| http://purl.uniprot.org/citations/12730200 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12730200 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12730200 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12730200 | http://www.w3.org/2000/01/rdf-schema#comment | "A genetic analysis of the anthranilate pathway of quinaldine degradation was performed. A 23-kb region of DNA from Arthrobacter ilicis Rü61a was cloned into the cosmid pVK100. Although Escherichia coli clones containing the recombinant cosmid did not transform quinaldine, cosmids harboring the 23-kb region, or a 10.8-kb stretch of this region, conferred to Pseudomonas putida KT2440 the ability to cometabolically convert quinaldine to anthranilate. The 10.8-kb fragment thus contains the genes coding for quinaldine 4-oxidase (Qox), 1H-4-oxoquinaldine 3-monooxygenase, 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase, and N-acetylanthranilate amidase. The qoxLMS genes coding for the molybdopterin cytosine dinucleotide-(MCD-), FeSI-, FeSII-, and FAD-containing Qox were inserted into the expression vector pJB653, generating pKP1. Qox is the first MCD-containing enzyme to be synthesized in a catalytically fully competent form by a heterologous host, P. putida KT2440 pKP1; the catalytic properties and the UV-visible and EPR spectra of Qox purified from P. putida KT2440 pKP1 were essentially like those of wild-type Qox. This provides a starting point for the construction of protein variants of Qox by site-directed mutagenesis. Downstream of the qoxLMS genes, a putative gene whose deduced amino acid sequence showed 37% similarity to the cofactor-inserting chaperone XdhC was located. Additional open reading frames identified on the 23-kb segment may encode further enzymes (a glutamyl tRNA synthetase, an esterase, two short-chain dehydrogenases/reductases, an ATPase belonging to the AAA family, a 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase/5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase-like protein, and an enzyme of the mandelate racemase group) and hypothetical proteins involved in transcriptional regulation, and metabolite transport."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.M301330200"xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m301330200"xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m301330200"xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kappl R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kappl R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kappl R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kraft R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kraft R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Kraft R."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Fetzner S."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Fetzner S."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Fetzner S."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Hauer B."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Hauer B."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Hauer B."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Huttermann J."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Huttermann J."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Huttermann J."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Parschat K."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Parschat K."xsd:string |
| http://purl.uniprot.org/citations/12730200 | http://purl.uniprot.org/core/author | "Parschat K."xsd:string |