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Enolase

 
Known also as: 2-phospho-D-glycerate hydro-lyase, 2-phosphoglycerate dehydratase

Known abbreviations: eno, b2779, JW2750

 

FUNCTION:
 
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation. 
 
CATALYTIC ACTIVITY:
 
2-phospho-D-glycerate = phosphoenolpyruvate + H2O. 
 
COFACTOR:
 
Magnesium. Required for catalysis and for stabilizing the dimer.
 
ENZYME REGULATION:
 
The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
 
PATHWAY:
 
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
 
SUBUNIT STRUCTURE:
 
Homodimer. Interacts with the C-terminal region of the endoribonuclease RNase E in the RNA degradosome. 
 
CELLULAR LOCALIZATION:
 
Cytoplasm › cytoskeleton. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the bacterial cell surface. 
 
POST-TRANSLATIONAL MODIFICATION:
 
Phosphorylated on serine residue(s).



This protein can be a part of a given complexes: Activities in which Enolase is involved: Pathways in which Enolase is involved:

NCBI GI number(s): 16130686
49175990
Species: Escherichia coli

Links to other databases:

Database ID Link
Uniprot P0A6P9 P0A6P9
BRENDA - -
KEGG eco:b2779 eco:b2779
PFAM: PF00113
PF03952
PF00113
PF03952
InterPro: IPR000941
IPR020810
IPR020809
IPR020811
IPR000941
IPR020810
IPR020809
IPR020811
CATH: - -
SCOP: - -
Solved crystal structures: 3H8A
2FYM
1E9I
[PDB] [details]
[PDB] [details]
[PDB] [details]


Protein sequence:
MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALE
LRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGT
ENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPM
MNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAK
GMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAAS
EFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDG
FAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLT
ETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRS
DRVAKYNQLIRIEEALGEKAPYNGRKEIKGQA

Enolase (Escherichia coli) is product of expression of eno gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The complete genome sequence of Escherichia coli K-12. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y Science 1997-09-05 (277) 9278503
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T Mol Syst Biol 2006-01-01 (2) 16738553
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y Mol Cell Proteomics 2009-01-01 (8) 18723842
Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase. Weng M, Makaroff CA, Zalkin H J Biol Chem 1986-04-25 (261) 3514618
A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Py B, Higgins CF, Krisch HM, Carpousis AJ Nature 1996-05-09 (381) 8610017
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Link AJ, Robison K, Church GM Electrophoresis 1997-08-01 (18) 9298646
Protein identification with N and C-terminal sequence tags in proteome projects. Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF J Mol Biol 1998-05-08 (278) 9600841
Phosphorylation of Escherichia coli enolase. Dannelly HK, Duclos B, Cozzone AJ, Reeves HC Biochimie 1989-01-01 (71) 2513001
Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export? Boel G, Pichereau V, Mijakovic I, Maze A, Poncet S, Gillet S, Giard JC, Hartke A, Auffray Y, Deutscher J J Mol Biol 2004-03-19 (337) 15003462
Global analysis of Escherichia coli RNA degradosome function using DNA microarrays. Bernstein JA, Lin PH, Cohen SN, Lin-Chao S Proc Natl Acad Sci U S A 2004-03-02 (101) 14981237
Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Morita T, Kawamoto H, Mizota T, Inada T, Aiba H Mol Microbiol 2004-11-01 (54) 15522087
RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. Taghbalout A, Rothfield L Proc Natl Acad Sci U S A 2007-02-01 (104) 17242352
Crystal structure of the Escherichia coli RNA degradosome component enolase. Kuhnel K, Luisi BF J Mol Biol 2001-10-26 (313) 11676541
Recognition of enolase in the Escherichia coli RNA degradosome. Chandran V, Luisi BF J Mol Biol 2006-04-21 (358) 16516921



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Last modification of this entry: Sept. 25, 2012.

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