Cloned (Comment) | Organism |
---|---|
produced in insect cells by baculoviral expression as truncated constructs consisting of the signal sequence, pro- and catalytic domains fused to a C-terminal His6 (hexahistidine) tag (residues 1460 of mouse ADAM10). | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | peptide libraries are used to define the cleavage site selectivity of TACE (EC 3.4.24.86) and ADAM10. The two proteases have distinct primary sequence requirements at multiple positions surrounding the cleavage site in their substrates, which allows to generate peptide substrates that are highly specific for each of these proteases. The major difference between the two protease specificities maps to the P1' position (immediately downstream of the cleavage site) of the substrate. At this position, TACE is selective for smaller aliphatic residues, whereas ADAM10 can accommodate aromatic amino acids. Using mutagenesis three residues in the S1' pockets of these enzymes are identified that dramatically influence specificity for both peptide and protein substrates | Mus musculus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADAM10 | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
physiological function | ADAM10 is a primary enzymes responsible for catalysing release of membrane-anchored proteins from the cell surface in metazoan organisms | Mus musculus |