Gene name
|
eno
|
Synonyms |
|
Essential |
no
|
Product |
enolase
|
Function |
enzyme in glycolysis/ gluconeogenesis
|
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
|
Hallo
|
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
Phenotypes of a mutant
- no growth on LB, requires glucose and malate
- essential according to Kobayashi et al. on LB PubMed
Database entries
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)
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
- Effectors of protein activity:
Database entries
Additional information
Expression and regulation
- Regulatory mechanism: transcription repression by CggR PubMed
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
- 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
- GP1215 (eno-Strep (spc)), purification from B. subtilis, for SPINE, available in Stülke lab
- 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
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]
[DOI]
(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
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]
[DOI]
(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]
[DOI]
(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]
[DOI]
(P p)