ArticlePloS one2014
Genome-based discovery of a novel membrane-bound 1,6-dihydroxyphenazine prenyltransferase from a marine actinomycete.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 24 citations in OpenAlex.
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- Characterization of the diastaphenazine/izumiphenazine C biosynthetic gene cluster from plant endophyte Streptomyces diastaticus W2.Microbial biotechnology · 2022Article
- Identification of the new prenyltransferase Ubi-297 from marine bacteria and elucidation of its substrate specificity.Beilstein journal of organic chemistry · 2022Article
- Bacterial terpenome.Natural product reports · 2021Review
- Isolation ofCommunications biology · 2019Article
- Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces sp. Z26, Isolated from Potato Rhizosphere in Morocco.Microbiology resource announcements · 2019Article
- Draft Genome Sequence of the Xanthocidin-Producing StrainMicrobiology resource announcements · 2018Article
- Biogenetic Relationships of Bioactive Sponge Merotriterpenoids.Marine drugs · 2017Review
- Computational-guided discovery and characterization of a sesquiterpene synthase from Streptomyces clavuligerus.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway.The Journal of biological chemistry · 2014Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, novel prenylated derivatives of 1,6-dihydroxyphenazine have been isolated from the marine sponge-associated Streptomyces sp. SpC080624SC-11. Genome sequencing of this strain now revealed a gene cluster containing all genes necessary for the synthesis of the phenazine and the isoprenoid moieties. Unexpectedly, however, the cluster did not contain a gene with similarity to previously investigated phenazine prenyltransferases, but instead a gene with modest similarity to the membrane-bound prenyltransferases of ubiquinone and menaquinone biosynthesis. Expression of this gene in E. coli and isolation of the membrane fraction proved that the encoded enzyme, Mpz10, catalyzes two successive prenylations of 1,6-dihydroxyphenazine. Mpz10 is the first example of a membrane-bound enzyme catalyzing the prenylation of a phenazine substrate, and one of few examples of membrane-bound enzymes involved in the prenylation of aromatic secondary metabolites in microorganisms.
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