Plant subtilisins.

  • 1 March 1999
    • journal article
    • review article
    • Vol. 64  (3) , 287-93
Abstract
This review presents a systematization of available data on subtilisin-like serine proteinases of plants. Enzymatic and physicochemical properties of the enzymes, their structure and processing, as well as their biological functions and origin are considered. Subtilisin-like proteinases of plants have a number of substantial differences from such typical subtilisins as subtilisin BPN or subtilisin Carlsberg. The plant subtilisins are characterized by much greater molecular mass, long inserts and C-terminal regions, and several cysteine residues, while typical subtilisins have no cysteine residues, and thiol-dependent bacterial subtilisins contain only one cysteine residue required for enzymatic activity.

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