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Literature summary for 4.2.1.11 extracted from
- alpha-Enolase: a promising therapeutic and diagnostic tumor target (2011), FEBS J., 278, 1064-1074.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the three genes, ENO1, ENO2 and ENO3, encoding for three isoforms of the enzyme, alpha-enolase, gamma-enolase, and beta-enolase, respectively, show high sequence identity | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell surface | putative ENOA translocation mechanism, overview | Homo sapiens | 9986 | - |
| extracellular | - |
Homo sapiens | - |
- |
| additional information | in breast, lung and pancreatic neoplasia, ENOA is localized on the surface of cancer cells, whereas in melanoma and nonsmall cell lung carcinoma cells it can also be secreted by exosomes | Homo sapiens | - |
- |
| plasma membrane | - |
Homo sapiens | 5886 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256 | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
three genes, ENO1, ENO2 and ENO3 encoding for three isoforms of the enzyme, alpha-enolase, gamma-enolase, and beta-enolase, respectively | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | ENOA in tumor cells is subjected to more acetylation, methylation and phoshorylation than in normal tissues | Homo sapiens |
| phosphoprotein | - |
Homo sapiens |
| side-chain modification | acetylation, methylation | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain cancer cell | ENOA is upregulated | Homo sapiens | - |
| breast cancer cell | cell surface ENOA is enhanced | Homo sapiens | - |
| cervix cancer cell | ENOA is upregulated | Homo sapiens | - |
| colonic cancer cell | ENOA is upregulated | Homo sapiens | - |
| eye cancer cell | ENOA is upregulated | Homo sapiens | - |
| follicular thyroid carcinoma cell | - |
Homo sapiens | - |
| gastric cancer cell | ENOA is upregulated | Homo sapiens | - |
| head and neck squamous cell carcinoma cell line | ENOA is upregulated | Homo sapiens | - |
| kidney cancer cell | ENOA is upregulated | Homo sapiens | - |
| leukemia cell | ENOA is upregulated | Homo sapiens | - |
| liver cancer cell | ENOA is upregulated | Homo sapiens | - |
| lung cancer cell | ENOA is upregulated | Homo sapiens | - |
| additional information | tissue-specific expression of isozymes: ENOA is present in almost all adult tissues, beta-enolase is expressed in muscle tissues, and gamma-enolase is found in neurons and neuroendocrine tissues | Homo sapiens | - |
| ovary cancer cell | ENOA is upregulated | Homo sapiens | - |
| pancreatic cancer cell | ENOA complexes with annexin A2, cytokeratin 8 and tissue-type plasminogen activator in raft membrane fractions of pancreatic cancer cells | Homo sapiens | - |
| prostate cancer cell | ENOA is upregulated | Homo sapiens | - |
| skeletal muscle cancer cell | ENOA is upregulated | Homo sapiens | - |
| skin cancer cell | ENOA is upregulated | Homo sapiens | - |
| testicular cancer cell | ENOA is upregulated | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256 | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the monomer of ENOA consists of a smaller N-terminal domain, residues 1-133, and a larger C-terminal domain, residues 141-431 | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-enolase | - |
Homo sapiens |
| beta-enolase | - |
Homo sapiens |
| ENOA | - |
Homo sapiens |
| gamma-enolase | - |
Homo sapiens |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Homo sapiens | In human follicular thyroid carcinoma cells, retinoic acid causes a decrease in ENOA levels that coincides with their reduced motility | down |
| Homo sapiens | ENOA expression is enhanced in diverse cancer cell types, e.g. cell surface ENOA in breast cancer cells, overview | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | in tumor cells, ENOA is upregulated and supports anaerobic proliferation, cf. Warburg effect, it is expressed at the cell surface, where it promotes cancer invasion, and is subjected to a specific array of post-translational modifications, namely acetylation, methylation and phosphorylation | Homo sapiens |
| additional information | overexpression of ENOA is associated with tumor development through a process known as aerobic glycolysis or the Warburg effect. ENOA induces autoantibody production and induces a specific immune response in tumors, overview | Homo sapiens |
| physiological function | cell surface ENOA is one of the many plasminogen-binding molecules, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256. Binding with ENOA lysyl residues leads to activation of plasminogen to plasmin by the proteolytic action of either tissue-type or urokinase-type plasminogen activators, overview. ENOA takes part, together with urokinase plasminogen activator receptor, integrins and some cytoskeletal proteins, in a multiprotein complex, called metastasome, responsible for adhesion, migration and proliferation in ovarian cancer cells | Homo sapiens |
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