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Literature summary extracted from
- Peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders (2019), Med. Hypotheses, 131, 109309 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.24.16 | pharmacology | the ability of Nln to process several neuropeptides suggests that it could potentially serve as a single therapeutic target to modulate the function of multiple targets, the noted neuropeptide systems, critically involved in various mechanisms of brain injury or cerebroprotection/restoration | Mus musculus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.16 | cytosol | - |
Mus musculus | 5829 | - |
| 3.4.24.16 | membrane | - |
Mus musculus | 16020 | - |
| 3.4.24.16 | mitochondrion | - |
Mus musculus | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.16 | Zn2+ | zinc metalloproteinase | Mus musculus |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.16 | angiotensin II + H2O | Mus musculus | - |
? | - |
? | |
| 3.4.24.16 | bradykinin + H2O | Mus musculus | - |
? | - |
? | |
| 3.4.24.16 | additional information | Mus musculus | angiotensin I, dynorphin A(1-8) and metorphamide are no substrates of neurolysin | ? | - |
? | |
| 3.4.24.16 | neurotensin + H2O | Mus musculus | - |
? | - |
? | |
| 3.4.24.16 | Substance P + H2O | Mus musculus | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.16 | Mus musculus | Q91YP2 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.16 | brain | the enzyme is upregulated in mouse brain after stroke | Mus musculus | - |
| 3.4.24.16 | forebrain | - |
Mus musculus | - |
| 3.4.24.16 | additional information | upregulation of Nln does not appear to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic Nln to the membranes and mitochondria | Mus musculus | - |
| 3.4.24.16 | neuron | primary | Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.16 | angiotensin II + H2O | - |
Mus musculus | ? | - |
? | |
| 3.4.24.16 | bradykinin + H2O | - |
Mus musculus | ? | - |
? | |
| 3.4.24.16 | additional information | angiotensin I, dynorphin A(1-8) and metorphamide are no substrates of neurolysin | Mus musculus | ? | - |
? | |
| 3.4.24.16 | neurotensin + H2O | - |
Mus musculus | ? | - |
? | |
| 3.4.24.16 | Substance P + H2O | - |
Mus musculus | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.16 | Nln | - |
Mus musculus |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.4.24.16 | Mus musculus | the enzyme is upregulated in mouse brain after stroke. Upregulation of Nln does not appear to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic Nln to the membranes and mitochondria | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.16 | physiological function | peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders. The enzyme is linked to neuronal cell death. Significant increase (about twofold) in quantity and activity of membrane Nln in ischemia-affected parts of the mouse brain. Enzyme Nln may play a role in processes modulating the brain's response to stroke | Mus musculus |
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Release 2023.1 (January 2023)
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