eno [2019-05-14 15:53:18]

enolase, glycolytic/ gluconeogenic enzyme, universally conserved protein

Locus: BSU33900

Isoelectric point: 4.49

Molecular weight: 46.42 kDa

Protein length: 430 aa

Gene length: 1293 bp

Function: enzyme in glycolysis/ gluconeogenesis

Product: enolase

Essential: Yes

E.C.: 4.2.1.11

Synonyms

Genomic Context

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Categories containing this gene/protein

• Metabolism → Carbon metabolism → Carbon core metabolism → Glycolysis
• Metabolism → Carbon metabolism → Carbon core metabolism → Gluconeogenesis
• Information processing → RNA synthesis and degradation → RNases → Effectors of RNA degradation
• Groups of genes → Essential genes
• Groups of genes → Membrane proteins
• Groups of genes → Phosphoproteins → Phosphorylation on a Ser residue
• Groups of genes → Phosphoproteins → Phosphorylation on a Thr residue
• Groups of genes → Phosphoproteins → Phosphorylation on a Tyr residue
• Groups of genes → Universally conserved proteins

Gene

Coordinates: 3,476,555 3,477,847

Phenotypes of a mutant

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

The protein

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 (single member, according to UniProt)

Kinetic information

• reversible Michaelis-Menten PubMed

Domains

• substrate binding domain (366369)

Modification

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

Cofactors

• Mg2

Effectors of protein activity

• Inhibited by EDTA PubMed

Structure

• 4A3R PubMed
• 1W6T (from Streptococcus pneumoniae) PubMed

Localization

• cytoplasm PubMed
• membrane associated PubMed
• exported, this requires a long, unbent -helix (from A108 to L126) PubMed

Additional information

• Enolase is a moonlighting protein. PubMed
• There are indications that this enzyme is an octamer PubMed
• universally conserved protein
• extensive information on the structure and enzymatic properties of Eno can be found at Proteopedia
• belongs to the 100 most abundant proteins PubMed

Expression and Regulation

Operons

• Genes: cggR-gapA-pgk-tpi-pgm-eno
  Description: PubMed

  Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon

  Regulatory mechanism

  • CggR: repression, PubMed, in CggR regulon

  Regulation

  • expression induced by glycolytic intermediates (CggR) CggR PubMed
  • the mRNA is processed between cggR and gapA by RNase Y, this requires the YmcA-YlbF-YaaT complex PubMed

• Genes: pgk-tpi-pgm-eno
  Description: PubMed

Biological materials

Mutant

• GP594 (eno::cat), available in Jörg Stülke's lab, PubMed
• GP698 (eno-pgm::cat), available in Jörg Stülke's lab, PubMed

Expression vectors

• pGP1426 (expression of eno in B. subtilis, in pBQ200), available in Jörg Stülke's lab
• pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Jörg Stülke's lab
• pGP563 (N-terminal His-tag, purification from E. coli, in pWH844), available in Jörg Stülke's lab, PubMed
• pGP1276 (N-terminal Strep-tag, purification from E. coli, in pGP172), available in Jörg Stülke's lab
• pGP93 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Jörg Stülke's lab, PubMed
• GP1215 (chromosomal eno-Strep fusion, spc), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab

LacZ fusion

• see pgk

GFP fusion

• pHT315-yfp-eno, available in Mijakovic lab
• GP1700 (in pBP43), expression of eno-GFP::spc under the native promoter, available in Jörg Stülke's lab PubMed

Two-hybrid system

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

FLAG-tag construct

• GP1214 (spc, based on pGP1331), available in Jörg Stülke's lab PubMed

Antibody

• available in Jörg Stülke's lab

Labs working on this gene/protein

• Jörg Stülke, University of Göttingen, Germany Homepage

References

Reviews

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Subcellular localization of enolase

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Other original publications

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