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http://purl.uniprot.org/citations/9399589http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9399589http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9399589http://www.w3.org/2000/01/rdf-schema#comment"The human ER-60 protease cDNA was expressed in Escherichia coli BL21 (DE3) cells using the pET-20b(+) T7 promoter. The recombinant ER-60 protease was obtained in a water-soluble form and purified through four sequential chromatographies. The ER-60 protease contains two CGHC motifs. When an alanine residue was substituted for the N-terminal cysteine residue in both motifs, the protease activity was not lost. However, when the C-terminal cysteine residue in both motifs was replaced by a serine residue, the cysteine protease activity, which was inhibited by p-chloromercuribenzoic acid (pCMB) but not by diisopropyl fluorophosphate (DFP), changed to serine protease activity, which was inhibited by DFP but not by pCMB. These results indicate that the C-terminal cysteine residue(s) of the CGHC motifs may constitute the active site(s) of ER-60 protease. The ER-60 protease has a C-terminal QEDL sequence, which was proved to serve as an ER-retention signal by deletion of the QEDL sequence. However, because QEDL could not serve as the ER-retention signal for protein disulfide isomerase or ERp72, it is suggested that amino acid residue(s) of ER-60 protease, other than the QEDL sequence itself, is complimentarily responsible for the ER retention of this protein."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a021830"xsd:string
http://purl.uniprot.org/citations/9399589http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a021830"xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Oda T."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Oda T."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Ito H."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Ito H."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Utsumi S."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Utsumi S."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Kito M."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Kito M."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Moriyama T."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Moriyama T."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Urade R."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/author"Urade R."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/pages"834-842"xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/pages"834-842"xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/title"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease."xsd:string
http://purl.uniprot.org/citations/9399589http://purl.uniprot.org/core/title"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease."xsd:string