1887

Abstract

Chorismate mutase (CM) catalyses the rearrangement of chorismate to prephenate and is also the first and the key enzyme that diverges the shikimate pathway to either tryptophan (Trp) or phenylalanine (Phe) and tyrosine (Tyr). is one of the most important amino acid producers for the fermentation industry and has been widely investigated. However, the gene(s) encoding CM has not been experimentally identified in . In this study, the gene, which was annotated as ‘conserved hypothetical protein’ in the genome, was genetically characterized to be essential for growth in minimal medium, and a mutant deleted of was a Phe and Tyr auxotroph. Genetic cloning and expression of in resulted in the formation of a new protein (NCgl0819) having CM activity. It was concluded that encoded the CM of (CM0819). CM0819 was demonstrated to be a homodimer and is a new member of the monofunctional CMs of the AroQ structural class. The CM0819 activity was not affected by Phe, Tyr or Trp. Two 3-deoxy---heptulosonate 7-phosphate (DAHP) synthases (DS0950 and DS2098, formerly NCgl0950 and NCgl2098) had been previously identified from . CM0819 significantly stimulated DAHP synthase (DS2098) activity. Physical interaction between CM0819 and DS2098 was observed. When CM0819 was present, DS2098 activity was subject to allosteric inhibition by chorismate and prephenate. Conserved hypothetical proteins homologous to CM0819 were identified in all known genomes, suggesting a universal occurrence of CM0819-like CMs in the genus .

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2009-10-01
2020-05-26
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