EC Number   |
Natural Substrates |
|---|
   3.4.21.B12 | 52 kDa prostatic acid phosphatase + H2O |
enzyme may be involved in the physiological clearance of prostatic acid phosphatase |
| 3.4.21.B12 | amelogenin + H2O |
the enzyme plays a pivotal role during dental enamel formation by degrading the major enamel protein, amelogenin, prior to the final steps of enamel hardening. KLK4 self-destructs once amelogenin is degraded. It progressively loses activity, becomes aggregated, and autofragmented when incubated without substrate in both the presence and absence of reducer. However, with non-ionic detergent present as proxy substrate, KLK4 remains active and intact throughout |
| 3.4.21.B12 | matrix metalloproteinase-1 + H2O |
the enzyme activates matrix metalloproteinase-1, a protease that promotes prostate tumor growth and metastasis. Matrix metalloproteinase-1 is produced in the tumor compartment of prostate cancer bone metastases, highlighting its accessibility to KLK4 at this site |
| 3.4.21.B12 | more |
enzyme is regulated by steroid hormones, contains androgen response elements in the proximal promotor region |
| 3.4.21.B12 | more |
enzyme participates in the degradation of enamel proteins in vivo |
| 3.4.21.B12 | more |
enzyme is involved in tissue remodeling and cancer metastasis |
| 3.4.21.B12 | more |
enzyme modulates the tumor-associated urokinase-type plasminogen activator/urokinase-type plasminogen activator receptor system activity by either activating the pro-enzyme form of urokinase-type plasminogen activator or cleaving the cell surface-associated urokinase-type plasminogen activator receptor |
| 3.4.21.B12 | more |
kallikrein-4 is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. In vitro dipeptidyl peptidase I activates pro-KLK4 to cleave a fluorogenic peptide containing a KLK4 cleavage site |
| 3.4.21.B12 | more |
the enzyme performs proteolytic autoactivation |
| 3.4.21.B12 | plasma hepatocyte growth factor activator zymogen + H2O |
activation, hepatocyte growth factor is mainly secreted from fibroblasts as an inactive single-chain precursor, which lacks biological activity |
