Difference between revisions of "Eno"

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(References)
(Phenotypes of a mutant)
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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essential  [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 12:04, 14 January 2009

  • 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
Eno context.gif




The gene

Basic information

  • Coordinates: 3475589 - 3476878

Phenotypes of a mutant

essential 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 + H(2)O
  • Protein family: enolase family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • substrate binding domain (366–369)
  • Modification: phosphorylated during sporulation
  • Cofactor(s): magnesium ion
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm.PubMed secreted. cell surface

Database entries

  • Structure:
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulation: neg. regulated by CggR PubMed, induced by sugar
  • Regulatory mechanism: repressor CggR PubMed, covalent substrate binding (Lys-339) causes inactivation, and is a possible signal for export of the protein
  • Additional information:

Biological materials

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

  1. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
  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