Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis

Porphyromonas gingivalis

Editorial Periodontal diseases have long been associated with an increased, yet moderate, risk for the development of atherosclerosis and coronary heart disease. The postulated mechanism underlying this association is the low grade systemic inflammatory response to pathogens engaged in chronic periodontal infection, such as Porphyromonas gingivalis, which may facilitate atheroma formation and t...

Rapid and efficient inactivation of IL-6 gingipains, lysine- and arginine-specific proteinases from Porphyromonas gingivalis.

Deregulation of the cytokine network is an important adaptation of pathogenic bacteria to modulate and evade a host immune response. Here we describe that IL-6 is rapidly and efficiently cleaved and inactivated by the arginine- and lysine-specific proteinases from Porphyromonas gingivalis, referred to as RGP-A, RGP-B, and KGP. One of the primary cleavage sites for RGPs has been mapped between R...

Metal cofactors of lysine-2,3-aminomutase.

Lysine-2,3-aminomutase from Clostridium SB4 contains iron and sulfide in equimolar amounts, as well as cobalt, zinc, and copper. The iron and sulfide apparently constitute an Fe-S cluster that is required as a cofactor of the enzyme. Although no B12 derivative can be detected, enzyme-bound cobalt is a cofactor; however, the zinc and copper bound to the enzyme do not appear to play a role in its...

Porphyromonas gingivalis strain-dependent activation of human endothelial cells.

Porphyromonas gingivalis is an important bacterium involved in periodontal diseases. Colonization by periodontopathogens has been associated with severe local inflammatory reactions in the connective tissue. In this study we characterized P. gingivalis-mediated infection and activation of human umbilical vein endothelial cells by using two strains of different virulence capacities, strains ATCC...

Endothelial Cells Strain-Dependent Activation of Human Porphyromonas gingivalis