Gene Symbol: TPI1
Description: triose-phosphate isomerase TPI1
Alias: triose-phosphate isomerase TPI1
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Krietsch W. Triosephosphate isomerase from yeast. Methods Enzymol. 1975;41:434-8 pubmed
  2. Brandina I, Graham J, Lemaitre Guillier C, Entelis N, Krasheninnikov I, Sweetlove L, et al. Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta. 2006;1757:1217-28 pubmed
    ..This suggests an unsuspected novel function for this complex in tRNA mitochondrial import. ..
  3. Vázquez Pérez A, Fernandez Velasco D. Pressure and denaturants in the unfolding of triosephosphate isomerase: the monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica. Biochemistry. 2007;46:8624-33 pubmed
    ..Therefore, dimerization prevents the pressure unfolding of the monomer. ..
  4. Fan X, Martin Brown S, Florens L, Li R. Intrinsic capability of budding yeast cofilin to promote turnover of tropomyosin-bound actin filaments. PLoS ONE. 2008;3:e3641 pubmed publisher
    ..Our results suggest that yeast cofilin has the intrinsic ability to promote actin cable turnover, and that the severing activity may rely on its ability to bind Tpm1. ..
  5. Reyes López C, González Mondragón E, Benitez Cardoza C, Chánez Cárdenas M, Cabrera N, Perez Montfort R, et al. The conserved salt bridge linking two C-terminal beta/alpha units in homodimeric triosephosphate isomerase determines the folding rate of the monomer. Proteins. 2008;72:972-9 pubmed publisher
    ..The value for the D225Q mutant, which is about 40% of the corresponding value for yTIM, would implicate the folding of only three quarters of a monomer chain in the transition state. ..
  6. Peimbert M, Dominguez Ramirez L, Fernandez Velasco D. Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution. Biochemistry. 2008;47:5556-64 pubmed publisher
    ..The change in the intermediate nature suggests that the relative stabilities of different folding units are similar so that subtle alterations in their stability produce a total transformation of the folding pathway. ..
  7. Hernandez Santoyo A, Dominguez Ramirez L, Reyes López C, González Mondragón E, Hernández Arana A, Rodriguez Romero A. Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Int J Mol Sci. 2012;13:10010-21 pubmed publisher
    ..The latter results were confirmed by means of Molecular Dynamics, which showed that this region, in the mutated enzyme, collapses at about 70 ns. ..
  8. Labastida Pólito A, Garza Ramos G, Camarillo Cadena M, Zubillaga R, Hernández Arana A. Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase. BMC Biochem. 2015;16:20 pubmed publisher
    ..strand-type residual structure, which appears below pH 8.0, is likely to be associated with increased irreversible aggregation of the unfolded protein. However, this denatured form apparently accelerates the refolding process. ..
  9. Compagno C, Brambilla L, Capitanio D, Boschi F, Ranzi B, Porro D. Alterations of the glucose metabolism in a triose phosphate isomerase-negative Saccharomyces cerevisiae mutant. Yeast. 2001;18:663-70 pubmed
    ..1996). Alterations of glucose metabolism imposed by the deletion of the TPI1 gene in Saccharomyces cerevisiae were studied in batch and continuous cultures...

More Information


  1. Overkamp K, Bakker B, Kötter P, Luttik M, van Dijken J, Pronk J. Metabolic engineering of glycerol production in Saccharomyces cerevisiae. Appl Environ Microbiol. 2002;68:2814-21 pubmed
    Inactivation of TPI1, the Saccharomyces cerevisiae structural gene encoding triose phosphate isomerase, completely eliminates growth on glucose as the sole carbon source...
  2. Rozovsky S, McDermott A. Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase. Proc Natl Acad Sci U S A. 2007;104:2080-5 pubmed
  3. Gulotta M, Qiu L, Desamero R, ROSGEN J, Bolen D, Callender R. Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomerase. Biochemistry. 2007;46:10055-62 pubmed
    ..Results indicate that the conformational shift hypothesis alone does not account for the effects of osmolytes on Km's. ..
  4. Araiza Olivera D, Chiquete Felix N, Rosas Lemus M, Sampedro J, Pena A, Mújica A, et al. A glycolytic metabolon in Saccharomyces cerevisiae is stabilized by F-actin. FEBS J. 2013;280:3887-905 pubmed publisher
    ..In S. cerevisiae, a glycolytic metabolon appear to assemble in association with F-actin. In this complex, fermentation activity is enhanced and enzymes are partially protected against inhibition by trehalose or by antibodies. ..
  5. Finnigan G, Duvalyan A, Liao E, Sargsyan A, Thorner J. Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system. Mol Biol Cell. 2016;27:2708-25 pubmed publisher
  6. Xu Y, Lorieau J, McDermott A. Triosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy. J Mol Biol. 2010;397:233-48 pubmed publisher
    ..These studies identify a number of new sites with particularly clear markers for ligand binding, paving the way for future studies of triosephosphate isomerase dynamics and mechanism. ..