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Gene Review

ENO1  -  phosphopyruvate hydratase ENO1

Saccharomyces cerevisiae S288c

Synonyms: 2-phospho-D-glycerate hydro-lyase 1, 2-phosphoglycerate dehydratase 1, ENOA, Enolase 1, G9160, ...
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Disease relevance of ENO1


High impact information on ENO1

  • Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor [1].
  • A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae [6].
  • 9. The dissociation of enolase appears to take place over a significantly smaller range (1.7 units), and dansyl conjugates of enolase show an even narrower range (0.9 unit) [7].
  • Cells expressing a 10-fold excess of RAD52 mRNA from the ENO1 promoter are no more resistant to MMS than are wild-type cells [8].
  • Binding sites for three distinct proteins were mapped within the upstream activation sites (UAS) of the yeast enolase genes ENO1 and ENO2 [9].

Chemical compound and disease context of ENO1


Biological context of ENO1

  • A complex positive regulatory region was located 445 base pairs (bp) upstream from the transcriptional initiation site which was required for ENO1 expression in cells grown on glycolytic or gluconeogenic carbon sources [12].
  • There are two enolase genes, ENO1 and ENO2, per haploid yeast genome [12].
  • Cis-acting sequences that modulate ENO1 URS (upstream repression site) element activity were identified by base pair substitution mutagenesis [13].
  • Combining an ENO1 deletion with ENO2-deficient expression causes a more severe fragmentation phenotype [14].
  • The plasmids are suitable for studies of germ tube induction or assessing germ tube formation by measuring yEGFP3 expression, for inducible expression of genes concomitant with germ tube formation by the HWP1 promoter, for constitutive expression of genes by the ENO1 promoter, and for expressing yEGFP3 using a promoter of choice [15].

Anatomical context of ENO1

  • Either deletion of the non-essential ENO1 gene or diminished expression of the essential ENO2 gene causes vacuole fragmentation in vivo, reflecting reduced fusion [14].
  • The results of several secondary-structure prediction programs were combined to produce an estimate of the regions of alpha-helix, beta-sheet and reverse turn for both chicken skeletal-muscle and yeast enolase sequences [16].
  • Enhanced secretion of cell wall bound enolase into culture medium by the soo1-1 mutation of Saccharomyces cerevisiae [17].
  • Antibodies against yeast enolase isozyme I cross-react with Ricinus plastid enolase but not with the cytosolic isozyme [18].

Associations of ENO1 with chemical compounds


Physical interactions of ENO1

  • Sequences that overlapped the UAS1 elements of both enolase genes bound a protein which was identified as the product of the RAP1 regulatory gene [9].
  • The upstream repression sequence from the yeast enolase gene ENO1 is a complex regulatory element that binds multiple trans-acting factors including REB1 [13].

Regulatory relationships of ENO1

  • The ENO1 URS element repressed transcription of the yeast CYC1 gene when positioned between the CYC1 upstream activation sequences (UAS elements) and TATAAA boxes [23].
  • In contrast, ENO2 expression is induced more than 20-fold in cells grown on glucose as the carbon source. cis-Acting regulatory sequences were mapped within the 5'-flanking region of the constitutively expressed yeast enolase gene ENO1 [12].
  • In the pdc2 pfk1 XSP18, strain, pfk1 suppresses the loss of induction of glucose-inducible enolase 2 brought about by XSP18 but fails to rescue temperature sensitivity [24].
  • Down-regulated enolase and up-regulated fumarase in the mutant strain seemed to play a role in the improved bioconversion of erythrose-4-phosphate to erythritol compared with the wild strain [25].

Other interactions of ENO1

  • Deletion of all or a portion of these latter sequences permitted glucose-dependent induction of ENO1 expression that was quantitatively similar to that of the glucose-inducible ENO2 gene [12].
  • These latter data show that the UAS/repression site is sufficient for transcriptional activation but is not sufficient to repress transcription of the enolase genes in a gcr1 genetic background [26].
  • A binding site for the yeast REB1 protein was identified near the 5' terminus of the ENO1 URS element [13].
  • The most pronounced reduction was obtained for HXK2 and ENO1 [27].
  • We suggest the existence of multiple binding to the ENO1 UAS by at least two factors: one is the factor which we purified with a molecular mass of 32 kDa on SDS/PAGE and the other is the factor like RAP1 protein which generally recognizes the RPG-box-like sequence [28].

Analytical, diagnostic and therapeutic context of ENO1

  • We also identified the other factor specific to the ENO1 UAS which gave a single peak at a molecular mass of 120 kDa in gel filtration [28].
  • The nuclear factor which specifically binds to the upstream activation sequence (UAS) of the enolase 1 gene (ENO1) of yeast Saccharomyces cerevisiae was purified by sequence-specific affinity chromatography [28].
  • Titration of Mg2+ with enolase allows for the calculation of 1/T2 for Mg2+ bound at site I of 1510 s-1 and a quadrupolar coupling constant chi = 0.30 MHz [29].
  • Comparison of enolase enzyme activities in whole cell extracts and cell culture supernatants showed the enzyme to be located primarily within cells [30].
  • Crossreactivity of enolase of C. albicans and Saccharomyces cerevisiae was also examined by immunoblotting and immunoblot inhibition test [31].


  1. Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Lebioda, L., Stec, B. Nature (1988) [Pubmed]
  2. Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. Cooper, J.A., Esch, F.S., Taylor, S.S., Hunter, T. J. Biol. Chem. (1984) [Pubmed]
  3. Identification of Candida albicans antigens reactive with immunoglobulin E antibody of human sera. Ishiguro, A., Homma, M., Torii, S., Tanaka, K. Infect. Immun. (1992) [Pubmed]
  4. A cDNA from Schizosaccharomyces pombe encoding a putative enolase. Jackson, J.C., Lopes, J.M. Gene (1995) [Pubmed]
  5. A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis. Brown, C.K., Kuhlman, P.L., Mattingly, S., Slates, K., Calie, P.J., Farrar, W.W. J. Protein Chem. (1998) [Pubmed]
  6. A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae. Entelis, N., Brandina, I., Kamenski, P., Krasheninnikov, I.A., Martin, R.P., Tarassov, I. Genes Dev. (2006) [Pubmed]
  7. Dynamics and time-averaged chemical potential of proteins: importance in oligomer association. Xu, G., Weber, G. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  8. Effects of controlled RAD52 expression on repair and recombination in Saccharomyces cerevisiae. Dornfeld, K.J., Livingston, D.M. Mol. Cell. Biol. (1991) [Pubmed]
  9. Multiple factors bind the upstream activation sites of the yeast enolase genes ENO1 and ENO2: ABFI protein, like repressor activator protein RAP1, binds cis-acting sequences which modulate repression or activation of transcription. Brindle, P.K., Holland, J.P., Willett, C.E., Innis, M.A., Holland, M.J. Mol. Cell. Biol. (1990) [Pubmed]
  10. Reverse protonation is the key to general acid-base catalysis in enolase. Sims, P.A., Larsen, T.M., Poyner, R.R., Cleland, W.W., Reed, G.H. Biochemistry (2003) [Pubmed]
  11. Quasi-irreversible inhibition of enolase of Streptococcus mutans by fluoride. Curran, T.M., Buckley, D.H., Marquis, R.E. FEMS Microbiol. Lett. (1994) [Pubmed]
  12. Transcription of the constitutively expressed yeast enolase gene ENO1 is mediated by positive and negative cis-acting regulatory sequences. Cohen, R., Yokoi, T., Holland, J.P., Pepper, A.E., Holland, M.J. Mol. Cell. Biol. (1987) [Pubmed]
  13. The upstream repression sequence from the yeast enolase gene ENO1 is a complex regulatory element that binds multiple trans-acting factors including REB1. Carmen, A.A., Holland, M.J. J. Biol. Chem. (1994) [Pubmed]
  14. Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. Decker, B.L., Wickner, W.T. J. Biol. Chem. (2006) [Pubmed]
  15. Integrative, multifunctional plasmids for hypha-specific or constitutive expression of green fluorescent protein in Candida albicans. Staab, J.F., Bahn, Y.S., Sundstrom, P. Microbiology (Reading, Engl.) (2003) [Pubmed]
  16. The predicted secondary structure of enolase. Sawyer, L., Fothergill-Gilmore, L.A., Russell, G.A. Biochem. J. (1986) [Pubmed]
  17. Enhanced secretion of cell wall bound enolase into culture medium by the soo1-1 mutation of Saccharomyces cerevisiae. Kim, K.H., Park, H.M. J. Microbiol. (2004) [Pubmed]
  18. Enolase isozymes from Ricinus communis: partial purification and characterization of the isozymes. Miernyk, J.A., Dennis, D.T. Arch. Biochem. Biophys. (1984) [Pubmed]
  19. Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway. Norbeck, J., Blomberg, A. J. Biol. Chem. (1997) [Pubmed]
  20. Molecular cloning and characterization of the Candida albicans enolase gene. Mason, A.B., Buckley, H.R., Gorman, J.A. J. Bacteriol. (1993) [Pubmed]
  21. Analysis of expression of yeast enolase 1 gene containing a longer pyrimidine-rich region located between the TATA box and transcription start site. Jigami, Y., Toshimitsu, N., Fujisawa, H., Uemura, H., Tanaka, H., Nakasato, S. J. Biochem. (1986) [Pubmed]
  22. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. Cabiscol, E., Piulats, E., Echave, P., Herrero, E., Ros, J. J. Biol. Chem. (2000) [Pubmed]
  23. Transcriptional regulation by an upstream repression sequence from the yeast enolase gene ENO1. Carmen, A.A., Brindle, P.K., Park, C.S., Holland, M.J. Yeast (1995) [Pubmed]
  24. Suppression of pdc2 regulating pyruvate decarboxylase synthesis in yeast. Velmurugan, S., Lobo, Z., Maitra, P.K. Genetics (1997) [Pubmed]
  25. Proteomic analysis of Candida magnoliae strains by two-dimensional gel electrophoresis and mass spectrometry. Lee, D.Y., Park, Y.C., Kim, H.J., Ryu, Y.W., Seo, J.H. Proteomics (2003) [Pubmed]
  26. Sequences within an upstream activation site in the yeast enolase gene ENO2 modulate repression of ENO2 expression in strains carrying a null mutation in the positive regulatory gene GCR1. Holland, J.P., Brindle, P.K., Holland, M.J. Mol. Cell. Biol. (1990) [Pubmed]
  27. Glycolytic flux is conditionally correlated with ATP concentration in Saccharomyces cerevisiae: a chemostat study under carbon- or nitrogen-limiting conditions. Larsson, C., Nilsson, A., Blomberg, A., Gustafsson, L. J. Bacteriol. (1997) [Pubmed]
  28. Purification and characterization of a nuclear factor which binds specifically to the upstream activation sequence of Saccharomyces cerevisiae enolase 1 gene. Machida, M., Jigami, Y., Tanaka, H. Eur. J. Biochem. (1989) [Pubmed]
  29. 25Mg NMR studies of yeast enolase and rabbit muscle pyruvate kinase. Lee, M.E., Nowak, T. Arch. Biochem. Biophys. (1992) [Pubmed]
  30. A subset of proteins found in culture supernatants of Candida albicans includes the abundant, immunodominant, glycolytic enzyme enolase. Sundstrom, P., Aliaga, G.R. J. Infect. Dis. (1994) [Pubmed]
  31. Detection of IgE antibody against Candida albicans enolase and its crossreactivity to Saccharomyces cerevisiae enolase. Ito, K., Ishiguro, A., Kanbe, T., Tanaka, K., Torii, S. Clin. Exp. Allergy (1995) [Pubmed]
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