The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

tpiA  -  triosephosphate isomerase

Escherichia coli O157:H7 str. Sakai

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ECs4844

  • The purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described [1].
  • The urea-induced unfolding of the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli, an eight-stranded (beta/alpha)(8) TIM barrel protein, has been shown to involve two stable equilibrium intermediates, I1 and I2, well populated at approximately 3 M and 5 M urea, respectively [2].
  • The role of native contact topology in the folding of a TIM barrel model based on the alpha-subunit of tryptophan synthase (alphaTS) from Salmonella typhimurium (Protein Data Bank structure 1BKS) was studied using both equilibrium and kinetic simulations [3].
  • By analysis of genomic clones, we have determined the complete nucleotide sequence of the gene encoding triosephosphate isomerase (TIM; EC in the thermophilic bacterium, Bacillus stearothermophilus [4].
  • The enzyme has a highly conserved catalytic TIM-barrel region as previously described for Serratia marcescens ChiA [5].

High impact information on ECs4844

  • To address this question, the gene encoding a sluggish mutant triose-phosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC has been subjected to random mutagenesis over its whole length by using "spiked" oligonucleotide primers [6].
  • Amino acid sequence comparison reveals that vTIM has an alanine in loop 8 (at position 238), whereas all other TIM sequences known to date have a serine [1].
  • An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein [7].
  • Both dihydroorotases are members of the metallo-dependent hydrolase superfamily, whose members have a distorted "TIM barrel" domain containing the active site [8].
  • This structure reveals an octameric particle of 422 symmetry, with each polypeptide chain organized in a (alphabeta)(8) TIM-like barrel catalytic domain attached to a U-shaped beta-sandwich domain [9].

Chemical compound and disease context of ECs4844


Biological context of ECs4844


Associations of ECs4844 with chemical compounds

  • Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein [15].
  • Paradoxically, P. vittata TPI activity was not more resistant to inhibition by arsenate in vitro than its bacterial counterpart suggesting that arsenate resistance of conventional TPI reaction was not the basis for the cellular arsenate resistance [11].
  • Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes [16].
  • P. vittata TPI activity was inhibited by incubation with reduced glutathione while bacterial TPI was unaffected [11].
  • We have predicted mutations that introduce triose phosphate isomerase activity into ribose-binding protein, a receptor that normally lacks enzyme activity [17].

Other interactions of ECs4844


Analytical, diagnostic and therapeutic context of ECs4844

  • The high representation of the TIM barrel as a scaffold for enzymatic proteins makes it an interesting model for protein engineering [20].


  1. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. Alvarez, M., Zeelen, J.P., Mainfroid, V., Rentier-Delrue, F., Martial, J.A., Wyns, L., Wierenga, R.K., Maes, D. J. Biol. Chem. (1998) [Pubmed]
  2. Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry. Rojsajjakul, T., Wintrode, P., Vadrevu, R., Robert Matthews, C., Smith, D.L. J. Mol. Biol. (2004) [Pubmed]
  3. Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape. Finke, J.M., Onuchic, J.N. Biophys. J. (2005) [Pubmed]
  4. Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus. Rentier-Delrue, F., Moyens, S., Lion, M., Martial, J.A. Gene (1993) [Pubmed]
  5. An endochitinase A from Vibrio carchariae: cloning, expression, mass and sequence analyses, and chitin hydrolysis. Suginta, W., Vongsuwan, A., Songsiriritthigul, C., Prinz, H., Estibeiro, P., Duncan, R.R., Svasti, J., Fothergill-Gilmore, L.A. Arch. Biochem. Biophys. (2004) [Pubmed]
  6. Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme. Hermes, J.D., Blacklow, S.C., Knowles, J.R. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  7. An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein. Wintrode, P.L., Rojsajjakul, T., Vadrevu, R., Matthews, C.R., Smith, D.L. J. Mol. Biol. (2005) [Pubmed]
  8. The crystal structure of a novel, latent dihydroorotase from Aquifex aeolicus at 1.7A resolution. Martin, P.D., Purcarea, C., Zhang, P., Vaishnav, A., Sadecki, S., Guy-Evans, H.I., Evans, D.R., Edwards, B.F. J. Mol. Biol. (2005) [Pubmed]
  9. X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases. Jozic, D., Kaiser, J.T., Huber, R., Bode, W., Maskos, K. J. Mol. Biol. (2003) [Pubmed]
  10. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Gualfetti, P.J., Iwakura, M., Lee, J.C., Kihara, H., Bilsel, O., Zitzewitz, J.A., Matthews, C.R. Biochemistry (1999) [Pubmed]
  11. Arsenic resistance in Pteris vittata L.: identification of a cytosolic triosephosphate isomerase based on cDNA expression cloning in Escherichia coli. Rathinasabapathi, B., Wu, S., Sundaram, S., Rivoal, J., Srivastava, M., Ma, L.Q. Plant Mol. Biol. (2006) [Pubmed]
  12. Discovery and investigation of a new, second triose phosphate isomerase in Klebsiella pneumoniae. Zheng, P., Sun, J., van den Heuvel, J., Zeng, A.P. J. Biotechnol. (2006) [Pubmed]
  13. Detection of ticarcillin-clavulonic acid susceptibility with microdilution method in Citrobacter, Hafnia, Proteus and some gram negative bacteria. Uraz, G., Oncül, O. Drug metabolism and drug interactions. (2004) [Pubmed]
  14. Identification of Mycoplasma pirum genes involved in the salvage pathways for nucleosides. Tham, T.N., Ferris, S., Kovacic, R., Montagnier, L., Blanchard, A. J. Bacteriol. (1993) [Pubmed]
  15. Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein. Wu, Y., Matthews, C.R. J. Mol. Biol. (2003) [Pubmed]
  16. Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes. Stehlin, C., Dahm, A., Kirschner, K. FEBS Lett. (1997) [Pubmed]
  17. Computational design of a biologically active enzyme. Dwyer, M.A., Looger, L.L., Hellinga, H.W. Science (2004) [Pubmed]
  18. Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. Leyva-Vazquez, M.A., Setlow, P. J. Bacteriol. (1994) [Pubmed]
  19. The association between a negatively charged ligand and the electronegative binding pocket of its receptor. Huang, H.C., Briggs, J.M. Biopolymers (2002) [Pubmed]
  20. In vivo fragment complementation of a (beta/alpha)(8) barrel protein: generation of variability by recombination. Soberón, X., Fuentes-Gallego, P., Saab-Rincón, G. FEBS Lett. (2004) [Pubmed]
WikiGenes - Universities