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InterPro: IPR020809 Enolase, conserved site
Protein matches
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UniProtKB Matches: 2582 proteins |
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Accession
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IPR020809 Enolase_CS |
Type
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Conserved_site |
Signatures
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InterPro Relationships
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Found in
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IPR000941 Enolase
IPR020810 Enolase, C-terminal
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GO Term annotation
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Process
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GO:0006096 glycolysis
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Function
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GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
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Component
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GO:0000015 phosphopyruvate hydratase complex
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Enolase (2-phospho-D-glycerate hydrolase) is an essential glycolytic enzyme that catalyses the interconversion of 2-phosphoglycerate and phosphoenolpyruvate [1, 2]. In vertebrates, there are 3 different, tissue-specific isoenzymes, designated alpha, beta and gamma. Alpha is present in most tissues, beta is localised in muscle tissue, and gamma is found only in nervous tissue. The functional
enzyme exists as a dimer of any 2 isoforms. In immature organs and in adult liver, it is usually an alpha homodimer, in adult skeletal muscle, a beta homodimer, and in adult neurons, a gamma homodimer. In developing muscle, it is usually an alpha/beta heterodimer, and in the developing nervous system, an
alpha/gamma heterodimer [3]. The tissue specific forms display minor kinetic differences. Tau-crystallin, one of the major lens proteins in some fish, reptiles and birds, has been shown [4] to be evolutionary related to enolase.
Neuron-specific enolase is released in a variety of neurological diseases, such as multiple sclerosis and after seizures or acute stroke. Several tumour cells have also been found positive for neuron-specific enolase. Beta-enolase deficiency is associated with glycogenosis type XIII defect.
The signature pattern for this entry is a conserved region located in the C-terminal third of the sequence.
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Structural links
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Database links
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Additional Reading
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de A S Navarro MV, Gomes Dias SM, Mello LV, da Silva Giotto MT, Gavalda S, Blonski C, Garratt RC, Rigden DJ.
Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics.
FEBS J. 274 2007 5077-89
[PubMed: 17822439]
http://dx.doi.org/10.1111/j.1742-4658.2007.06027.x
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Chandran V, Luisi BF.
Recognition of enolase in the Escherichia coli RNA degradosome.
J. Mol. Biol. 358 2006 8-15
[PubMed: 16516921]
http://dx.doi.org/10.1016/j.jmb.2006.02.012
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Qin J, Chai G, Brewer JM, Lovelace LL, Lebioda L.
Fluoride inhibition of enolase: crystal structure and thermodynamics.
Biochemistry 45 2006 793-800
[PubMed: 16411755]
http://dx.doi.org/10.1021/bi051558s
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Chai G, Brewer JM, Lovelace LL, Aoki T, Minor W, Lebioda L.
Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase.
J. Mol. Biol. 341 2004 1015-21
[PubMed: 15289101]
http://dx.doi.org/10.1016/j.jmb.2004.05.068
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Sims PA, Menefee AL, Larsen TM, Mansoorabadi SO, Reed GH.
Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit.
J. Mol. Biol. 355 2006 422-31
[PubMed: 16309698]
http://dx.doi.org/10.1016/j.jmb.2005.10.050
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Lebioda L, Stec B, Brewer JM.
The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology.
J. Biol. Chem. 264 1989 3685-93
[PubMed: 2645275]
http://intl.jbc.org/cgi/reprint/264/7/3685.pdf
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InterPro 23.1
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