| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/2000/01/rdf-schema#comment | "D-amino acids exist in living organisms as specialized components of many different machineries. Biosynthesis of D-amino acids from racemization of predominant L-enantiomers is catalyzed by a single enzyme. Here, we report the finding of a novel 2-component amino acid racemase for D-to-L inversion in D-arginine metabolism of Pseudomonas aeruginosa. From DNA microarray analysis, the putative dauBAR operon (for D-arginine utilization) of unknown functions was found to be highly induced by D-arginine. The importance of the dau operon in D-arginine metabolism was demonstrated by the findings that strains with a lesion at dauA or dauB failed to use D-arginine as sole carbon source. Two lines of evidence suggest that DauA and DauB are required for D-to-L racemization of arginine. First, growth complementation of an L-arginine auxotroph by D-arginine was abolished by a lesion at dauA or dauB. Second, D-arginine induced L-arginine-specific genes in the parental strain PAO1 but not in its dauA or dauB mutants. This hypothesis was further supported by activity measurements of the purified enzymes: DauA catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH. Thus, we propose that DauA and DauB are coupled catabolic and anabolic dehydrogenases to perform D-to-L racemization of arginine, which serves as prerequisite of D-arginine utilization through L-arginine catabolic pathways."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0808269106"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0808269106"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/author | "Li C."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/author | "Li C."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/author | "Lu C.D."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/author | "Lu C.D."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/pages | "906-911"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/pages | "906-911"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/title | "Arginine racemization by coupled catabolic and anabolic dehydrogenases."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/title | "Arginine racemization by coupled catabolic and anabolic dehydrogenases."xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/volume | "106"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://purl.uniprot.org/core/volume | "106"xsd:string |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19139398 |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19139398 |
| http://purl.uniprot.org/citations/19139398 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19139398 |
| http://purl.uniprot.org/citations/19139398 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19139398 |
| http://purl.uniprot.org/citations/19139398 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19139398 |