Application of a Plasmid Carrying a Gene for Orotate Phosphoribosyltransferase (pyrE) to Orotidine-5-monophosphate Production in Escherichia coli K-12

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Two kilobase (2.0kb) DNA fragments bearing a gene (pyrE) for orotate phosphoribosyltransferase (OPTase) were cloned into pBR322, from both Escherichia coli K-12 C600 and its derivative, purine-sensitive mutant PS100 (caused, by a pyrE mutation). Introduction of the resulting hybrid plasmids (designated as pNE24 with DNA from C600, and pNE31 with DNA from PS100) into E. coli K-12 increased the amount of OPTase in the host cells to 30-80 fold. The PS100 cells with pNE31 overproduced a mutant-type OPTase with a decreased level of activity as compared to the wild-type OPTase. The purine-sensitive phenotype of PS100 was completely suppressed by introduction of either pNE24 or pNE31. In a reaction involving the conversion of orotate to orotidine-5-monophosphate (OMP) by an E. coli crude extract, the increased OPTase activity on the use of the hybrid plasmid, pNE24, was favorable for a high conversion rate.
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