Protein Variants | Comment | Organism |
---|---|---|
E425L | variant has an increased activity, especially at lower temperatures (25-30°C) and the highest affinity for the substrate and catalytic efficiency among all studied variants | Homo sapiens |
I373N | mutant shows a significant loss of cooperativity | Homo sapiens |
additional information | a PDZ domain deletion mutant at 37°C shows 2.0fold higher cleavage activity assayed with beta-casein than wild-type | Homo sapiens |
R337L | mutant has an increased activity at all temperatures tested, higher affinity for the substrate and a higher turnover rate | Homo sapiens |
R432L | variant has an increased activity with beta-casein and the peptide Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitro benzoic acid) at various temperatures | Homo sapiens |
V226K | variant has an increased activity with beta-casein and the peptide Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitro benzoic acid) at various temperatures | Homo sapiens |
V431D | variant has a decreased activity, especially with beta-casein | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O43464 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) + H2O | - |
Homo sapiens | ? | - |
? | |
beta-casein + H2O | - |
Homo sapiens | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | during thermal activation, the PDZ domain changes its position versus the protease domain inside a subunit, including a prominent change affecting the L3 regulatory loop of the protease domain, and also changes its interactions with the protease domain of the adjacent subunit, specifically with its L1* regulatory loop containing the active site serine. The alpha5 helix of PDZ is involved in both, the intra- and intersubunit changes of interactions and seems to play an important role in HtrA2 activation | Homo sapiens |