title: Plant subtilisins.
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.
authors: Laboratory of Protein Chemistry, State Research Institute of Genetics and Selection of Industrial Microorganisms, Moscow, 113545, Russia. annamb@genebee.msu.su
authors: A M
authors: AM
authors: Bogacheva
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain / Q000235:genetics; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013381:Subtilisins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D009842:Oligopeptides; D013381:Subtilisins