Application | Comment | Organism |
---|---|---|
molecular biology | neurolysin can be used as a molecular tool for analysis of properties of cancer-producing matrix metalloproteinases MMP-2 and MMP-9, quantitative determination of cleavage activity of neurolysin toward MMPspecific fluorescence-quenching peptides, overview | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
expression of the FLAG-tagged brain enzyme in Saccharomyces cerevisiae strain BJ2168 on the cell surface, subcloning in Escherichia coli strain DH5alpha | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid | - |
Rattus norvegicus | |
(2R)-[(4-biphenylylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide | - |
Rattus norvegicus | |
3-(4-phenoxyphenylsulfonyl)-propylthiirane | - |
Rattus norvegicus | |
EDTA | complete inhibition at 4 mg/ml | Rattus norvegicus | |
H-Cys1-Thr-Thr-His-Trp-Gly-Phe-Thr-Leu-Cys10-OH | - |
Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Rattus norvegicus | 9986 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | dependent on, neurolysin contains a His-Glu-Xaa-Xaa-His zinc binding motif in its active domain that traps a zinc molecule using two histidine residues | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
neurotensin + H2O | Rattus norvegicus | neurolysin regulates the amount of bioactive peptide neurotensin, which functions in the modulation of central dopaminergic and cholinergic circuits, thermoregulation, intestinal motility, and blood pressure regulation. In cancer cells, neurotensin accelerates cell progression | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Rattus norvegicus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
quantitative determination of cleavage activity of neurolysin toward MMP-specific fluorescence-quenching peptides | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | residues His425, Ala426, Cys428, Pro193, Gln482, Asp410, Thr495, Leu397, and Thr471 are involved in substrate recognition, as well as the tyrosine-rich loop 604GGYDGQYYGY613, overview, poor activity with the MMP-3 substrate [(7-methoxycoumarin-4-yl)acetyl]-RPKPVENvaWRK(Dnp[2,4-dinitrophenyl])-NH2 | Rattus norvegicus | ? | - |
? | |
neurotensin + H2O | - |
Rattus norvegicus | ? | - |
? | |
neurotensin + H2O | neurolysin regulates the amount of bioactive peptide neurotensin, which functions in the modulation of central dopaminergic and cholinergic circuits, thermoregulation, intestinal motility, and blood pressure regulation. In cancer cells, neurotensin accelerates cell progression | Rattus norvegicus | ? | - |
? | |
[(7-methoxycoumarin-4-yl)acetyl]-RPKPYANvaWMK(Dnp)-NH2 + H2O | a substrate of MMP-2 and MMP-9 | Rattus norvegicus | ? | - |
? | |
[(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH + H2O | - |
Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structural comparison between neurolysin and MMP-9, overview | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
More | neurolysin belongs to the M3 metallopeptidase family | Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Rattus norvegicus |