| http://purl.uniprot.org/citations/11237598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11237598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11237598 | http://www.w3.org/2000/01/rdf-schema#comment | "The N-carbamoyl-D-amino-acid amidohydrolase (D-NCAase) is used on an industrial scale for the production of D-amino acids. The crystal structure of D-NCAase was solved by multiple isomorphous replacement with anomalous scattering using xenon and gold derivatives, and refined to 1.95 A resolution, to an R-factor of 18.6 %. The crystal structure shows a four-layer alpha/beta fold with two six-stranded beta sheets packed on either side by two alpha helices. One exterior layer faces the solvent, whereas the other one is buried and involved in the tight intersubunit contacts. A long C-terminal fragment extends from a monomer to a site near a dyad axis, and associates with another monomer to form a small and hydrophobic cavity, where a xenon atom can bind. Site-directed mutagenesis of His129, His144 and His215 revealed strict geometric requirements of these conserved residues to maintain a stable conformation of a putative catalytic cleft. A region located within this cleft involving Cys172, Glu47, and Lys127 is proposed for D-NCAase catalysis and is similar to the Cys-Asp-Lys site of N-carbamoylsarcosine amidohydrolase. The homologous active-site framework of these enzymes with distinct structures suggests convergent evolution of a common catalytic mechanism."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2000.4380"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2000.4380"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Chen C.-Y."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Chen C.-Y."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Wang W.-C."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Wang W.-C."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Hsu W.-H."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Hsu W.-H."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Chien F.-T."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/author | "Chien F.-T."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/pages | "251-261"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/pages | "251-261"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/title | "Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/title | "Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft."xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/volume | "306"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://purl.uniprot.org/core/volume | "306"xsd:string |
| http://purl.uniprot.org/citations/11237598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11237598 |
| http://purl.uniprot.org/citations/11237598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11237598 |