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. 1972 Apr;110(1):18–25. doi: 10.1128/jb.110.1.18-25.1972

Biochemical and Genetic Studies on Ubiquinone Biosynthesis in Escherichia coli K-12: 4-Hydroxybenzoate Octaprenyltransferase

I G Young 1, R A Leppik 1, J A Hamilton 1, F Gibson 1
PMCID: PMC247373  PMID: 4552989

Abstract

Three ubiquinone-deficient mutants of Escherichia coli unable to convert 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate were isolated and examined. The results of genetic analysis suggest that each of the mutants carries a mutation in a gene designated ubiA which can be represented at minute 79 on the E. coli chromosome map. The conversion of 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate, catalyzed by 4-hydroxybenzoate octaprenyltransferase, was studied with a strain of E. coli that is blocked in the common pathway of aromatic biosynthesis and consequently accumulates the precursor of the side chain of ubiquinone. Both the side-chain precursor and 4-hydroxybenzoate octaprenyltransferase were shown to be membrane-bound. The enzyme required Mg2+ for optimal activity. The ubiA− mutants were found to lack 4-hydroxybenozate octaprenyltransferase activity, which suggested that the ubiA gene is the structural gene coding for this enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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