Eno

• Description: enolase, glycolytic/ gluconeogenic enzyme
  
  

Gene name	eno
Synonyms
Essential	yes
Product	enolase
Function	enzyme in glycolysis/ gluconeogenesis
MW, pI	46,4 kDa, 4.49
Gene length, protein length	1290 bp, 430 amino acids
Immediate neighbours	pgm, yvgK
Gene sequence (+200bp)	Protein sequence
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 3475589 - 3476878

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O

• Protein family: enolase family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • substrate binding domain (366–369)

• Modification: phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 PubMed

• Cofactor(s): magnesium ion

• Effectors of protein activity:

• Interactions: Eno-PfkA, Eno-Rny PubMed

• Localization: cytoplasm PubMed and membrane associated PubMed

Database entries

• Structure:

• Swiss prot entry: [3]

• KEGG entry: [4]

• E.C. number: [5]

Expression and regulation

• Operon:
  • cggR-gapA-pgk-tpiA-pgm-eno
  • pgk-tpiA-pgm-eno

• Sigma factor: SigA

• Regulation:

cggR: neg. regulated by CggR PubMed, induced by sugar

pgk: constitutive PubMed

• Regulatory mechanism: transcription repression by CggR PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector: pGP563 (N-terminal His-tag, in pWH844), pGP93 (N-terminal Strep-tag, for SPINE, in pGP380), available in Stülke lab

• lacZ fusion:

• GFP fusion: pHT315-yfp-eno, available in Mijakovic lab

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody: available in Stülke lab

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

References

1. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press PubMed
2. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
3. Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
4. Leyva-Vazquez, M. A., and Setlow, P. (1994) Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J Bacteriol 176: 3903-3910. PubMed
5. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed