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  • Title: A membrane-bound prenyltransferase catalyzes the O-prenylation of 1,6-dihydroxyphenazine in the marine bacterium Streptomyces sp. CNQ-509.
    Author: Zeyhle P, Bauer JS, Steimle M, Leipoldt F, Rösch M, Kalinowski J, Gross H, Heide L.
    Journal: Chembiochem; 2014 Nov 03; 15(16):2385-92. PubMed ID: 25224759.
    Abstract:
    Streptomyces sp. CNQ-509 produces the rare O-prenylated phenazines marinophenazines A and B. To identify the enzyme catalyzing the O-prenyl transfer in marinophenazine biosynthesis, we sequenced the genome of S. sp. CNQ-509. This led to the identification of two genomic loci harboring putative phenazine biosynthesis genes. The first locus contains orthologues for all seven genes involved in phenazine-1-carboxylic acid biosynthesis in pseudomonads. The second locus contains two known phenazine biosynthesis genes and a putative prenyltransferase gene termed cnqPT1. cnqPT1 codes for a membrane protein with sequence similarity to the prenyltransferase UbiA of ubiquinone biosynthesis. The enzyme CnqPT1 was identified as a 1,6-dihydroxyphenazine geranyltransferase, which catalyzes the C-O bond formation between C-1 of the geranyl moiety and O-6 of the phenazine scaffold. CnqPT1 is the first example of a prenyltransferase catalyzing O-prenyl transfer to a phenazine.
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