| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/2000/01/rdf-schema#comment | "The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.1996.0332"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.1996.0332"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/author | "Schulz G.E."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/author | "Schulz G.E."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/author | "Dreyer M.K."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/author | "Dreyer M.K."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/pages | "458-466"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/pages | "458-466"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/title | "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/title | "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure."xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/volume | "259"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://purl.uniprot.org/core/volume | "259"xsd:string |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8676381 |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8676381 |
| http://purl.uniprot.org/citations/8676381 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8676381 |
| http://purl.uniprot.org/citations/8676381 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8676381 |
| http://purl.uniprot.org/citations/8676381 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8676381 |