Difference between revisions of "Eno"

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* '''Mutant:'''  
 
* '''Mutant:'''  
** GP594 (''eno''::''cat''), available in [[Jörg Stülke]]'s lab  
+
** GP594 (''eno''::''cat''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
** GP599 (''eno''::''erm''), available in [[Jörg Stülke]]'s lab  
+
** GP599 (''eno''::''erm''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
** GP698 (''eno''-''[[pgm]]''::''cat''), available in [[Jörg Stülke]]'s lab
+
** GP698 (''eno''-''[[pgm]]''::''cat''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  
Line 182: Line 182:
 
<pubmed> 8994873 </pubmed>
 
<pubmed> 8994873 </pubmed>
 
==Subcellular localization of enolase==
 
==Subcellular localization of enolase==
'''Additional publications:''' {{PubMed|15003462,21856851}}
+
<pubmed> 16479537 18763711 20497499 15003462,21856851</pubmed>
<pubmed> 16479537 18763711 20497499 </pubmed>
 
  
 
==Other original publications==
 
==Other original publications==

Revision as of 16:59, 13 July 2013

Gene name eno
Synonyms
Essential Yes (PubMed)
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
Sequences Protein DNA DNA_with_flanks
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, essential genes, 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

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

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

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


Other original publications

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Joseph A Newman, Lorraine Hewitt, Cecilia Rodrigues, Alexandra S Solovyova, Colin R Harwood, Richard J Lewis
Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome.
J. Mol. Biol.: 2012, 416(1);121-36
[PubMed:22198292] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J. Bacteriol.: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol. Microbiol.: 2010, 77(4);958-71
[PubMed:20572937] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol. Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS ONE: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol. Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Stefanie Ehinger, Wolf-Dieter Schubert, Simone Bergmann, Sven Hammerschmidt, Dirk W Heinz
Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites.
J. Mol. Biol.: 2004, 343(4);997-1005
[PubMed:15476816] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab. Eng.: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol. Microbiol.: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

C K Brown, P L Kuhlman, S Mattingly, K Slates, P J Calie, W W Farrar
A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis.
J. Protein Chem.: 1998, 17(8);855-66
[PubMed:9988532] [WorldCat.org] (P p)

M A Leyva-Vazquez, P Setlow
Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.
J. Bacteriol.: 1994, 176(13);3903-10
[PubMed:8021172] [WorldCat.org] [DOI] (P p)

R P Singh, P Setlow
Enolase from spores and cells of Bacillus megaterium: two-step purification of the enzyme and some of its properties.
J. Bacteriol.: 1978, 134(1);353-5
[PubMed:25885] [WorldCat.org] (P p)