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Literature summary for 3.4.24.18 extracted from
- Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney (1987), Biochem. J., 241, 229-235.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,10-phenanthroline | at neutral and alkaline pH-values, reversible by dialysis | Mus musculus |  |
| EDTA | at neutral and alkaline pH-values, reversible by dialysis | Mus musculus | |
| additional information | - |
Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | intrinsic protein | Mus musculus | 16020 | - |
| membrane | renal brush border membrane | Mus musculus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Calcium | metalloendopeptidase | Mus musculus | |
| Calcium | 3 mol calcium per mol subunit (atomic absorption spectroscopy) | Mus musculus | |
| Calcium | tightly bound, no addition of Ca2+ required | Mus musculus | |
| Zinc | metalloendopeptidase | Mus musculus | |
| Zinc | 1 mol zinc per mol subunit (atomic absorption spectroscopy) | Mus musculus | |
| Zinc | tightly bound, no addition of Zn2+ required | Mus musculus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
amino acid composition | Mus musculus |
| 85000 | - |
4 * 85000, mouse | Mus musculus |
| 320000 | - |
mouse, gel filtration, SDS-PAGE in the absence of 2-mercaptoethanol | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | about 18% carbohydrates, mostly N-linked sugars | Mus musculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| angiotensin II + H2O | poor substrate | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
| angiotensin II + H2O | cleavage site: Tyr-Ile | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
| angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
| azocasein + H2O | - |
Mus musculus | fragments of azocasein | - |
? | |
| bradykinin + H2O | one cleavage site: Phe-Ser | Mus musculus | Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg | - |
? | |
| Insulin B-chain + H2O | the others are Leu6-Cys(SO3-)7, Ala14-Leu15, Gly8-Ser9, His10-Leu11, Leu15-Tyr16, His5-Leu6 and Leu17-Val18 | Mus musculus | Hydrolyzed insulin B-chain | 13 different peptide fragments | ? | |
| Insulin B-chain + H2O | oxidized form | Mus musculus | Hydrolyzed insulin B-chain | 13 different peptide fragments | ? | |
| additional information | no hydrolysis of Leu 4-nitroanilide, benzoyl-Arg-4-nitroanilide, succinyl-Ala 4-nitroanilide, Arg 4-methylcoumarinin 7-amide, benzoyl-Phe-Val-Arg 4-methylcoumarin 7-amide, Gly-Gly-Phe-Leu, Tyr-Gly-Gly-Phe-Leu, Tyr-Gly-Gly-Phe-Met, Leu-Arg-Arg-Ala-Ser-Leu-Gly, Ala-Phe-Pro-Leu-Gly-Phe, benzoyl-Phe-Val-Arg | Mus musculus | ? | - |
? | |
| additional information | hydrolyzes peptides of at least 8 amino acids and prefers peptide bonds flanked by hydrophobic or neutral amino acid residues although hydrolysis is not limited to these bonds | Mus musculus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | dimeric meprin seems to be catalytically active | Mus musculus |
| tetramer | SDS-PAGE | Mus musculus |
| tetramer | 4 * 85000, mouse | Mus musculus |
| tetramer | in the presence of 2-mercaptoethanol | Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mus musculus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
t1/2: 30 min at pH 7.5 | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pI: multiple bonds in the range of 4-5, presumably due to glycosylation | Mus musculus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
below, rapid irreversible denaturation | Mus musculus |
| 7.5 | - |
t1/2: 30 min at 60°C | Mus musculus |
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