Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the membrane-associated enzyme form increases during neuronal differentation and appears to be responsible for the overall augmentation of endopeptidase activity observed during neuronal maturation | Mus musculus | 16020 | - |
soluble | the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin | Mus musculus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin. The neuronal membrane-associated activity would be responsible for the physiological inactivation of the peptide either in the synaptic cleft, beside the neurotensin receptors, or inside early endosomal compartments in which receptor-ligand complexes would have been internalized | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
astrocyte | contain only soluble enzyme | Mus musculus | - |
neuron | contains both soluble and membrane-associated enzyme | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin. The neuronal membrane-associated activity would be responsible for the physiological inactivation of the peptide either in the synaptic cleft, beside the neurotensin receptors, or inside early endosomal compartments in which receptor-ligand complexes would have been internalized | Mus musculus | ? | - |
? |