ENO1/YGR254W Summary Help

Standard Name ENO1
Systematic Name YGR254W
Alias HSP48
Feature Type ORF, Verified
Description Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description ENO1
Gene Product Alias enolase 1
Chromosomal Location
ChrVII:1000927 to 1002240 | ORF Map | GBrowse
Gene Ontology Annotations All ENO1 GO evidence and references
  View Computational GO annotations for ENO1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 27 genes
Classical genetics
Large-scale survey
80 total interaction(s) for 56 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 34
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 5
  • Co-crystal Structure: 5
  • Co-purification: 1
  • PCA: 2
  • Protein-RNA: 1
  • Reconstituted Complex: 2

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 11
  • Positive Genetic: 8
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 3

Expression Summary
Length (a.a.) 437
Molecular Weight (Da) 46,816
Isoelectric Point (pI) 6.6
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:1000927 to 1002240 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1314 1000927..1002240 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003486

ENO1 and ENO2 are the two S. cerevisiae genes encoding phosphopyruvate hydratase, which catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis. The enolase enzymes function as dimeric phosphopyruvate hydratase complexes (1). Replacement of His373 with asparagine (H373N enolase) or phenylalanine (H373F enolase) reduces enzymatic activity of Eno1p to ca. 10% and 0.0003% of its native enzyme activity, respectively (6).

Log phase cells grown on glucose contain 20-fold more Eno2p than Eno1p, whereas cells grown on ethanol or glycerol plus lactate contain similar amounts of both proteins (1). Enolase catalyses the first common step of glycolysis and gluconeogenesis. During gluconeogenesis, ENO1 and ENO2 catalyze the reverse reaction --- the synthesis of phosphoenolpyruvate from 2-phosphoglycerate (7, ,8, 9). This reaction is important for growth on non-sugar carbon sources like ethanol, glycerol, or peptone, when the gluconeogenesis pathway is used to synthesize glucose.

The reactions of gluconeogenesis, shown here, mediate conversion of pyruvate to glucose, which is the opposite of glycolysis, the formation of pyruvate from glucose. While these two pathways have several reactions in common, they are not the exact reverse of each other. As the glycolytic enzymes phosphofructokinase (Pfk1p, Pfk2p) and pyruvate kinase (Cdc19p) only function in the forward direction, the gluconeogenesis pathway replaces those steps with the enzymes pyruvate carboxylase (Pyc1p, Pyc2p) and phosphoenolpyruvate carboxykinase (Pck1p) -generating oxaloacetate as an intermediate from pyruvate to phosphoenolpyruvate- and also the enzyme fructose-1,6-bisphosphatase (Fbp1p) (reviewed in 10). Overall, the gluconeogenic reactions convert two molecules of pyruvate to a molecule of glucose, with the expenditure of six high-energy phosphate bonds, four from ATP and two from GTP.

Last updated: 2005-07-05 Contact SGD

References cited on this page View Complete Literature Guide for ENO1
1) McAlister L and Holland MJ  (1982) Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes. J Biol Chem 257(12):7181-8
2) Entian KD, et al.  (1987) Studies on the regulation of enolases and compartmentation of cytosolic enzymes in Saccharomyces cerevisiae. Biochim Biophys Acta 923(2):214-21
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
5) Foyn H, et al.  (2013) Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12(1):42-54
6) Brewer JM, et al.  (1997) Effect of site-directed mutagenesis of His373 of yeast enolase on some of its physical and enzymatic properties. Biochim Biophys Acta 1340(1):88-96
7) Cohen R, et al.  (1987) Transcription of the constitutively expressed yeast enolase gene ENO1 is mediated by positive and negative cis-acting regulatory sequences. Mol Cell Biol 7(8):2753-61
8) Wold F and Ballou CE  (1957) Studies on the enzyme enolase. I. Equilibrium studies. J Biol Chem 227(1):301-12
9) Wold F and Ballou CE  (1957) Studies on the enzyme enolase. II. Kinetic studies. J Biol Chem 227(1):313-28
10) Klein CJ, et al.  (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1)():13-24