RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11914073http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11914073http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11914073http://www.w3.org/2000/01/rdf-schema#comment"The psychrophilic Pseudoalteromonas haloplanctis alpha-amylase is shown to form ternary complexes with two alpha-amylase inhibitors present in the active site region, namely, a molecule of Tris and a trisaccharide inhibitor or heptasaccharide inhibitor, respectively. The crystal structures of these complexes have been determined by X-ray crystallography to 1.80 and 1.74 A resolution, respectively. In both cases, the prebound inhibitor Tris is expelled from the active site by the incoming oligosaccharide inhibitor substrate analogue, but stays linked to it, forming well-defined ternary complexes with the enzyme. These results illustrate competition in the crystalline state between two inhibitors, an oligosaccharide substrate analogue and a Tris molecule, bound at the same time in the active site region. Taken together, these structures show that the enzyme performs transglycosylation in the complex with the pseudotetrasaccharide acarbose (confirmed by a mutant structure), leading to a well-defined heptasaccharide, considered as a more potent inhibitor. Furthermore, the substrate-induced ordering of water molecules within a channel highlights a possible pathway used for hydrolysis of starch and related poly- and oligosaccharides."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.org/dc/terms/identifier"doi:10.1021/bi0160516"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.org/dc/terms/identifier"doi:10.1021/bi0160516"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Haser R."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Haser R."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Roth M."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Roth M."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Aghajari N."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/author"Aghajari N."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/pages"4273-4280"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/pages"4273-4280"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/title"Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/title"Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase."xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/11914073http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/11914073http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11914073
http://purl.uniprot.org/citations/11914073http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11914073
http://purl.uniprot.org/citations/11914073http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11914073
http://purl.uniprot.org/citations/11914073http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11914073