Cloned (Comment) | Organism |
---|---|
expression of procaspase-2 in Escherichia coli strain BL21(DE3) | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
NaCl | activates at 50 mM, the enzyme is stable until 150 mM NaCl | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
procaspase-7 + H2O | Homo sapiens | activation | caspase-7 + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant procaspase-2 from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography to over 95% | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
strict requirement for an Asp residue at P1, with Asp316 being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-/- | catalysis is mediated by a mechanism involving a catalytic dyad composed of a cysteine residue as the catalytic nucleophile and a histidine residue | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
neuroblastoma cell | - |
Homo sapiens | - |
SK-N-BE(2) cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
procaspase-7 + H2O | activation | Homo sapiens | caspase-7 + ? | - |
? | |
procaspase-7 + H2O | activation by cleavage at Asp198 and Asp206 | Homo sapiens | caspase-7 + ? | - |
? | |
VDVAD-7-amido-4-methylcoumarin + H2O | - |
Homo sapiens | VDVAD + 7-amino-4-methylcoumarin | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7.2 | - |
Homo sapiens |