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Gene Review

tpiA  -  triosephosphate isomerase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3911, JW3890, tpi
 
 
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Disease relevance of tpiA

 

High impact information on tpiA

  • Here, we provide evidence that a nonsense codon at position 1, 2 or 10 reduces the abundance of nucleus-associated TPI mRNA to an average of only 84% of normal because translation reinitiates at the methionine codon at position 14 [6].
  • These and related findings lend credence to the concept that the nonsense-mediated reduction in the half-life of nucleus-associated TPI mRNA involves cytoplasmic ribosomes [6].
  • A comparison of the amino acid sequence of both the PGK and the TIM parts of the fusion protein with those of known PGKs and TIMs reveals high similarity to the corresponding enzymes from different procaryotic and eucaryotic organisms [3].
  • The corresponding pgk and tpi genes are part of the apparent gap operon of T. maritima [3].
  • Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme [7].
 

Chemical compound and disease context of tpiA

  • An E. coli TIM crystal grown in the absence of 2PG, diffracting to 2.6 A resolution, was later obtained by application of the technique of macro-seeding using a seed crystal grown from a mother liquor without 2PG [8].
  • This is consistent with the hypothesis that PV4-8 TPI increased arsenate resistance in E. coli by directly or indirectly functioning as an arsenate reductase [9].
  • Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein [10].
  • Four proteins (triosephosphate isomerase, alpha galactosidase, Hsp90, and glucosamine 6-phosphate synthase) constitute the majority of E. coli proteins that bind and potentially may coelute during chromatography [11].
 

Biological context of tpiA

  • The amino acid sequences of the three enzymes show up to 62% (GAPDH), 48% (PGK), and 44% (TPI) identity in comparison with respective enzymes from other organisms [12].
  • The three additional genes found on the 4.5-kb DNA fragment encoded for proteins involved in aromatic amino acid biosynthesis (aroA), DNA bending (himD), and carbohydrate metabolism (tpiA) [13].
  • Sequence analysis of the chromosomal region flanking the Tn5 within KW239 revealed strong similarities to a number of known Escherichia coli gene products and DNA sequences: the nusA operon, including the complete initiator tRNA(Met) gene, metY; a tRNA(Leu) gene; the tpiA gene product; and the MrsA protein [14].
  • We have determined the sequence requirements for the N-terminal protein hinge of the active-site lid of triosephosphate isomerase [15].
  • Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase [16].
 

Associations of tpiA with chemical compounds

  • Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism [17].
  • Each of the second-site mutations increases the specific catalytic activity of a triosephosphate isomerase in which the catalytic base, glutamate-165, has been changed to aspartate [16].
  • The essential catalytic base at the active site of the glycolytic enzyme triosephosphate isomerase is the carboxylate group of Glu-165, which directly abstracts either the 1-pro-R proton of dihydroxyacetone phosphate or the 2-proton of (R)-glyceraldehyde 3-phosphate to yield the cis-enediol intermediate [18].
  • Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate [18].
  • We have replaced asparagine residues at the subunit interface of yeast triosephosphate isomerase (TIM) using site-directed mutagenesis in order to elucidate the effects of substitutions on the catalytic activity and conformational stability of the enzyme [19].
 

Other interactions of tpiA

  • The secG gene, downstream tpiA, does not make part of this polygenic organization, being actively transcribed as a monocistronic mRNA during transition to the stationary phase of growth [20].
 

Analytical, diagnostic and therapeutic context of tpiA

  • Protein engineering on trypanosomal triosephosphate isomerase (TIM) converted this oligomeric enzyme into a stable, monomeric protein that is enzymatically active [21].
  • Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme [19].
  • Sedimentation equilibrium ultracentrifugation runs showed that RE-TIM is a monomer in solution [22].
  • Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase [23].
  • This sequence, and that of a region conserved in all known bacterial triosephosphate isomerases, was used to design oligonucleotide primers for the synthesis of a lactococcal tpi probe by PCR [5].

References

  1. Application of hybrid plasmids carrying glycolysis genes to ATP production by Escherichia coli. Shimosaka, M., Fukuda, Y., Murata, K., Kimura, A. J. Bacteriol. (1982) [Pubmed]
  2. Transcriptional analysis of the gap-pgk-tpi-ppc gene cluster of Corynebacterium glutamicum. Schwinde, J.W., Thum-Schmitz, N., Eikmanns, B.J., Sahm, H. J. Bacteriol. (1993) [Pubmed]
  3. Phosphoglycerate kinase and triosephosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex. Schurig, H., Beaucamp, N., Ostendorp, R., Jaenicke, R., Adler, E., Knowles, J.R. EMBO J. (1995) [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. The Lactococcus lactis triosephosphate isomerase gene, tpi, is monocistronic. Cancilla, M.R., Davidson, B.E., Hillier, A.J., Nguyen, N.Y., Thompson, J. Microbiology (Reading, Engl.) (1995) [Pubmed]
  6. Evidence that translation reinitiation abrogates nonsense-mediated mRNA decay in mammalian cells. Zhang, J., Maquat, L.E. EMBO J. (1997) [Pubmed]
  7. Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Straus, D., Raines, R., Kawashima, E., Knowles, J.R., Gilbert, W. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  8. Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution. Noble, M.E., Zeelen, J.P., Wierenga, R.K., Mainfroid, V., Goraj, K., Gohimont, A.C., Martial, J.A. Acta Crystallogr. D Biol. Crystallogr. (1993) [Pubmed]
  9. 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]
  10. Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein. Vadrevu, R., Falzone, C.J., Matthews, C.R. Protein Sci. (2003) [Pubmed]
  11. Genomic data for alternate production strategies. I. Identification of major contaminating species for Cobalt(+2) immobilized metal affinity chromatography. Cai, Y., Moore, M., Goforth, R., Henry, R., Beitle, R. Biotechnol. Bioeng. (2004) [Pubmed]
  12. Identification, sequence analysis, and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomerase. Eikmanns, B.J. J. Bacteriol. (1992) [Pubmed]
  13. Ribosomal protein S1 (RpsA) of Buchnera aphidicola, the endosymbiont of aphids: characterization of the gene and detection of the product. Clark, M.A., Baumann, L., Baumann, P., Rouhbakhsh, D. Curr. Microbiol. (1996) [Pubmed]
  14. Multiple loci of Pseudomonas syringae pv. syringae are involved in pathogenicity on bean: restoration of one lesion-deficient mutant requires two tRNA genes. Rich, J.J., Willis, D.K. J. Bacteriol. (1997) [Pubmed]
  15. The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. Xiang, J., Sun, J., Sampson, N.S. J. Mol. Biol. (2001) [Pubmed]
  16. Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. Blacklow, S.C., Liu, K.D., Knowles, J.R. Biochemistry (1991) [Pubmed]
  17. Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Nickbarg, E.B., Davenport, R.C., Petsko, G.A., Knowles, J.R. Biochemistry (1988) [Pubmed]
  18. Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate. Raines, R.T., Sutton, E.L., Straus, D.R., Gilbert, W., Knowles, J.R. Biochemistry (1986) [Pubmed]
  19. Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme. Casal, J.I., Ahern, T.J., Davenport, R.C., Petsko, G.A., Klibanov, A.M. Biochemistry (1987) [Pubmed]
  20. Chromosomal organization and transcription analysis of genes in the vicinity of Pseudomonas aeruginosa glmM gene encoding phosphoglucosamine mutase. Tavares, I.M., Leitão, J.H., Sá-Correia, I. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  21. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Borchert, T.V., Abagyan, R., Jaenicke, R., Wierenga, R.K. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  22. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. Schliebs, W., Thanki, N., Jaenicke, R., Wierenga, R.K. Biochemistry (1997) [Pubmed]
  23. Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase. Beaucamp, N., Hofmann, A., Kellerer, B., Jaenicke, R. Protein Sci. (1997) [Pubmed]
 
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