Gingipain R
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.37 gingipain R
Gingipain R is a secreted arginine-specific cysteine endopeptidase from the bacterium Porphyromonas gingivalis, strongly activated by glycine and stabilized by Ca2+, with a precursor containing a hemagglutinin domain. Although misleadingly described as trypsin-like in early literature, it is a cysteine peptidase and the type example of peptidase family C25. It hydrolyzes proteins and small-molecule substrates with a preference for Arg at P1. In the periodontal pocket it degrades host immunoglobulins, collagen and cytokines, driving periodontal disease. It features a catalytic cysteine within an unusual RgpB-like fold stabilized by Ca2+.
Gingipain R is a secreted arginine-specific cysteine endopeptidase from the bacterium Porphyromonas gingivalis, strongly activated by glycine and stabilized by Ca2+, with a precursor containing a hemagglutinin domain. Although misleadingly described as trypsin-like in early literature, it is a cysteine peptidase and the type example of peptidase family C25. It hydrolyzes proteins and small-molecule substrates with a preference for Arg at P1. In the periodontal pocket it degrades host immunoglobulins, collagen and cytokines, driving periodontal disease. It features a catalytic cysteine within an unusual RgpB-like fold stabilized by Ca2+.
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