| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Insulin-degrading enzyme
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| http://www.biopax.org/relea... |
IDE_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
3.4.24.56,
Abeta-degrading protease,
Insulin protease,
Insulinase,
Insulysin
|
| http://www.biopax.org/relea... |
FUNCTION: Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia. CATALYTIC ACTIVITY: Degradation of insulin, glucagon and other polypeptides. No action on proteins. COFACTOR: Binds 1 zinc ion per subunit. ENZYME REGULATION: Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi. Inhibited by bacitracin. Inhibited by S-nitrosylation and oxidation agents. SUBUNIT: Homodimer. Can form higher oligomers. Interacts (via N- terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform may function as an entry receptor for this virus. SUBCELLULAR LOCATION: Cytoplasm. Cell surface. Note=Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform. PTM: The N-terminus is blocked. MISCELLANEOUS: ATP-binding induces a conformation change. SIMILARITY: Belongs to the peptidase M16 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch |