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Literature summary for 3.4.24.81 extracted from
- Upregulation of the alpha-secretase ADAM10--risk or reason for hope? (2010), FEBS J., 277, 1585-1596.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | ADAM10 as target for Alzheimers disease therapy | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E384A | the point mutation which compromises the zinc-binding consensus motif, leads to a substantial decrease in amyloid precursor protein-alpha secretion | Mus musculus |
| E384A | the point mutation which compromises the zinc-binding consensus motif, leads to a substantial decrease in amyloid precursor protein-alpha secretion | Homo sapiens |
| N439 | mutation at the N-glycosylation site N439 increase ADAM10s susceptibility to proteolytical degradation | Homo sapiens |
| Q170H | significant evidence for an association of Alzheimers disease with the metalloproteinase with respect to two mutations: Q170H and R181G | Homo sapiens |
| R181G | significant evidence for an association of Alzheimers disease with the metalloproteinase with respect to two mutations: Q170H and R181G | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the typical multidomain structure of ADAM10 as a type I integral transmembrane protein consists of a prodomain, a catalytical domain with a conserved zinc binding sequence, a cysteine-rich disintegrin-like domain, a transmembrane domain and a rather short cytoplasmic domain | Homo sapiens | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zinc | ADAM10 belongs to the subgroup of metzincins within the zinc proteinases family | Homo sapiens |  |
| Zinc | ADAM10 belongs to the subgroup of metzincins within the zinc proteinases family. The catalytical domain of ADAM10 contains a typical zinc-binding consensus motif | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amyloid precursor protein + H2O | Mus musculus | cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity | ? | - |
? | |
| amyloid precursor protein + H2O | Homo sapiens | cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | glycosylation sites in the catalytic and disintegrin domain contain high-mannose as well as complex type N-glycans | Homo sapiens |
| proteolytic modification | the nascent protein itself is not functional and is produced as a zymogen. After cleavage of the signalling sequence, ADAM10 enters the secretory pathway to be processed and thereby activated by the proprotein convertases furin or PC7 | Mus musculus |
| proteolytic modification | the nascent protein itself is not functional and is produced as a zymogen. After cleavage of the signalling sequence, ADAM10 enters the secretory pathway to be processed and thereby activated by the proprotein convertases furin or PC7 | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HEK-293 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amyloid precursor protein + H2O | cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity | Mus musculus | ? | - |
? | |
| amyloid precursor protein + H2O | cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADAM10 | - |
Mus musculus |
| ADAM10 | - |
Homo sapiens |
| metalloproteinase 10 | - |
Mus musculus |
| metalloproteinase 10 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | mice with a dominant negative mutant of ADAM10 show lowered amounts of APPs-alpha, accompanied by an enhanced amount of plaques and learning deficiencies in the Morris water maze test | Mus musculus |
| physiological function | ADAM10 and TACE (EC 3.4.24.86) are the major sheddases that balance the beta-site amyloid precursor protein cleaving enzyme-driven generation of Abeta peptides | Mus musculus |
| physiological function | ADAM10 and TACE (EC 3.4.24.86) are the major sheddases that balance the beta-site amyloid precursor protein cleaving enzyme-driven generation of Abeta peptides. ADAM10 regulates axon withdrawal by ephrin. ADAM10 plays a role in the aetiology of Alzheimers disease | Homo sapiens |
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