Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space | Rattus norvegicus | 5737 | - |
extracellular | EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space | Rattus norvegicus | - |
- |
additional information | EP24.15 does not contain a membrane anchoring motif yet it is localised to the extracellular surface of the plasma membrane | Rattus norvegicus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | dependent on | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
75000 | - |
- |
Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O | Rattus norvegicus | i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(15). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide | pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ? | i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | the enzyme activity is dependent upon phosphorylation by protein kinase A on serine residue 644. Phosphorylation of this conserved site reduces enzyme affinity for binding LHRH-I | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | substrate specificity of EP24.15, overview | Rattus norvegicus | ? | - |
? | |
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O | i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 that cleaves the hormone at the fifth and sixth bond of the decapeptide (Tyr5-Gly6) to form LHRH-(15) | Rattus norvegicus | pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly | i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5) | ? | |
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O | i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(15). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide | Rattus norvegicus | pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ? | i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor | ? |
Synonyms | Comment | Organism |
---|---|---|
EP24.15 | - |
Rattus norvegicus |
metalloendopeptidase EC 3.4.24.15 | - |
Rattus norvegicus |
More | the enzyme is a Zn-dependent a thermolysin like metalloendopeptidase | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
metabolism | EP24.15 is the main enzyme of luteinizing hormone-releasing hormone, i.e. LHRH, metabolism as the prime mediator of LHRH-I degradation in both the brain and periphery | Rattus norvegicus |
physiological function | many roles of EP24.15 in the metabolism of neuropeptides and in cell regulation, overview | Rattus norvegicus |