| http://purl.uniprot.org/citations/12144777 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12144777 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12144777 | http://www.w3.org/2000/01/rdf-schema#comment | "Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(02)00632-0"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(02)00632-0"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Adachi H."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Adachi H."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Satow Y."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Satow Y."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Tsujimoto M."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Tsujimoto M."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Nitanai Y."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/author | "Nitanai Y."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/pages | "177-184"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/pages | "177-184"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/title | "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/title | "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/volume | "321"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://purl.uniprot.org/core/volume | "321"xsd:string |
| http://purl.uniprot.org/citations/12144777 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12144777 |
| http://purl.uniprot.org/citations/12144777 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12144777 |