ENO1/YGR254W Summary Help

ENO1 BASIC INFORMATION

Standard Name ENO1
Systematic Name YGR254W
Alias HSP48
Feature Type ORF, Verified
Description Enolase I, a phosphopyruvate hydratase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression is repressed in response to glucose (1, 2 and see Summary Paragraph)
Name Description ENO1
Gene Product Alias enolase 1
GO 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
High-throughput
Pathways
Interactions ENO1 All interactions details and references
35 total interaction(s) for 25 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 4
  • Co-crystal Structure: 5
  • Protein-RNA: 1
  • Reconstituted Complex: 1
Genetic Interactions
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 3
Sequence Information
ChrVII:1000932 to 1002245 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2005-11-29 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1314 1000932..1002245 2005-11-29 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000003486

ENO1 RESOURCES

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Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for ENO1

SUMMARY PARAGRAPH for ENO1

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 (3).

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 (4, ,5, 6). 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 7). 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: 2005-07-11

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) 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
4) 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
5) WOLD F and BALLOU CE  (1957) Studies on the enzyme enolase. I. Equilibrium studies. J Biol Chem 227(1):301-12
6) WOLD F and BALLOU CE  (1957) Studies on the enzyme enolase. II. Kinetic studies. J Biol Chem 227(1):313-28
7) Klein CJ, et al.  (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1):13-24