title: Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins.
abstract: The protease that degrades the beta subunit of the soybean (Glycine max (L.) Merrill) storage protein beta-conglycinin was purified from the cotyledons of seedlings grown for 12 days. The enzyme was named protease C2 because it is the second enzyme to cleave the beta-conglycinin storage protein, the first (protease C1) being one that degrades only the alpha' and alpha subunits of the storage protein to products similar in size and sequence to the remaining intact beta subunit. Protease C2 activity is not evident in vivo until 4 days after imbibition of the seed. The 31 kDa enzyme is a cysteine protease with a pH optimum with beta-conglycinin as substrate of 5.5. The action of protease C2 on native beta-conglycinin produces a set of large fragments (52-46 kDa in size) and small fragments (29-25 kDa). This is consistent with cleavage of all beta-conglycinin subunits at the region linking their N- and C-domains. Protease C2 also cleaves phaseolin, the Phaseolus vulgaris vicilin homologous to beta-conglycinin, to fragments in the 25-28 kDa range. N-Terminal sequences of isolated beta-conglycinin and phaseolin products show that protease C2 cleaves at a bond within a very mobile surface loop connecting the two compact structural domains of each subunit. The protease C2 cleavage specificity appears to be dictated by the substrate's three-dimensional structure rather than a specificity for a particular amino acid or sequence.
authors.affiliation: Department of Biological Sciences, P.O. Box 6000, State University of New York at Binghamton, Binghamton, NY 13902-6000, USA.
authors.forename: S
authors.initials: S
authors.lastname: Seo
authors.forename: A
authors.initials: A
authors.lastname: Tan-Wilson
authors.forename: K A
authors.initials: KA
authors.lastname: Wilson
mesh_terms: D000595:Amino Acid Sequence; D052179:Antigens, Plant; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005916:Globulins / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010940:Plant Proteins; D011480:Protease Inhibitors / Q000494:pharmacology; D011487:Protein Conformation; D055314:Seed Storage Proteins; D012639:Seeds; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D030262:Soybean Proteins / Q000737:chemistry / Q000378:metabolism*; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D052179:Antigens, Plant; D005916:Globulins; D010446:Peptide Fragments; D010940:Plant Proteins; D011480:Protease Inhibitors; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max; C048826:phaseolin protein, Phaseolus vulgaris; D003546:Cysteine Endopeptidases; C427222:soybean protease C2