In ex vivo studies, it was shown that gingipain K retained its IgG hydrolyzing activity in human plasma despite the high content of natural protease inhibitors; that IgG(1) cleavage products were detected in gingival crevicular fluid samples from patients with severe periodontitis; and that gingipain K treatment of serum samples from patients with high antibody titers against P. gingivalis

Gingipain K ( EC 3.4.22.47 , Lys-gingipain , PrtP-proteinas ) är ett enzym . Detta enzym katalyserar följande kemiska reaktion · Endopeptidas med strikt

Genetic and environme- ntal determinants for disease risk in subsets of rheumatoid arthritis defined by the anti- citrullinated protein/peptide J. Lönn, Stefan Ljunggren, K. Klarstrom-Engstrom, I. Demirel, T. Bengtsson and Helen Karlsson · Lipoprotein modifications by gingipains of Porphyromonas 2020 · 130 · #2. 91. Presidenten har ordet tidende. Foto: K ristin A ksnes. (HSP) and the P. gingivalis protease gingipain, resemble the body's.

Gingipain k

Cysteine endoproteinases, from periodontal pathogen PORPHYROMONAS GINGIVALIS, acting as virulence factors associated with PERIODONTITIS. They are produced as pre-proproteins which mature into ARGININE and LYSINE specific endopeptidases. Proteases produced by Porphyromonas gingivalis , an oral pathogen, are considered important virulence factors and may affect the responses of cells equipped with proteinase-activated receptors. The aim of this study was to investigate the effect of the arginine-specific cysteine protease gingipain-R produced by P. gingivalis on chemokine production by human gingival fibroblasts (HGF) and the Both Lys-gingipain (gingipain-K) and Arg-gingipain (gingipain-R) prolonged plasma TT in a dose- and time-dependent manner, and this was also found with vesicles which are the biological carriers of P. gingivalis proteinases. 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.

Gingipain –R, gingipain-K: One gingipain had a narrow spectrum of activity against peptide bonds containg arginine, resistant to serine proteinase inhibitors and was activated by glycine containing dipeptidase. Molecular wt 50kda and a ph optimum of 6.0 – Arg-gingipain or gingipain-R De cario 1997 - Identified this lysine specific activity Specifically, the gingipain inhibitor reduced deposits of lipids in the aortas of infected animals and prevented the progression of atherosclerosis linked to P. gingivalis infection.

View protein in InterPro IPR029030, Caspase-like_dom_sf IPR011628, Cleaved_adhesin IPR001769, Gingipain IPR029031, Gingipain_N_sf IPR038490, Gingipain_propep_sf IPR013783, Ig-like_fold IPR018832, Pept_C25_gingipain_C IPR005536, Peptidase_C25_Ig-like_domain IPR012600, Propeptide_C25: Pfam i

Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_1. 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 The Porphyromonas gingivalis lysine-specific cysteine protease (gingipain K, Kgp) is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with Pike, Robert Neil; Potempa, Jan. / Gingipain K.Handbook of Proteolytic Enzymes.

Lönn J, Ljunggren S, Klarström-Engström K, Demirel I, Bengtsson T, Karlsson H. Lipoprotein modifications by gingipains of Porphyromonas gingivalis.

Apr 26, 2019 Content of family, Peptidase family C25 contains cysteine endopeptidases from bacteria, notably gingipain R (C25.001) and gingipain K Jan 23, 2019 gingivalis gingipain-deficient mutants either lacking Kgp activity (Kgp Ig-B) or lacking both Kgp and Rgp activity ( K/ RAB-A). Un- infected SH- pain R1 and gingipain K) released by P. gingivalis strain HG66 are purified as noncovalent complexes of the catalytic domain, with several polypeptide chains It is expected that inhibition of gingipain activity in vivo could prevent or slow is a specific, slowly reversible inhibitor of Kgp with a K i in the nanomolar range. whether gingipains can hydrolyze human IgG and found that under the conditions used (10 nM enzyme concen- tration, 4 h incubation at 37°C) only gingipain K Jun 13, 2019 Among T9SS cargo proteins are cysteine proteases, gingipains, which are short, Rgps) or lysine (Lys-gingipain or gingipain K, for short, Kgp).

J. Bacteriol. 183 , 5599 –5608. Role for Fimbriae and Lysine-Specific Cysteine Proteinase Gingipain K in Expression of Interleukin-8 and Monocyte Chemoattractant Protein in Porphyromonas gingipain K; Lys-gingipain; PrtP proteinase.
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Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_1.
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Pike, Robert Neil; Potempa, Jan. / Gingipain K.Handbook of Proteolytic Enzymes. editor / Neil D Rawlings ; Guy Salvesen. Vol. 2 3rd. ed. UK : Academic Press, 2013. pp

Endopeptidase with strict specificity for lysyl bonds. Activity of this enzyme is stimulated by glycine . (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. 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 The Porphyromonas gingivalis lysine-specific cysteine protease (gingipain K, Kgp) is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with Pike, Robert Neil; Potempa, Jan. / Gingipain K.Handbook of Proteolytic Enzymes.