Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa.
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pchB alone converts isochorismate to salicylate in an E. coli entB strain; pchBA are necessary for salicylate formation in P. aeruginosa.
"an entB mutant of E. coli blocked in the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate formed salicylate when transformed with a pchB expression construct"
Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities.
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Purified PchB is a cofactor-independent isochorismate pyruvate lyase with a secondary chorismate mutase activity.
"In the reaction catalyzed by this enzyme, isochorismate --> salicylate + pyruvate, no cofactors appear to be required."
Isochorismate pyruvate lyase: a pericyclic reaction mechanism?
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IPL reaction proceeds with quantitative C2 to C9 hydrogen transfer, consistent with a pericyclic mechanism.
"the label is quantitatively transferred from C2 to C9"
Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme.
pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42.
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The physiological role of PchB is salicylate production for pyochelin; the mutase activity is non-physiological.
"has non-physiological chorismate mutase activity, albeit with considerably lower catalytic efficiency than for the lyase activity"