title: Pericyclic reactions catalyzed by chorismate-utilizing enzymes.
abstract: One of the fundamental questions of enzymology is how catalytic power is derived. This review focuses on recent developments in the structure--function relationships of chorismate-utilizing enzymes involved in siderophore biosynthesis to provide insight into the biocatalysis of pericyclic reactions. Specifically, salicylate synthesis by the two-enzyme pathway in Pseudomonas aeruginosa is examined. The isochorismate-pyruvate lyase is discussed in the context of its homologues, the chorismate mutases, and the isochorismate synthase is compared to its homologues in the MST family (menaquinone, siderophore, or tryptophan biosynthesis) of enzymes. The tentative conclusion is that the activities observed cannot be reconciled by inspection of the active site participants alone. Instead, individual activities must arise from unique dynamic properties of each enzyme that are tuned to promote specific chemistries.
authors.affiliation: Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States. lamb@ku.edu
authors.forename: Audrey L
authors.initials: AL
authors.lastname: Lamb
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D001665:Binding Sites; D002384:Catalysis; D002826:Chorismate Mutase / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D018360:Crystallography, X-Ray; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011550:Pseudomonas aeruginosa / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D007527:Isoenzymes; D002826:Chorismate Mutase