A Membrane‐Bound Prenyltransferase Catalyzes the O‐Prenylation of 1, 6‐Dihydroxyphenazine in the Marine Bacterium Streptomyces sp. CNQ‐509. Issue 16 (15th September 2014)

• Record Type: Journal Article
• Authors: Zeyhle, Philipp; Bauer, Judith S.; Steimle, Marco; Leipoldt, Franziska; Rösch, Manuela; Kalinowski, Jörn; Gross, Harald; Heide, Lutz
• Is Part Of: Chembiochem. Volume 15:Issue 16(2014)
• Page Start: 2385
• Page End: 2392
• Publication Date: 2014-09-15
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201402394
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p> <italic>Streptomyces</italic> 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 <italic>S.</italic> 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 <italic>cnqPT1. cnqPT1</italic> 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.</p> </abstract>