| http://purl.uniprot.org/citations/11937513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11937513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11937513 | http://www.w3.org/2000/01/rdf-schema#comment | "Isochorismate pyruvate-lyase (IPL), the second enzyme of pyochelin biosynthesis and the product of the pchB gene, was purified to homogeneity from Pseudomonas aeruginosa. In the reaction catalyzed by this enzyme, isochorismate --> salicylate + pyruvate, no cofactors appear to be required. At the pH optimum (pH 6.8), the enzyme displayed Michaelis-Menten kinetics, with an apparent K(m) of 12.5 microm for isochorismate and a kcat of 106 min(-1), calculated per monomer. The native enzyme behaved as a homodimer, as judged by molecular sieving chromatography, electrophoresis under nondenaturing conditions, and cross-linking experiments. PchB has approximately 20% amino acid sequence identity with AroQ-class chorismate mutases (CMs). Chorismate was shown to be converted to prephenate by purified PchB in vitro, with an apparent K(m) of 150 microm and a kcat of 7.8 min(-1). An oxabicyclic diacid transition state analog and well characterized inhibitor of CMs competitively inhibited both IPL and CM activities of PchB. Moreover, a CM-deficient Escherichia coli mutant, which is auxotrophic for phenylalanine and tyrosine, was functionally complemented by the cloned P. aeruginosa pchB gene for growth in minimal medium. A mutant form of PchB, in which isoleucine 88 was changed to threonine, had no detectable IPL activity, but retained wild-type CM activity. In conclusion, the 11.5-kDa subunit of PchB appears to contain a single active site involved in both IPL and CM activity."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m202410200"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m202410200"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Kast P."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Kast P."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Haas D."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Haas D."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Gaille C."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/author | "Gaille C."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/pages | "21768-21775"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/pages | "21768-21775"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/title | "Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/title | "Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities."xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11937513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11937513 |
| http://purl.uniprot.org/citations/11937513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11937513 |
| http://purl.uniprot.org/citations/11937513 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11937513 |
| http://purl.uniprot.org/citations/11937513 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11937513 |