Eno

• 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: forms octamers PubMed part of the RNA degradosome PubMed Eno-PfkA PubMed, K(D) of the interaction: 40 nM PubMed Eno-Rny PubMed, K(D) of the interaction: 100 nM 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: 4A3R PubMed 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 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)