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http://purl.uniprot.org/citations/10657258http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10657258http://www.w3.org/2000/01/rdf-schema#comment"Crystal structures of human pancreatic alpha-amylase (HPA) in complex with naturally occurring inhibitors have been solved. The tetrasaccharide acarbose and a pseudo-pentasaccharide of the trestatin family produced identical continuous electron densities corresponding to a pentasaccharide species, spanning the -3 to +2 subsites of the enzyme, presumably resulting from transglycosylation. Binding of the acarviosine core linked to a glucose residue at subsites -1 to +2 appears to be a critical part of the interaction process between alpha-amylases and trestatin-derived inhibitors. Two crystal forms, obtained at different values of pH, for the complex of HPA with the protein inhibitor from Phaseolus vulgaris (alpha-amylase inhibitor) have been solved. The flexible loop typical of the mammalian alpha-amylases was shown to exist in two different conformations, suggesting that loop closure is pH-sensitive. Structural information is provided for the important inhibitor residue, Arg-74, which has not been observed previously in structural analyses."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.org/dc/terms/identifier"doi:10.1042/bj3460201"xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Henrissat B."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Payan F."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Rouge P."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Puigserver A."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Nahoum V."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Bischoff H."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Roux G."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/author"Anton V."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/name"Biochem J"xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/pages"201-208"xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/title"Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors."xsd:string
http://purl.uniprot.org/citations/10657258http://purl.uniprot.org/core/volume"346"xsd:string
http://purl.uniprot.org/citations/10657258http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10657258
http://purl.uniprot.org/citations/10657258http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10657258
http://purl.uniprot.org/uniprot/#_P04746-mappedCitation-10657258http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10657258
http://purl.uniprot.org/uniprot/P04746http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10657258