Abstract

Publisher Summary This chapter examines the activity, specificity and structural chemistry of clostridium collagenases. The clostridial collagenases are distinguished by their ability to digest native, triple-helical types I, II and III collagens into a mixture of small peptides under physiological conditions. A variety of collagen-based assays is available to quantify these activities. Clostridial collagenases also digest other types of collagen, but these reactions have not been characterized in detail. The initial proteolytic events in the hydrolysis of type I, II, and III collagens by the class I and II collagenases have been delineated and the kinetic parameters for these reactions measured. The class I and II enzymes initially attack all three collagens at distinct hyper-reactive sites whose sequences have been identified. Clostridium histolyticum is a pathogenic anaerobe that causes gas gangrene. All strains of the bacterium elaborate a collagenase, but the amount depends on the strain and the culture medium. The bacterium presumably uses the collagenases as a means to invade the host and possibly to degrade host protein for nutritional purposes. The clostridial collagenases also appear able to digest most if not all of the other collagen types, while the vertebrate collagenases cannot.

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