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Mode of the inhibition of venom collagenase by actinonin
Author(s) -
Price Joseph A.,
Sun Jing
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.982.7
Subject(s) - collagenase , venom , non competitive inhibition , envenomation , enzyme , protease , chemistry , substrate (aquarium) , pharmacology , biochemistry , stereochemistry , biology , ecology
Snake envenomation remains an endemic health problem in much of the world. A new approach to controlling its pathology may be the use of enzyme inhibitors. A preliminary characterization was made of the mode of C. atrox collagenase inhibition by the protease inhibitor actinonin. The reaction progresses nearly linearly for close to an hour at room temperature. Reaction data for combinations of seven levels of inhibitor and six levels of substrate were fit to Michaelis‐Menten equations by nonlinear regression to determine values of apparent Km and Vmax. In these dose response experiments apparent Vmax, Km, and Vmax/Km decreased as the concentration of the inhibitor was increased. This pattern is most consistent with noncompetitive enzyme inhibition. These results better characterize this agonist in reactions with whole venom, and make actinonin a compound of interest in developing new anti‐venom therapeutics. Support or Funding Information No extramural funding supported this work.