EC Number   |
General Information |
Reference |
|---|
   3.4.14.1 | malfunction |
mutations in the cathepsin C gene result in an autosomal recessive disorder, Papillon-Lefevre syndrome |
708279 |
| 3.4.14.1 | physiological function |
a recombinant form of cathepsin C lacking its exclusion domain is a monomer with endoprotease activity and affinity for hydrophobic residues such as Phe, Leu or Pro, but not Val, in the P2 position. As opposed to cathepsin C, it does not require chloride ions for its activity. Recombinant truncated cathepsin C has elastolytic and gelatinolytic activity comparable to other cysteine cathepsins |
755315 |
| 3.4.14.1 | physiological function |
inhibition results in the formation of an immature trophozoite that leads to parasite death |
717480 |
| 3.4.14.1 | physiological function |
may activate kallikrein-4 during enamel formation |
693377 |
| 3.4.14.1 | physiological function |
overexpression of cathepsin C in vitro significantly delays the cytopathic effect evoked by Singapore grouper iridovirus and inhibit the viral genes transcription. Overexpression significantly increases the expression of proinflammatory cytokines during Singapore grouper iridovirus infection |
753614 |
| 3.4.14.1 | physiological function |
Plasmodium berghei dpap2-minus parasites grow normally, differentiate into gametocytes, and generate sporozoites that are infectious to mice when fed to a mosquito. Isoform dpap1 transcription is more than 2fold upregulated in the dpap2-negative clonal lines, possibly compensating for the loss of isoform dpap2. When inhibitor 3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one is added to the dpap2-negative parasites just before a mosquito membrane feed, mosquito infectivity is not affected |
-, 731143 |
| 3.4.14.1 | physiological function |
Plasmodium falciparum dpap2-minus parasites are viable and produce morphologically normal gametocytes. Both wild-type and dpap2-negative parasites are sensitive to inhibitor 3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one, indicating that, unlike many antimalarials, 3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one has activity against parasites at both the asexual and sexual stages |
731143 |
| 3.4.14.1 | physiological function |
survival in DPPI-/- mice lacking dipeptidyl peptidase I is significantly better than in DPPI+/+ mice 8 d after infection in a Klebsiella pneumoniae lung infection model. DPPI-/- mice have significantly fewer bacteria in the lung than infected DPPI+/+ mice, but no difference in lung histopathology, lung injury, or cytokine levels. Levels of surfactant protein D, but not of surfactant protein A, are higher in DPPI-/- than in DPPI+/+ BAL fluid, and DPPI-/- BAL fluid aggregate bacteria more effectively than control BAL fluid. Sequencing of the amino terminus of surfactant protein D reveals two or eight additional amino acids in surfactant protein D isolated from DPPI-/- mice, suggesting processing by DPPI |
731258 |
| 3.4.14.1 | physiological function |
the maturation of proCatC obeys a multistep mechanism that can be entirely managed by CatS in neutrophilic precursor cells. CatS inhibition by a cell-permeable inhibitor abrogates the release of the heavy and light chains from proCatC and blocks 80% of CatC activity. Under these conditions, the activity of neutrophil serine proteases is not abolished in precursor cell cultures |
754144 |
