| http://purl.uniprot.org/citations/12535607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12535607 | http://www.w3.org/2000/01/rdf-schema#comment | "Twenty-five analogs of D-glucose were examined as reversible inhibitors of yeast alpha-glucosidase (EC 3.2.1.20). The K(i) values range from 0.38 mM for 6-deoxy-D-glucose (quinovose) to 1.0 M for D-lyxose at pH=6.3 (0.1 M NaCl, 25 degrees ). All the monosaccharides and the three disaccharides (maltose, isomaltose and alpha,alpha-trehalose) were found to be linear competitive inhibitors with respect to alpha-p-nitrophenyl glucoside (pNPG) hydrolysis. Multiple inhibition analysis reveals that there are at least three monosaccharide binding sites on the enzyme. One of these can be occupied by glucose [K(i)=1.8(+/-0.1) mM], one by D-galactose [K(i)=164(+/-11) mM] and one by D-mannose [K(i)=120(+/-9) mM]. The pH dependence for glucose binding closely follows that of V/K [pK(a1)=5.55(+/-0.15), pK(a2)=6.79(+/-0.15)], but the binding of mannose does not. Although the glucose subsite can be occupied simultaneously with the mannose or galactose subsites in the enzyme-product complex, no transglucosylation can be detected between pNPG and either mannose or galactose. This suggests that neither of these nonglucose subsites can be occupied in a productive manner in the covalent glucosyl-enzyme intermediate."xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1570-9639(02)00474-0"xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/author | "Yao X."xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/author | "Byers L."xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/author | "Mauldin R."xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/pages | "22-29"xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/title | "Multiple sugar binding sites in alpha-glucosidase."xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://purl.uniprot.org/core/volume | "1645"xsd:string |
| http://purl.uniprot.org/citations/12535607 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12535607 |
| http://purl.uniprot.org/citations/12535607 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12535607 |
| http://purl.uniprot.org/uniprot/#_P07265-mappedCitation-12535607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12535607 |
| http://purl.uniprot.org/uniprot/P07265 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/12535607 |