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Titolo:
Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins
Autore:
Seo, SB; Tan-Wilson, A; Wilson, KA;
Indirizzi:
SUNY Binghamton, Dept Biol Sci, Binghamton, NY 13902 USA SUNY Binghamton Binghamton NY USA 13902 iol Sci, Binghamton, NY 13902 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1545, anno: 2001,
pagine: 192 - 206
SICI:
0167-4838(20010209)1545:1-2<192:PCACEI>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR STORAGE PROTEIN; PHASEOLUS-VULGARIS L; PROTEOLYTIC CLEAVAGE; GERMINATING SOYBEANS; POLYACRYLAMIDE GELS; GLYCINE-MAX; SH-EP; DEGRADATION; EXPRESSION; GENE;
Keywords:
cysteine protease; proteolysis; soybean; glycine mex; glycinin; beta-conglycinin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, KA SUNY Binghamton, Dept Biol Sci, POB 6000, Binghamton, NY 13902 USA SUNY Binghamton POB 6000 Binghamton NY USA 13902 , NY 13902 USA
Citazione:
S.B. Seo et al., "Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins", BBA-PROT ST, 1545(1-2), 2001, pp. 192-206

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 linkingtheir 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 particularamino acid or sequence. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 21:58:37