Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms.
A vacuolar processing enzyme was detected in soybean protein bodies. A 39-kDa immunoreactive polypeptide obtained by chromatography on a hydroxyapatite column processed both a decapeptide substrate and proproteins. A cDNA was isolated for a 55-kDa protein with 71% identity to the castor bean vacuolar processing enzyme.
Shimada
T
T
Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.
Hiraiwa
N
N
Nishimura
M
M
Hara-Nishimura
I
I
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002367:Ricinus communis / Q000201:enzymology; D002845:Chromatography; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D017931:DNA Primers; D018076:DNA, Complementary / Q000302:isolation & purification; D017886:Durapatite; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010947:Plants, Toxic; D011498:Protein Precursors / Q000378:metabolism*; D012547:Schistosoma / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity; D014617:Vacuoles / Q000201:enzymology
D017931:DNA Primers; D018076:DNA, Complementary; D011498:Protein Precursors; D017886:Durapatite; D003546:Cysteine Endopeptidases; C089278:vacuolar processing enzyme