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Volumn 116, Issue 3, 1994, Pages 541-546

Isolation and analysis of cdna encoding a precursor of canavalia ensiformis asparaginyl endopeptidase (legumain)

Author keywords

Asparaginyl endopeptidase; CDNA; Cysteine proteinase; Jack bean legumain; Posttranslational proteolysis

Indexed keywords

ASPARAGINE; CLOSTRIPAIN; COMPLEMENTARY DNA; ENZYME PRECURSOR; ISOENZYME; PAPAIN; PROTEINASE;

EID: 0027990302     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a124559     Document Type: Article
Times cited : (56)

References (18)
  • 1
    • 0022001083 scopus 로고
    • Polypeptide ligation occurs during post-translational modification of concanavalin A
    • Carrington, D.M., Auffret, A., and Hanke, D.E. (1985) Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature 313, 64-67
    • (1985) Nature , vol.313 , pp. 64-67
    • Carrington, D.M.1    Auffret, A.2    Hanke, D.E.3
  • 3
    • 0027477474 scopus 로고
    • Asparaginyl endopeptidase of jack bean seeds: Purification, characterization, and high utility in protein sequence analysis
    • Abe, Y., Shirane, K., Yokosawa, H., Matsushita, H., Mitta, M., Kato, I., and Ishii, S. (1993) Asparaginyl endopeptidase of jack bean seeds: Purification, characterization, and high utility in protein sequence analysis. J. Biol. Chem. 268, 3525-3529
    • (1993) J. Biol. Chem , vol.268 , pp. 3525-3529
    • Abe, Y.1    Shirane, K.2    Yokosawa, H.3    Matsushita, H.4    Mitta, M.5    Kato, I.6    Ishii, S.7
  • 4
    • 0017407885 scopus 로고
    • Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings
    • Baumgartner, B. and Chrispeels, M.J. (1977) Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings. Eur. J. Biochem. 77, 223-233
    • (1977) Eur. J. Biochem , vol.77 , pp. 223-233
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 5
    • 0020131172 scopus 로고
    • Purification and partial characterization of protease B from germinating vetch seeds
    • Shutov, A.D., Lanh, D.N., and Vaintraub, I.A. (1982) Purification and partial characterization of protease B from germinating vetch seeds. Biokhimiya [Engl. Trans.] 47, 678-685
    • (1982) Biokhimiya [Engl. Trans.] , vol.47 , pp. 678-685
    • Shutov, A.D.1    Lanh, D.N.2    Vaintraub, I.A.3
  • 6
    • 0021764122 scopus 로고
    • Proteinase from germinating bean cotyledons: Evidence for involvement of a thiol group in catalysis
    • Csoma, C. and Polgar, L. (1984) Proteinase from germinating bean cotyledons: Evidence for involvement of a thiol group in catalysis. Biochem. J. 222, 769-776
    • (1984) Biochem. J , vol.222 , pp. 769-776
    • Csoma, C.1    Polgar, L.2
  • 7
    • 0026556773 scopus 로고
    • A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean
    • Scott, M.P., Jung, R., Muntz, K., and Nielsen, N.C. (1992) A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proc. Natl. Acad. Sci. USA 89, 658-662
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 658-662
    • Scott, M.P.1    Jung, R.2    Muntz, K.3    Nielsen, N.C.4
  • 8
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays
    • Kembhavi, A.A., Buttle, D.J., Knight, C.G., and Barett, A.J. (1993) The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays. Arch. Biochem. Biophys. 303, 208-213
    • (1993) Arch. Biochem. Biophys , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barett, A.J.4
  • 9
    • 0027249370 scopus 로고
    • A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme
    • Muramatsu, M. and Fukazawa, C. (1993) A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme. Eur. J. Biochem. 215, 123-132
    • (1993) Eur. J. Biochem , vol.215 , pp. 123-132
    • Muramatsu, M.1    Fukazawa, C.2
  • 10
    • 0003450992 scopus 로고
    • Academic Press, San Diego, U.S.A
    • Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (1992) Enzyme Nomenclature 1992, Academic Press, San Diego, U.S.A.
    • (1992) Enzyme Nomenclature
  • 11
  • 13
    • 0027244427 scopus 로고
    • The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene
    • Dargatz, H., Diefenthal, T., Witte, V., Reipen, G., and von Wettstein, D. (1993) The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene. Mol. Gen. Genet. 240, 140-145
    • (1993) Mol. Gen. Genet , vol.240 , pp. 140-145
    • Dargatz, H.1    Diefenthal, T.2    Witte, V.3    Reipen, G.4    Von Wettstein, D.5
  • 14
    • 0027431179 scopus 로고
    • Purification of an endo- proteinase that digests the wheat ‘Em’ protein in vitro, and determination of its cleavage sites
    • Taylor, R.M. and Cuming, A.C. (1993) Purification of an endo- proteinase that digests the wheat ‘Em’ protein in vitro, and determination of its cleavage sites. FEBS Lett. 331, 76-80
    • (1993) FEBS Lett , vol.331 , pp. 76-80
    • Taylor, R.M.1    Cuming, A.C.2
  • 15
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura, I., Inoue, K., and Nishimura, M. (1991) A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett. 294, 89-93
    • (1991) FEBS Lett , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 16
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydryl-endopep- tidase (SH-EP) from cotyledons of germinating Vigna mungo seeds
    • Akafuku, H., Yamauchi, D., Mitsuhashi, W., and Minamikawa, T. (1989) Nucleotide sequence of cDNA for sulfhydryl-endopep- tidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Res. 17, 6733
    • (1989) Nucleic Acids Res , vol.17 , pp. 6733
    • Akafuku, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 17
    • 0025113503 scopus 로고
    • Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol proteases of the papain family
    • Kalinski, A., Weisemann, J.M., Matthews, B.F., and Herman, E.M. (1990) Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol proteases of the papain family. J. Biol. Chem. 265, 13843-13848
    • (1990) J. Biol. Chem , vol.265 , pp. 13843-13848
    • Kalinski, A.1    Weisemann, J.M.2    Matthews, B.F.3    Herman, E.M.4
  • 18
    • 0026176684 scopus 로고
    • Nucleotide sequence of cDNA for an endopeptidase (EP-Cl) from pods of maturing Phaseolus vulgaris fruits
    • Tanaka, T., Yamauchi, D., and Minamikawa, T. (1991) Nucleotide sequence of cDNA for an endopeptidase (EP-Cl) from pods of maturing Phaseolus vulgaris fruits. Plant Mol. Biol. 16, 1083-1084
    • (1991) Plant Mol. Biol , vol.16 , pp. 1083-1084
    • Tanaka, T.1    Yamauchi, D.2    Minamikawa, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.