Structures and Functions of Precursors of Bacterial Proteases

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Abstract
The data on the precursors of bacterial proteases were generalized. The structure and special features of processing of the precursors of bacillary subtilisins, the α-lytic protease from Lysobacterenzymogenesand the related chymotrypsin-like proteases from Streptomycesgriseus, and the metalloproteases from bacilli and Pseudomonasaeruginosawere discussed. The approaches to producing the precursors and the protease propeptides and to in vitrocharacterizing them were particularly analyzed. The following physiological functions of the propeptides within the protease precursors were considered probable: (a) inhibition of the proteases to protect the host cells from the proteolytic damage; (b) participation in the folding of the mature enzyme; and (c) providing for the protease interaction with the bacterial cell surveillance mechanisms, including protease translocation through the cell wall.

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