This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Potempa, J.; Pike, R.; Travis, J.: The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain. Infect. Immun., 63, 1176–1182 (1995)
Bedi, G.S.: Purification and characterization of lysine-and arginine-specific gingivain proteases from Porphyromonas gingivalis. Prep. Biochem., 24, 251–261 (1994)
Pike, R.; McGraw, W.; Potempa, J.; Travis, J.: Lysine-and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J. Biol. Chem., 269, 406–411 (1994)
Potempa, J.; Travis, J.: Porphyromonas gingivalis proteinases in periodontitis, a review. Acta Biochim. Pol., 43, 455–465 (1996)
Pavloff, N.; Pemberton, P.A.; Potempa, J.; Chen, W.C.; Pike, R.N.; Prochazka, V.; Kiefer, M.C.; Travis, J.; Barr, P.J.: Molecular cloning and characterization of Porphyromonas gingivalis lysine-specific gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases. J. Biol. Chem., 272, 1595–1600 (1997)
Abe, N.; Kadowaki, T.; Okamoto, K.; Nakayama, K.; Ohishi, M.; Yamamoto, K.: Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease. J. Biochem., 123, 305–312 (1998)
Fujimura, S.; Hirai, K.; Shibata, Y.; Nakayama, K.; Nakamura, T.: Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis. FEMS Microbiol. Lett., 163, 173–179 (1998)
Banbula, A.; Bugno, M.; Kuster, A.; Heinrich, P.C.; Travis, J.; Potempa, J.: Rapid and efficient inactivation of IL-6 gingipains, lysine-and arginine-specific proteinases from Porphyromonas Gingivalis. Biochem. Biophys. Res. Commun., 261, 598–602 (1999)
Sroka, A.; Sztukowska, M.; Potempa, J.; Travis, J.; Genco, C.A.: Degradation of host heme proteins by lysine-and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis. J. Bacteriol., 183, 5609–5616 (2001)
Olczak, T.; Dixon, D.W.; Genco, C.A.: Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins. J. Bacteriol., 183, 5599–5608 (2001)
Curtis, M.A.; Opoku, J.A.; Rangarajan, M.; Gallagher, A.; Sterne, J.A.C.; reid, C.R.; Evans, H.E.A.; Samuelsson, B.: Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor. Infect. Immun., 70, 6968–6975 (2002)
Nassar, H.; Chou, H.H.; Khlgatian, M.; Gibson, F.C., 3rd; Van Dyke, T.E.; Genco, C.A.: Role for fimbriae and lysine-specific cysteine proteinase gingipain K in expression of interleukin-8 and monocyte chemoattractant protein in Porphyromonas gingivalis-infected endothelial cells. Infect. Immun., 70, 268–276 (2002)
Baba, A.; Kadowaki, T.; Asao, T.; Yamamoto, K.: Roles for Arg-and Lysgingipains in the disruption of cytokine responses and loss of viability of human endothelial cells by Porphyromonas gingivalis infection. Biol. Chem., 383, 1223–1230 (2002)
Simpsonv, W.; Olczak, T.; Genco, C.A.: Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis. Acta Biochim. Pol., 51, 253–262 (2004)
Smalley, J.W.; Thomas, M.F.; Birss, A.J.; Withnall, R.; Silver, J.: A combination of both arginine-and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin. Biochem. J., 379, 833–840 (2004)
Abe, N.; Baba, A.; Takii, R.; Nakayama, K.; Kamaguchi, A.; Shibata, Y.; Abiko, Y.; Okamoto, K.; Kadowaki, T.; Yamamoto, K.: Roles of Arg-and Lysgingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes. Biol. Chem., 385, 1041–1047 (2004)
Liu, X.; Sroka, A.; Potempa, J.; Genco, C.A.: Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR. Biol. Chem., 385, 1049–1057 (2004)
Mezyk-Kopec, R.; Bzowska, M.; Potempa, J.; Bzowska, M.; Jura, N.; Sroka, A.; Black, R.A.; Bereta, J.: Inactivation of membrane tumor necrosis factor α by gingipains from Porphyromonas gingivalis. Infect. Immun., 73, 1506–1514 (2005)
Bialas, A.; Grembecka, J.; Krowarsch, D.; Otlewski, J.; Potempa, J.; Mucha, A.: Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity. J. Med. Chem., 49, 1744–1753 (2006)
Kishimoto, M.; Yoshimura, A.; Naito, M.; Okamoto, K.; Yamamoto, K.; Golenbock, D.T.; Hara, Y.; Nakayama, K.: Gingipains inactivate a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling. Microbiol. Immunol., 50, 315–325 (2006)
Sztukowska, M.; Sroka, A.; Bugno, M.; Banbula, A.; Takahashi, Y.; Pike, R.N.; Genco, C.A.; Travis, J.; Potempa, J.: The C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities. Mol. Microbiol., 54, 1393–1408 (2004)
Cronan, C.A.; Potempa, J.; Travis, J.; Mayo, J.A.: Inhibition of Porphyromonas gingivalis proteinases (gingipains) by chlorhexidine: synergistic effect of Zn(II). Oral Microbiol. Immunol., 21, 212–217 (2006)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2009). Gingipain K. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_1
Download citation
DOI: https://doi.org/10.1007/978-3-540-85705-1_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-85704-4
Online ISBN: 978-3-540-85705-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)