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Gene name eno
Essential no
Product enolase
Function enzyme in glycolysis/ gluconeogenesis
Gene expression levels in SubtiExpress: eno
Interactions involving this protein in SubtInteract: Eno
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 46,4 kDa, 4.49
Gene length, protein length 1290 bp, 430 amino acids
Immediate neighbours yvbK, pgm
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Eno context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Eno expression.png

Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins, universally conserved proteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

  • Locus tag: BSU33900

Phenotypes of a mutant

  • no growth on LB, requires glucose and malate
  • essential according to Kobayashi et al. on LB PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
  • Protein family: enolase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: reversible Michaelis-Menten PubMed
  • Domains:
    • substrate binding domain (366–369)
  • Modification: phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 PubMed, PubMed, PubMed
  • Cofactor(s): Mg2+
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:

Biological materials

  • Mutant:
    • GP594 (eno::cat), available in Stülke lab
    • GP599 (eno::erm), available in Stülke lab
    • GP698 (eno-pgm::cat), available in Stülke lab
    • GP1215 (eno-Strep (spc)), purification from B. subtilis, for SPINE, available in Stülke lab
  • Expression vector:
    • pGP1426 (expression of eno in B. subtilis, in pBQ200), available in Stülke lab
    • pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
    • pGP563 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP1276 (N-terminal Strep-tag, purification from E. coli, in pGP172), available in Stülke lab
    • pGP93 (N-terminal Strep-tag, purification from B. subtilis, 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
  • FLAG-tag construct: GP1214 (spc, based on pGP1331), available in the Stülke lab
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks



G H Reed, R R Poyner, T M Larsen, J E Wedekind, I Rayment
Structural and mechanistic studies of enolase.
Curr. Opin. Struct. Biol.: 1996, 6(6);736-43
[PubMed:8994873] [WorldCat.org] (P p)

Subcellular localization of enolase

Additional publications: PubMed

Carsten Jers, Malene Mejer Pedersen, Dafni Katerina Paspaliari, Wolfgang Schütz, Christina Johnsson, Boumediene Soufi, Boris Macek, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.
Mol. Microbiol.: 2010, 77(2);287-99
[PubMed:20497499] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Grégory Boël, Vianney Pichereau, Ivan Mijakovic, Alain Mazé, Sandrine Poncet, Sylvie Gillet, Jean-Christophe Giard, Axel Hartke, Yanick Auffray, Josef Deutscher
Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?
J. Mol. Biol.: 2004, 337(2);485-96
[PubMed:15003462] [WorldCat.org] [DOI] (P p)

Other original publications