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 fu
nctions and origin are considered. Subtilisin-like proteinases of plants ha
ve a number of substantial differences from such typical subtilisins as sub
tilisin BPN' or subtilisin Carlsberg. The plant subtilisins are characteriz
ed by much greater molecular mass, long inserts and C-terminal regions, and
several cysteine residues, while typical subtilisins have no cysteine resi
dues, and thiol-dependent bacterial subtilisins contain only one cysteine r
esidue required for enzymatic activity.