Autoproteolytic processing of aspartic proteinase from sunflower seeds.
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.
Park
H
H
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Kusakabe
I
I
Sakakibara
Y
Y
Kobayashi
H
H
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
D002403:Cathepsins; D016282:Aspartic Acid Endopeptidases; C109797:phytepsin