, Volume 213, Issue 3, pp 134–147

New advances in coenzyme Q biosynthesis

  • Catherine F. Clarke
Focus on Cellular Biochemistry

DOI: 10.1007/BF01282151

Cite this article as:
Clarke, C.F. Protoplasma (2000) 213: 134. doi:10.1007/BF01282151


Coenzyme Q (or ubiquinone) is the product of two distinct biosynthetic pathways: the lipid “tail” of coenzyme Q is formed via the isoprene biosynthetic pathway, and the quinone ring derives from the metabolism of either shikimic acid or tyrosine. In general, eukaryotic organisms use the classical mevalonate pathway to form isopentenyl- and dimethylallyl-diphosphate, the five carbon building blocks of the polyisoprenoid tail, and prokaryotes use 1-deoxy-D-xylulose-5-phosphate, formed via the Rohmer pathway. The quinone ring precursor is 4-hydroxybenzoic acid, which is formed directly from chorismate inSaccharomyces cerevisiae andEscherichia coli, or from tyrosine in animal cells. Ring modification steps including prenylation, decarboxylation, and successive hydroxylation and methylation steps form the fully substituted benzoquinone ring of coenzyme Q. Many of the genes and polypeptides involved in coenzyme Q biosynthesis have been isolated and characterized by utilizing strains ofE. coli andS. cerevisiae with mutations in theubi andCOQ genes, respectively. This article reviews recent progress in characterizing the biosynthesis of coenzyme Q inE. coli, S. cerevisiae, and other eukaryotic organisms.


Ubiquinone Ubiquinone-biosynthetic genes Mitochondrial proteins 

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Catherine F. Clarke
    • 1
  1. 1.Department of Chemistry and BiochemistryUniversity of California Los AngelesLos AngelesUSA

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