thiamin diphosphate in yeasts
1Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387, Kraków, Poland
© 2007 University of Wrocław, Poland. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. (CC BY-NC-ND 3.0)
Citation Information: Cellular and Molecular Biology Letters. Volume 13, Issue 2, Pages 271–282, ISSN (Online) 1689-1392, DOI: 10.2478/s11658-007-0055-5, April 2008
- Published Online:
Thiamin (vitamin B1) is an essential molecule for all living organisms. Its major biologically active derivative is thiamin diphosphate, which serves as a cofactor for several enzymes involved in carbohydrate and amino acid metabolism. Important new functions for thiamin and its phosphate esters have recently been suggested, e.g. in gene expression regulation by influencing mRNA structure, in DNA repair after UV illumination, and in the protection of some organelles against reactive oxygen species. Unlike higher animals, which rely on nutritional thiamin intake, yeasts can synthesize thiamin de novo. The biosynthesis pathways include the separate synthesis of two precursors, 4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate and 5-(2-hydroxyethyl)-4-methylthiazole phosphate, which are then condensed into thiamin monophosphate. Additionally, yeasts evolved salvage mechanisms to utilize thiamin and its dephosphorylated late precursors, 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole, from the environment. The current state of knowledge on the discrete steps of thiamin biosynthesis in yeasts is far from satisfactory; many intermediates are postulated only by analogy to the much better understood biosynthesis process in bacteria. On the other hand, the genetic mechanisms regulating thiamin biosynthesis in yeasts are currently under extensive exploration. Only recently, the structures of some of the yeast enzymes involved in thiamin biosynthesis, such as thiamin diphosphokinase and thiazole synthase, were determined at the atomic resolution, and mechanistic proposals for the catalysis of particular biosynthetic steps started to emerge.
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