Difference between revisions of "Eno"

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(Biological materials)
(Biological materials)
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** pGP563 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab  
 
** pGP563 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab  
 
** pGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [[SPINE]], in [[pGP380]]), available in [[Stülke]] lab  
 
** pGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [[SPINE]], in [[pGP380]]), available in [[Stülke]] lab  
pGP1500 (expression in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab
+
** pGP1500 (expression in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab
 
 
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''

Revision as of 10:42, 7 July 2009

  • Description: enolase, glycolytic/ gluconeogenic enzyme

Gene name eno
Synonyms
Essential yes
Product enolase
Function enzyme in glycolysis/ gluconeogenesis
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 pgm, yvgK
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Eno context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU33900

Phenotypes of a mutant

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:
  • Localization: cytoplasm (according to Swiss-Prot), cytoplasm PubMed and membrane associated PubMed

Database entries

  • Structure: 3ES8 (from Oceanobacillus iheyensis, complex with Mg(2+) and malate)
  • KEGG entry: [3]

Additional information

There are indications that this enzyme is an octamer PubMed

Expression and regulation

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

Biological materials

  • Mutant: GP698 (cat), available in Stülke lab
  • Expression vector:
    • pGP563 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP93 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
    • pGP1500 (expression in B. subtilis, in pBQ200), 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

Your additional remarks

References