Karilysin   

Jan Potempa, ... Abdulkarim Y. Karim, in Handbook of Proteolytic Enzymes (Third Edition), 2013

Name and History

Tannerella forsythia (formerly Bacteroides forsythus), together withand Treponema denticola, are considered to be the major periodontal pathogens [1]. A common feature of these organisms is the production of high levels of proteolytic activity. This activity is considered an important virulence factor contributing to pathological chronic inflammation, which drives tissue damage in periodontitis [2]. The proteolytic activity of the latter two pathogens has been characterized but very little is known about peptidasesproduced by T. forsythia. As a matter of fact, out of two dozen genes putatively encoding secretory proteases in the T. forsythia genome, only two enzymes have been characterized at the protein level. A first one, referred to as PrtH [3,4], is remotely related to caspases [5]; the other, karilysin, resembles matrix metalloproteases. The name karilysin was derived from the name of the Ph.D. student (Karim), who cloned, expressed and characterized the protein and ‘lysin’ reflecting the metallopeptidolytic nature of the enzyme [6]. Karilysin is expressed as a proenzyme (proKly). Consecutive autoproteolytic cleavages at N- and C-terminal segments generate forms of the active enzyme with molecular masses of 48 kDa, 38 kDa, and 18 kDa referred to as Kly48, Kly38, and Kly18, respectively.

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