REVIEW: Plant Subtilisins

A. M. Bogacheva

Laboratory of Protein Chemistry, State Research Institute of Genetics and Selection of Industrial Microorganisms, 1-yi Dorozhnyi Proezd 1, Moscow, 113545 Russia; fax: (095) 315-0501; E-mail: annamb@genebee.msu.su

Received August 31, 1998; Revision received December 1, 1998

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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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KEY WORDS: serine proteinases, plant subtilisins, primary structure, subfamilies

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