Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9UKR0 | gene KLK12 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
endothelial cell | - |
Homo sapiens | - |
lung | lung endothelial microvascular cells | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-ISLMKYRPPGF-(3-NO2)-Tyr + H2O | very low activity | Homo sapiens | ? | - |
? | |
Abz-SPFRSSR-(3-NO2)-Tyr + H2O | low activity | Homo sapiens | ? | - |
? | |
high molecular weight kininogen + H2O | proteolysis pattern, overview. Release of bradykinin, a fragment containing the C-terminal end of kinins. The kininogenase activity of the enzyme is poor due to the resistance of hydrolysis of the K-R bond on the N-terminal side of the bradykinin sequence in the kininogen | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
kallikrein-related peptidase 12 | - |
Homo sapiens |
KLK12 | - |
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 |
---|---|---|
physiological function | proangiogenic activity of the enzyme in lung endothelial cells. The enzyme may interfere with kininostatin-related antiangiogenic activity by cleaving the D5 domain | Homo sapiens |