Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins
DC Field | Value | Language |
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dc.contributor.author | Seo, Sang-beom | - |
dc.contributor.author | Tan-Wilson,Anna | - |
dc.contributor.author | Wilson, Karl A. | - |
dc.date.accessioned | 2022-05-11T00:40:12Z | - |
dc.date.available | 2022-05-11T00:40:12Z | - |
dc.date.issued | 2001-02 | - |
dc.identifier.issn | 0167-4838 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57470 | - |
dc.description.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 a 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 is 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. (C) 2001 Elsevier Science B.V. All rights reserved. | - |
dc.format.extent | 15 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/S0167-4838(00)00277-6 | - |
dc.identifier.bibliographicCitation | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, v.1545, no.1-2, pp 192 - 206 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000167072700021 | - |
dc.identifier.scopusid | 2-s2.0-0035830722 | - |
dc.citation.endPage | 206 | - |
dc.citation.number | 1-2 | - |
dc.citation.startPage | 192 | - |
dc.citation.title | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | - |
dc.citation.volume | 1545 | - |
dc.type.docType | Article | - |
dc.publisher.location | 네델란드 | - |
dc.subject.keywordAuthor | cysteine protease | - |
dc.subject.keywordAuthor | proteolysis | - |
dc.subject.keywordAuthor | soybean | - |
dc.subject.keywordAuthor | glycine mex | - |
dc.subject.keywordAuthor | glycinin | - |
dc.subject.keywordAuthor | beta-conglycinin | - |
dc.subject.keywordPlus | MAJOR STORAGE PROTEIN | - |
dc.subject.keywordPlus | PHASEOLUS-VULGARIS L | - |
dc.subject.keywordPlus | PROTEOLYTIC CLEAVAGE | - |
dc.subject.keywordPlus | GERMINATING SOYBEANS | - |
dc.subject.keywordPlus | POLYACRYLAMIDE GELS | - |
dc.subject.keywordPlus | GLYCINE-MAX | - |
dc.subject.keywordPlus | SH-EP | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | GENE | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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