Revision as of 20:35, 10 September 2011

Description: enolase, glycolytic/ gluconeogenic enzyme, universally conserved protein

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 This image was kindly provided by SubtiList

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

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:
- Inhibited by EDTA PubMed

Interactions:
- part of the RNA degradosome PubMed
- Eno-PfkA PubMed
- Eno-Rny PubMed
- Eno-CshA PubMed

Localization:
- cytoplasm PubMed
- membrane associated PubMed
- exported, this requires a long, unbent α-helix (from A108 to L126) PubMed

Database entries

Structure: 1W6T (from Streptococcus pneumoniae) PubMed

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
extensive information on the structure and enzymatic properties of Eno can be found at Proteopedia

Expression and regulation

Operon:
- cggR-gapA-pgk-tpiA-pgm-eno PubMed
- pgk-tpiA-pgm-eno PubMed

Sigma factor: SigA PubMed

Regulation:
- expression activated by glucose (3.3 fold) PubMed
- cggR: induced by glycolytic substrates CggR PubMed
- pgk: constitutive PubMed

Regulatory mechanism: transcription repression by CggR PubMed

Additional information:

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

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

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

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] [DOI] (P p)

Subcellular localization of enolase

Additional publications: PubMed

Other original publications

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)

@@ Line 1: / Line 1: @@
-Versuch
+* '''Description:''' enolase, glycolytic/ gluconeogenic enzyme, [[universally conserved protein]]<br/><br/>
+{| align="right" border="1" cellpadding="2"
+|-
+|style="background:#ABCDEF;" align="center"|'''Gene name'''
+|''eno''
+|-
+|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
+|-
+|style="background:#ABCDEF;" align="center"| '''Essential''' || no
+|-
+|style="background:#ABCDEF;" align="center"| '''Product''' || enolase
+|-
+|style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis/ gluconeogenesis
+|-
+|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Eno Eno]
+|-
+|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
+|-
+|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46,4 kDa, 4.49
+|-
+|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1290 bp, 430 amino acids
+|-
+|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvbK]]'', ''[[pgm]]''
+|-
+|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15395&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
+|-
+|colspan="2" | '''Genetic context''' <br/> [[Image:eno_context.gif]]
+ <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
+|-
+|}
+__TOC__
+<br/><br/><br/><br/><br/><br/>
+= [[Categories]] containing this gene/protein =
+{{SubtiWiki category|[[carbon core metabolism]]}},
+{{SubtiWiki category|[[membrane proteins]]}},
+{{SubtiWiki category|[[phosphoproteins]]}},
+{{SubtiWiki category|[[universally conserved proteins]]}}
+= This gene is a member of the following [[regulons]] =
+{{SubtiWiki regulon|[[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  [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
+=== Database entries ===
+* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html]
+* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10899]
+=== Additional information===
+=The protein=
+=== Basic information/ Evolution ===
+* '''Catalyzed reaction/ biological activity:''' 2-phospho-D-glycerate = phosphoenolpyruvate + H<sub>2</sub>O (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 [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
+* '''Domains:'''
+** substrate binding domain (366–369)
+* '''Modification:''' phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
+* '''Cofactor(s):''' Mg2+
+* '''Effectors of protein activity:'''
+** Inhibited by EDTA [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
+* '''[[SubtInteract|Interactions]]:'''
+** part of the [[RNA degradosome]]  {{PubMed|19193632}}
+** [[Eno]]-[[PfkA]] {{PubMed|19193632}}
+** [[Eno]]-[[Rny]] {{PubMed|19193632,21803996}}
+** [[Eno]]-[[CshA]] {{PubMed|20572937}}
+* '''[[Localization]]:'''
+** cytoplasm [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
+** membrane associated [http://www.ncbi.nlm.nih.gov/sites/entrez/18763711 PubMed]
+** exported, this requires a long, unbent α-helix (from A108 to L126)  {{PubMed|15003462,21856851}}
+=== Database entries ===
+* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1W6T 1W6T] (from ''Streptococcus pneumoniae'') {{PubMed|15476816}}
+* '''UniProt:''' [http://www.uniprot.org/uniprot/P37869 P37869]
+* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU33900]
+* '''E.C. number:''' [http://www.expasy.org/enzyme/4.2.1.11 4.2.1.11]
+=== Additional information===
+* Enolase is a [[moonlighting proteins|moonlighting protein]]. [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed]
+* There are indications that this enzyme is an octamer [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
+* [[universally conserved protein]]
+* extensive information on the structure and enzymatic properties of Eno can be found at [http://www.proteopedia.org/wiki/index.php/Enolase Proteopedia]
+=Expression and regulation=
+* '''Operon:'''
+** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
+** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
+* '''Sigma factor:''' [[SigA]] {{PubMed|11489127}}
+* '''Regulation:'''
+** expression activated by glucose (3.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+** ''[[cggR]]'': induced by glycolytic substrates [[CggR]] {{PubMed|11489127}}
+** ''[[pgk]]'': constitutive {{PubMed|11489127}}
+* '''Regulatory mechanism:''' transcription repression by [[CggR]] {{PubMed|11489127}}
+* '''Additional information:'''
+=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
+* '''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
+* '''FLAG-tag construct:''' GP1214 (spc, based on [[pGP1331]]), available in the [[Stülke]] lab
+* '''Antibody:''' available in [[Stülke]] lab
+=Labs working on this gene/protein=
+[[Stülke|Jörg Stülke]], University of Göttingen, Germany
+[http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
+=Your additional remarks=
+=References=
+==Reviews==
+<pubmed> 8994873 </pubmed>
+==Subcellular localization of enolase==
+'''Additional publications:''' {{PubMed|21856851}}
+<pubmed> 16479537 18763711 15003462 20497499 </pubmed>
+==Other original publications==
+<pubmed> 17726680, 17218307, 12850135, 19193632, 11489127, 8021172, 17505547, 25885, 20572937 15476816 9988532 ,21803996</pubmed>
+[[Category:Protein-coding genes]]

Difference between revisions of "Eno"

Revision as of 20:35, 10 September 2011

Contents

Categories containing this gene/protein

This gene is a member of the following regulons

The gene

Basic information

Phenotypes of a mutant

Database entries

Additional information

The protein

Basic information/ Evolution

Extended information on the protein

Database entries

Additional information

Expression and regulation

Biological materials

Labs working on this gene/protein

Your additional remarks

References

Reviews

Subcellular localization of enolase

Other original publications

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