| http://purl.uniprot.org/citations/10692366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10692366 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10692366 | http://www.w3.org/2000/01/rdf-schema#comment | "In the arginine biosynthetic pathway of the vast majority of prokaryotes, the formation of ornithine is catalyzed by an enzyme transferring the acetyl group of N-alpha-acetylornithine to glutamate (ornithine acetyltransferase [OATase]) (argJ encoded). Only two exceptions had been reported-the Enterobacteriaceae and Myxococcus xanthus (members of the gamma and delta groups of the class Proteobacteria, respectively)-in which ornithine is produced from N-alpha-acetylornithine by a deacylase, acetylornithinase (AOase) (argE encoded). We have investigated the gene-enzyme relationship in the arginine regulons of two psychrophilic Moritella strains belonging to the Vibrionaceae, a family phylogenetically related to the Enterobacteriaceae. Most of the arg genes were found to be clustered in one continuous sequence divergently transcribed in two wings, argE and argCBFGH(A) ["H(A)" indicates that the argininosuccinase gene consists of a part homologous to known argH sequences and of a 3' extension able to complement an Escherichia coli mutant deficient in the argA gene, encoding N-alpha-acetylglutamate synthetase, the first enzyme committed to the pathway]. Phylogenetic evidence suggests that this new clustering pattern arose in an ancestor common to Vibrionaceae and Enterobacteriaceae, where OATase was lost and replaced by a deacylase. The AOase and ornithine carbamoyltransferase of these psychrophilic strains both display distinctly cold-adapted activity profiles, providing the first cold-active examples of such enzymes."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.6.1609-1615.2000"xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.6.1609-1615.2000"xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Glansdorff N."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Glansdorff N."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Legrain C."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Legrain C."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Xu Y."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Xu Y."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Liang Z."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Liang Z."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Ruger H.J."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/author | "Ruger H.J."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/pages | "1609-1615"xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/pages | "1609-1615"xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/title | "Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/title | "Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase."xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/volume | "182"xsd:string |
| http://purl.uniprot.org/citations/10692366 | http://purl.uniprot.org/core/volume | "182"xsd:string |