| http://purl.uniprot.org/citations/10464225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10464225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10464225 | http://www.w3.org/2000/01/rdf-schema#comment | "The Pseudomonas aeruginosa fabI structural gene, encoding enoyl-acyl carrier protein (ACP) reductase, was cloned and sequenced. Nucleotide sequence analysis revealed that fabI is probably the last gene in a transcriptional unit that includes a gene encoding an ATP-binding protein of an ABC transporter of unknown function. The FabI protein was similar in size and primary sequence to other bacterial enoyl-ACP reductases, and it contained signature motifs for the FAD-dependent pyridine nucleotide reductase and glucose/ribitol dehydrogenase families, respectively. The chromosomal fabI gene was disrupted, and the resulting mutant was viable but possessed only 62% of the total enoyl-ACP reductase activity found in wild-type cell extracts. The fabI-encoded enoyl-ACP reductase activity was NADH dependent and inhibited by triclosan; the residual activity in the fabI mutant was also NADH dependent but not inhibited by triclosan. An polyhistidine-tagged FabI protein was purified and characterized. Purified FabI (i) could use NADH but not NADPH as a cofactor; (ii) used both crotonyl-coenzyme A and crotonyl-ACP as substrates, although it was sixfold more active with crotonyl-ACP; and (iii) was efficiently inhibited by low concentrations of triclosan. A FabI Gly95-to-Val active-site amino acid substitution was generated by site-directed mutagenesis, and the mutant protein was purified. The mutant FabI protein retained normal enoyl-ACP reductase activity but was highly triclosan resistant. When coupled to FabI, purified P. aeruginosa N-butyryl-L-homoserine lactone (C4-HSL) synthase, RhlI, could synthesize C4-HSL from crotonyl-ACP and S-adenosylmethionine. This reaction was NADH dependent and inhibited by triclosan. The levels of C4-HSL and N-(3-oxo)-dodecanoyl-L-homoserine lactones were reduced 50% in a fabI mutant, corroborating the role of FabI in acylated homoserine lactone synthesis in vivo."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.181.17.5489-5497.1999"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.181.17.5489-5497.1999"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/author | "Hoang T.T."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/author | "Hoang T.T."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/author | "Schweizer H.P."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/author | "Schweizer H.P."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/pages | "5489-5497"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/pages | "5489-5497"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/title | "Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/title | "Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis."xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/volume | "181"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://purl.uniprot.org/core/volume | "181"xsd:string |
| http://purl.uniprot.org/citations/10464225 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10464225 |
| http://purl.uniprot.org/citations/10464225 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10464225 |
| http://purl.uniprot.org/citations/10464225 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10464225 |
| http://purl.uniprot.org/citations/10464225 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10464225 |
| http://purl.uniprot.org/uniprot/Q9ZFE4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10464225 |
| http://purl.uniprot.org/uniprot/Q9ZFE4#attribution-6F8990288EB7097FCF11882BF05E106C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10464225 |