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Literature summary for 3.4.24.16 extracted from
- Neurolysin from initial detection to latest advances (2018), Neurochem. Res., 43, 2017-2024 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene NLN | Rattus norvegicus |
| gene NLN | Mus musculus |
| gene NLN | Homo sapiens |
| gene NLN | Sus scrofa |
| gene NLN | Bos taurus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of Nln knockout C57BL6 | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Mcc-Pro-Leu | Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers product inhibition | Bos taurus |  |
| Mcc-Pro-Leu | Nln-mediated hydrolysis of QFS yields a degradation product that triggers a relatively product inhibition | Homo sapiens | |
| Mcc-Pro-Leu | Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers a product inhibition | Mus musculus | |
| Mcc-Pro-Leu | Nln-mediated hydrolysis of QFS yields a degradation product that triggers a relatively product inhibition | Rattus norvegicus | |
| Mcc-Pro-Leu | Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers a relatively product inhibition | Sus scrofa | |
| additional information | Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin | Bos taurus | |
| additional information | Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin | Homo sapiens | |
| additional information | Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin | Mus musculus | |
| additional information | Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin | Rattus norvegicus | |
| additional information | Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin | Sus scrofa | |
| Pro-Ile | - |
Bos taurus | |
| Pro-Ile | - |
Homo sapiens | |
| Pro-Ile | - |
Mus musculus | |
| Pro-Ile | - |
Rattus norvegicus | |
| Pro-Ile | - |
Sus scrofa | |
| Pro-L-PhePsi(PO2CH2)Gly-Pro | - |
Bos taurus | |
| Pro-L-PhePsi(PO2CH2)Gly-Pro | - |
Homo sapiens | |
| Pro-L-PhePsi(PO2CH2)Gly-Pro | - |
Mus musculus | |
| Pro-L-PhePsi(PO2CH2)Gly-Pro | - |
Rattus norvegicus | |
| Pro-L-PhePsi(PO2CH2)Gly-Pro | - |
Sus scrofa | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Mus musculus | 16020 | - |
| membrane | - |
Homo sapiens | 16020 | - |
| membrane | - |
Sus scrofa | 16020 | - |
| membrane | - |
Bos taurus | 16020 | - |
| mitochondrion | - |
Rattus norvegicus | 5739 | - |
| mitochondrion | - |
Mus musculus | 5739 | - |
| mitochondrion | - |
Homo sapiens | 5739 | - |
| mitochondrion | - |
Sus scrofa | 5739 | - |
| mitochondrion | - |
Bos taurus | 5739 | - |
| plasma membrane | - |
Rattus norvegicus | 5886 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | zinc metallopeptidase | Rattus norvegicus | |
| Zn2+ | zinc metallopeptidase | Mus musculus | |
| Zn2+ | zinc metallopeptidase | Homo sapiens | |
| Zn2+ | zinc metallopeptidase | Sus scrofa | |
| Zn2+ | zinc metallopeptidase | Bos taurus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GlpLYENKPRRPYIL + H2O | Homo sapiens | neurotensin, secreted human neuropeptide | GlpLYENKPRRP + YIL | - |
? | |
| additional information | Mus musculus | Nln hydrolyses several substrates that are affected by brain injury | ? | - |
? | |
| additional information | Mus musculus C57BL6 | Nln hydrolyses several substrates that are affected by brain injury | ? | - |
? | |
| neurotensin + H2O | Rattus norvegicus | secreted neuropeptide | ? | - |
? | |
| neurotensin + H2O | Mus musculus | secreted neuropeptide | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | Sus scrofa | secreted neuropeptide | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | Bos taurus | secreted neuropeptide | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | Mus musculus C57BL6 | secreted neuropeptide | GlpLYENKPRRP + YIL | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | A2VDQ5 | - |
- |
| Homo sapiens | Q9BYT8 | - |
- |
| Mus musculus | Q91YP2 | - |
- |
| Mus musculus C57BL6 | Q91YP2 | - |
- |
| Rattus norvegicus | P42676 | - |
- |
| Sus scrofa | Q02038 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| B16F10-Nex2 cell | - |
Mus musculus | - |
| brain | - |
Rattus norvegicus | - |
| brain | - |
Mus musculus | - |
| brain | - |
Homo sapiens | - |
| brain | - |
Sus scrofa | - |
| brain | - |
Bos taurus | - |
| gastric fundus | - |
Rattus norvegicus | - |
| gastric smooth muscle | - |
Rattus norvegicus | - |
| gastrointestinal tract | - |
Rattus norvegicus | - |
| gastrointestinal tract | - |
Mus musculus | - |
| gastrointestinal tract | - |
Sus scrofa | - |
| ileum | - |
Rattus norvegicus | - |
| intestine | - |
Homo sapiens | - |
| intestine | - |
Bos taurus | - |
| melanoma cell | - |
Mus musculus | - |
| additional information | membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke | Mus musculus | - |
| N1E-115 cell | - |
Mus musculus | - |
| neuron | primary cultured cells | Rattus norvegicus | - |
| neuron | primary cultured cells | Mus musculus | - |
| neuron | primary cultured cells | Homo sapiens | - |
| neuron | primary cultured cells | Sus scrofa | - |
| neuron | primary cultured cells | Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GlpLYENKPRRPYIL + H2O | neurotensin, secreted human neuropeptide | Homo sapiens | GlpLYENKPRRP + YIL | - |
? | |
| GlpLYENKPRRPYIL + H2O | neurotensin, secreted human neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond | Homo sapiens | GlpLYENKPRRP + YIL | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | - |
Mus musculus | ? | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | - |
Sus scrofa | ? | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | - |
Bos taurus | ? | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | substrate QFS | Rattus norvegicus | ? | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | substrate QFS | Homo sapiens | ? | - |
? | |
| Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | - |
Mus musculus C57BL6 | ? | - |
? | |
| additional information | Nln hydrolyses several substrates that are affected by brain injury | Mus musculus | ? | - |
? | |
| additional information | Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln | Sus scrofa | ? | - |
? | |
| additional information | Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln | Bos taurus | ? | - |
? | |
| additional information | Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln. Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp is particularly useful to study Nln distribution and ontogeny in murine brain | Mus musculus | ? | - |
? | |
| additional information | QFS and neurotensin compete for their hydrolysis by enzyme Nln | Rattus norvegicus | ? | - |
? | |
| additional information | QFS and neurotensin compete for their hydrolysis by enzyme Nln | Homo sapiens | ? | - |
? | |
| additional information | Nln hydrolyses several substrates that are affected by brain injury | Mus musculus C57BL6 | ? | - |
? | |
| additional information | Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln. Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp is particularly useful to study Nln distribution and ontogeny in murine brain | Mus musculus C57BL6 | ? | - |
? | |
| neurotensin + H2O | secreted neuropeptide | Rattus norvegicus | ? | - |
? | |
| neurotensin + H2O | secreted neuropeptide, major cleavage is the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond. Neurotensin in which Tyr 11 is replaced by a D-Tyr11 or D-Phe11 residue fully resists degradation both in vitro as well as in vivo, after intracerebroventricular administration in rat | Rattus norvegicus | ? | - |
? | |
| neurotensin + H2O | secreted neuropeptide | Mus musculus | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide | Sus scrofa | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide | Bos taurus | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond | Mus musculus | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond | Sus scrofa | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond | Bos taurus | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide | Mus musculus C57BL6 | GlpLYENKPRRP + YIL | - |
? | |
| neurotensin + H2O | secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond | Mus musculus C57BL6 | GlpLYENKPRRP + YIL | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endopeptidase 3.4.24.16 | - |
Rattus norvegicus |
| endopeptidase 3.4.24.16 | - |
Mus musculus |
| endopeptidase 3.4.24.16 | - |
Homo sapiens |
| endopeptidase 3.4.24.16 | - |
Sus scrofa |
| endopeptidase 3.4.24.16 | - |
Bos taurus |
| neurotensin-cleaving enzyme | - |
Rattus norvegicus |
| neurotensin-cleaving enzyme | - |
Mus musculus |
| neurotensin-cleaving enzyme | - |
Homo sapiens |
| neurotensin-cleaving enzyme | - |
Sus scrofa |
| neurotensin-cleaving enzyme | - |
Bos taurus |
| Nln | - |
Rattus norvegicus |
| Nln | - |
Mus musculus |
| Nln | - |
Homo sapiens |
| Nln | - |
Sus scrofa |
| Nln | - |
Bos taurus |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Mus musculus | membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the M3 metallopeptidase family | Rattus norvegicus |
| evolution | the enzyme belongs to the M3 metallopeptidase family | Mus musculus |
| evolution | the enzyme belongs to the M3 metallopeptidase family | Homo sapiens |
| evolution | the enzyme belongs to the M3 metallopeptidase family | Sus scrofa |
| evolution | the enzyme belongs to the M3 metallopeptidase family | Bos taurus |
| physiological function | Nln secreted from B16F10-Nex2 melanoma cells might be able control angiogenesis. Nln hydrolyses several substrates that are affected by brain injury | Mus musculus |
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Release 2023.1 (January 2023)
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