EC Number |
General Information |
Reference |
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3.4.22.37 | malfunction |
human keratinocyte Rgp-deficient and Kgp-deficient double mutant cells do not cleave protease-activated recptor-1 and -2. The single Rgp-negative mutant cleaves protease-activated recptor-2 |
709842 |
3.4.22.37 | malfunction |
Porphyromonas gingivalis double mutant RgpA/RgpB cells do not induce apoptosis in human gingvial epithelial cells |
707889 |
3.4.22.37 | malfunction |
Porphyromonas gingivalis RgpA/B double mutant do not induce buccal edema and gingivitis in BALB/c or C57BL/6 mice |
709355 |
3.4.22.37 | malfunction |
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain. Proteolytic activity of Rgp is required for membrane vesicles entry. Only few Rgp-null membrane vesicles enter the cells, and these negligibly degrade transferrin receptor, whereas paxillin and focal adhesion kinase degradation is significant |
708711 |
3.4.22.37 | malfunction |
the roles of several virulence factors in homotypic biofilm development by Porphyromonas gingivalis. A RgpA/B double mutant develops channel-like biofilms with fibrillar and tall microcolonies in PBS. When this mutant is studied in diluted trypticase soy broth, there is an increase in the number of peaks and the morphology changed to taller and loosely packed biofilms. Results suggests that Rgp controlls microcolony morphology and biovolume and acts coordinately with other virulence factors such as long (FimA) and short (Mfa) fimbriae to regulate the development of mature biofilms |
707890 |
3.4.22.37 | malfunction |
using Porphyromonas gingivalis null mutant KDP136 (triple mutant for RgpA/RgpB/Kgp) gingipain-sensitive ligand are identified. Two proteins encoded by protein-coding sequence PGN_0748 and PGN_0728 are obtained |
708710 |
3.4.22.37 | metabolism |
methaemoglobin formation by R-gingipain facilitates extraction of haem from haemoglobin by HmuY (haem-binding protein) |
718267 |
3.4.22.37 | metabolism |
the presence of Rgps promotes caspase-1 activation. The caspase-1-dependent interleukin-1beta response is cooperatively diminished by isoforms RgpA and RgpB |
-, 731625 |
3.4.22.37 | more |
the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing |
-, 754780 |
3.4.22.37 | more |
the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent |
-, 754780 |