1478263-83-0Relevant academic research and scientific papers
A Membrane-Bound Prenyltransferase Catalyzes the O-Prenylation of 1,6-Dihydroxyphenazine in the Marine Bacterium Streptomyces sp. CNQ-509
Zeyhle, Philipp,Bauer, Judith S.,Steimle, Marco,Leipoldt, Franziska,R?sch, Manuela,Kalinowski, J?rn,Gross, Harald,Heide, Lutz
, p. 2385 - 2392 (2014)
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.
A membrane-bound prenyltransferase catalyzes the O-prenylation of 1,6-dihydroxyphenazine in the marine bacterium streptomyces sp. CNQ-509
Zeyhle, Philipp,Bauer, Judith S.,Steimle, Marco,Leipoldt, Franziska,R?sch, Manuela,Kalinowski, J?rn,Gross, Harald,Heide, Lutz
, p. 2385 - 2392 (2015/03/03)
Streptomyces sp. CNQ-509 produces the rare O-prenylated phe-nazines 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 identificatio
