title: Autoproteolytic processing of aspartic proteinase from sunflower seeds.
abstract: The autoproteolytic processing of mature aspartic proteinase from sunflower seeds was investigated. The mature aspartic proteinase (48 kDa) was processed at N65s-D66s in the plant-specific region of the enzyme to form 34-kDa and 14-kDa subunits. The next step was the hydrolysis of the A25s-Q26s and N97s-E98s bonds to form a 39-kDa enzyme that consisted of 29-kDa and 9-kDa disulfide-bonded subunits. Finally, bonds including V1s-M2s, M2s-S3s, C100s-D101s, and D101s-R102s were cleaved to form non-covalently bound subunits (29 kDa and 9 kDa) by eliminating the disulfide bonds in the plant-specific region of the protein.
authors.affiliation: Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Park
authors.forename: I
authors.initials: I
authors.lastname: Kusakabe
authors.forename: Y
authors.initials: Y
authors.lastname: Sakakibara
authors.forename: H
authors.initials: H
authors.lastname: Kobayashi
mesh_terms: D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D002403:Cathepsins / Q000737:chemistry / Q000378:metabolism; D006368:Helianthus / Q000201:enzymology*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D012639:Seeds / Q000201:enzymology
chemical_list: D002403:Cathepsins; D016282:Aspartic Acid Endopeptidases; C109797:phytepsin