Difference between revisions of "Eno"
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** 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 of ''[[pgm]]'' and ''[[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 | ||
+ | ** pGP1276 (N-terminal Strep-tag, purification from ''E. coli'', in [[pGP172]]), available in [[Stülke]] lab | ||
* '''lacZ fusion:''' | * '''lacZ fusion:''' |
Revision as of 09:27, 14 February 2011
- Description: enolase, glycolytic/ gluconeogenic enzyme, universally conserved protein
Gene name | eno |
Synonyms | |
Essential | no |
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 | yvbK, pgm |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
carbon core metabolism, membrane proteins, phosphoproteins, universally conserved proteins
This gene is a member of the following regulons
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)
- Cofactor(s): Mg2+
- Effectors of protein activity:
- Inhibited by EDTA PubMed
Database entries
- UniProt: P37869
- KEGG entry: [3]
- E.C. number: 4.2.1.11
Additional information
- Enolase is a moonlighting protein. PubMed
- There are indications that this enzyme is an octamer PubMed
- universally conserved protein
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- pGP1426 (expression of eno in B. subtilis, in pBQ200), available in Stülke lab
- pGP399 (expression of eno from E. coli in B. subtilis, in pBQ200), 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
- pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
- pGP1276 (N-terminal Strep-tag, purification from E. coli, in pGP172), available in Stülke lab
- lacZ fusion:
- see pgk
- 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
Reviews
Subcellular localization of enolase
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
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)