Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | inhibits, a negative regulator of meprin beta | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Homo sapiens | 9986 | - |
membrane | meprin beta is a membrane-bound protein with a transmembrane helix and a small C-terminal cytosolic domain | Homo sapiens | 16020 | - |
additional information | meprin beta is primarily membrane-bound and forms asymmetric disulfide linked homodimer at the cell surface | Homo sapiens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc-dependent metalloprotease | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-collagen I + H2O | Homo sapiens | maturation | collagen I + collagen I propeptide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q16820 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the crystal structure of the zymogen form of meprin beta revealsthat the active side is shielded by the pro-peptide. Gln62 is directed away from the salt bridge that is formed by Glu163 and Lys248. The new N-terminus is formed by Asp62 after removal of the pro-peptide by tryptic serine protease cleavage between Arg61 and Gln62. In active meprin beta N62 forms a salt bridge with E163 and thus removes the new N-terminus from the active site, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-collagen I + H2O | maturation | Homo sapiens | collagen I + collagen I propeptide | - |
? | |
pro-collagen I + H2O | cleavage of the C-terminal pro-domain | Homo sapiens | collagen I + collagen I propeptide | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | the enzyme consists of the protease domain with a 39 amino acid long inhibitory pro-peptide, a MAM domain, a TRAF domain, an EGF-like domain, a transmembrane helix, and a small C-terminal cytosolic domain | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
meprin beta | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | ablation of one of the two zinc metalloproteinases, meprin beta and BMP-1, leads to different collagen I associated phenotypes in vivo | Homo sapiens |
metabolism | the zinc metalloproteinases meprin beta and BMP-1 are differentially regulated by CaCl2, overview | Homo sapiens |
additional information | structural differences between meprin beta and BMP-1 (EC 3.4.24.21). Molecular dynamics simulation | Homo sapiens |
physiological function | a reduction in activity is reported under increasing calcium concentrations for meprin beta | Homo sapiens |