This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis → Polyprenyl Biosynthesis|
Some taxa known to possess this pathway include : Actinomyces bovis, Actinomyces israelii, Actinomyces viscosus, Agrobacterium tumefaciens, Bacteroides eggerthii, Bacteroides fragilis, Bacteroides ovatus, Bacteroides thetaiotaomicron, Bacteroides vulgatus, Bradyrhizobium japonicum, Brucella abortus, Brucella melitensis, Corynebacterium flavescens, Corynebacterium nephridii, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter oxydans, Homo sapiens, Komagataeibacter xylinus, Leifsonia aquatica, Nocardiopsis dassonvillei, Parabacteroides distasonis, Paracoccus denitrificans, Porphyromonas asaccharolytica, Prevotella melaninogenica, Prevotella oralis, Pseudomonas denitrificans, Rathayibacter iranicus, Rathayibacter tritici, Rhodobacter sphaeroides, Rhodomicrobium vannielii, Rhodopseudomonas palustris, Rhodospirillum rubrum, Schizosaccharomyces pombe, Serratia plymuthica, Xanthobacter autotrophicus
In this pathway multiple units of isopentenyl diphosphate (IPP) undergo a series of polymerizations to form a polyisoprenoid chain.
The sequential addition of isoprenyl units to (2E,6E)-farnesyl diphosphate is performed by polyprenyl diphosphate synthase enzymes such as the Escherichia coli K-12 enzyme octaprenyl diphosphate synthase or the human decaprenyl diphosphate synthase.
Additional isoprenoid units are added to a maximal length that is determined by the specific enzyme. Most organisms generate polyprenyl chains of predominantly one length. Once completed, the polyprenyl chain is incorporated into other molecules, such as quinones. The enzyme that attaches the polyprenyl chain to the quinone precursor molecule does not have a preference towards a particular length. Thus, the length of the polyprenyl chain in the mature quinone molecule is determined by the predominant polyprenyl diphosphate synthase enzyme of the organism.
In most organisms there is one type of a predominant quinone, with a specific polyprenyl chain length. However, most organisms also have minor amounts of quinones with a different polyprenyl chain length. For a review detailing the polyprenyl chain length in different bacteria, see [Collins81a].
Superpathways: superpathway of menaquinol-10 biosynthesis
Mollet07: Mollet J, Giurgea I, Schlemmer D, Dallner G, Chretien D, Delahodde A, Bacq D, de Lonlay P, Munnich A, Rotig A (2007). "Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders." J Clin Invest 117(3);765-72. PMID: 17332895
Rotig00: Rotig A, Appelkvist EL, Geromel V, Chretien D, Kadhom N, Edery P, Lebideau M, Dallner G, Munnich A, Ernster L, Rustin P (2000). "Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency." Lancet 356(9227);391-5. PMID: 10972372
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