| http://purl.uniprot.org/citations/8103452 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8103452 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8103452 | http://www.w3.org/2000/01/rdf-schema#comment | "The complete amino acid sequence of a subunit of sweet potato beta-amylase, a homotetramer, was established by sequence analysis of peptides obtained by digestions with Achromobacter protease I and Staphylococcus aureus V8 protease and by cyanogen bromide cleavage of the S-carboxymethylated subunit. The subunit of the enzyme is a single polypeptide consisting of 498 amino acid residues. It showed 50-60% identity in the amino acid sequence with those of beta-amylases from soybean and barley, while it about 25% with those of three bacterial beta-amylases deduced from the cDNA sequences. Sweet potato beta-amylase was completely inactivated with 2,3-epoxypropyl alpha-D-[U-14C]glucopyranoside. Sequence analysis of the inactivated enzyme revealed that Glu187 was specifically esterified by the affinity labeling with the above reagent, proposing that Glu187 is a potent candidate involved directly in the catalysis with this plant beta-amylase."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1993.tb18112.x"xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1993.tb18112.x"xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Sakiyama F."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Sakiyama F."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Toda H."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Toda H."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Nitta Y."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Nitta Y."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Asanami S."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Asanami S."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Kim J.P."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/author | "Kim J.P."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/pages | "25-38"xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/pages | "25-38"xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/title | "Sweet potato beta-amylase. Primary structure and identification of the active-site glutamyl residue."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/title | "Sweet potato beta-amylase. Primary structure and identification of the active-site glutamyl residue."xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/volume | "216"xsd:string |
| http://purl.uniprot.org/citations/8103452 | http://purl.uniprot.org/core/volume | "216"xsd:string |