The bacteria Tannerella forsythia has been widely identified as a pathogen associated with periodontal disease.  Previously, we have presented a procedure describing the isolation of a newly identified protease with gelatinase activity.  Here we show the ability of this protease to cleave type 1 collagen.  Highly fluorescein-labeled type I collagen was incubated with the purified enzyme and increase in relative fluorescence due to relief of fluorescent quenching by enzymatic cleavage was measured.  Furthermore, inhibition of the enzyme by the metalloproteinase inhibitor 1,10-phenanthroline was also shown to take place in a dose-dependent manner. The kinetic constants Km and Vmax were determined for cleavage of type 1 collagen.

Analysis of enzyme kinetics and inhibition of collagenase activity of a protease isolated from <i>Tannerella forsythia</i>

243rd National Meeting (2012)

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Analysis of enzyme kinetics and inhibition of collagenase activity of a protease isolated from Tannerella forsythia