[1]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/17.21.8862; PubMed=2587223 [NCBI, ExPASy, EBI, Israel, Japan]
Peshavaria M.,
Hinks L.J.,
Day I.N.M.;
"Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone.";
Nucleic Acids Res. 17:8862-8862(1989).
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[2]
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NUCLEOTIDE SEQUENCE.
PubMed=1840492 [NCBI, ExPASy, EBI, Israel, Japan]
Peshavaria M.,
Day I.N.M.;
"Molecular structure of the human muscle-specific enolase gene (ENO3).";
Biochem. J. 275:427-433(1991).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-85.
DOI=10.1093/nar/18.7.1893; PubMed=2336366 [NCBI, ExPASy, EBI, Israel, Japan]
Cali L.,
Feo S.,
Oliva D.,
Giallongo A.;
"Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE).";
Nucleic Acids Res. 18:1893-1893(1990).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8513787 [NCBI, ExPASy, EBI, Israel, Japan]
Giallongo A.,
Venturella S.,
Oliva D.,
Barbieri G.,
Rubino P.,
Feo S.;
"Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA.";
Eur. J. Biochem. 214:367-374(1993).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-71 AND ALA-85.
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[6]
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VARIANTS MUSCLE-SPECIFIC BETA-ENOLASE DEFICIENCY ASP-156 AND GLU-374.
DOI=10.1002/ana.1095; PubMed=11506403 [NCBI, ExPASy, EBI, Israel, Japan]
Comi G.P.,
Fortunato F.,
Lucchiari S.,
Bordoni A.,
Prelle A.,
Jann S.,
Keller A.,
Ciscato P.,
Galbiati S.,
Chiveri L.,
Torrente Y.,
Scarlato G.,
Bresolin N.;
"Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis.";
Ann. Neurol. 50:202-207(2001).
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[7]
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INTERACTION WITH PNKD.
PubMed=15188056 [NCBI, ExPASy, EBI, Israel, Japan]
Li T.-B.,
Liu X.-H.,
Feng S.,
Hu Y.,
Yang W.-X.,
Han Y.,
Wang Y.-G.,
Gong L.-M.;
"Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle.";
Acta Biochim. Biophys. Sin. 36:412-418(2004).
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- FUNCTION: Appears to have a function in striated muscle development and regeneration.
- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
- COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. Interacts with PNKD.
- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity).
- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells.
- DISEASE: Defects in ENO3 are the cause of muscle-specific enolase-beta deficiency (glycogenesis type XIII) [MIM:131370]. It is a glycogen storage myopathy which results in exercise-induced myalgias, generalized muscle weakness and fatigability. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected in patients.
- SIMILARITY: Belongs to the enolase family.
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