| http://purl.uniprot.org/citations/17428786 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17428786 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17428786 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/17428786 | http://www.w3.org/2000/01/rdf-schema#comment | "The complete degradation of uric acid to (S)-allantoin, as recently elucidated, involves three enzymatic reactions. Inactivation by pseudogenization of the genes of the pathway occurred during hominoid evolution, resulting in a high concentration of urate in the blood and susceptibility to gout. Here, we describe the 1.8A resolution crystal structure of the homodimeric 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase, which catalyzes the last step in the urate degradation pathway, for both ligand-free enzyme and enzyme in complex with the substrate analogs (R)-allantoin and guanine. Each monomer comprises ten alpha-helices, grouped into two domains and assembled in a novel fold. The structure and the mutational analysis of the active site have allowed us to identify some residues that are essential for catalysis, among which His-67 and Glu-87 appear to play a particularly significant role. Glu-87 may facilitate the exit of the carboxylate group because of electrostatic repulsion that destabilizes the ground state of the substrate, whereas His-67 is likely to be involved in a protonation step leading to the stereoselective formation of the (S)-allantoin enantiomer as reaction product. The structural and functional characterization of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase can provide useful information in view of the potential use of this enzyme in the enzymatic therapy of gout."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m701297200"xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m701297200"xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Zanotti G."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Zanotti G."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Cendron L."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Cendron L."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Percudani R."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Percudani R."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Ramazzina I."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Ramazzina I."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Berni R."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Berni R."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Folli C."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/author | "Folli C."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/pages | "18182-18189"xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/pages | "18182-18189"xsd:string |
| http://purl.uniprot.org/citations/17428786 | http://purl.uniprot.org/core/title | "The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation."xsd:string |