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Aureothin

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Aureothin
Names
IUPAC name 2-methoxy-3,5-dimethyl-6-oxolan-2-yl]pyran-4-one
Identifiers
CAS Number
3D model (JSmol)
ChEBI
ChemSpider
KEGG
PubChem CID
UNII
InChI
  • InChI=1S/C22H23NO6/c1-13(9-16-5-7-18(8-6-16)23(25)26)10-17-11-19(28-12-17)21-14(2)20(24)15(3)22(27-4)29-21/h5-10,19H,11-12H2,1-4H3/b13-9+,17-10-/t19-/m1/s1Key: GQKXCBCSVYJUMI-WACKOAQBSA-N
SMILES
  • CC1=C(OC(=C(C1=O)C)OC)2C/C(=C/C(=C/C3=CC=C(C=C3)(=O))/C)/CO2
Properties
Chemical formula C22H23NO6
Molar mass 397.427 g·mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C , 100 kPa). Infobox references
Chemical compound

Aureothin is a natural product of a cytotoxic shikimate-polyketide antibiotic with the molecular formula C22H23NO6. Aureothin is produced by the bacterium Streptomyces thioluteus that illustrates antitumor, antifungal, and insecticidal activities and the new aureothin derivatives can be antifungal and antiproliferative. In addition, aureothin, a nitro compound from Streptomyces thioluteus, was indicated to have pesticidal activity against the bean weevil by interfering with mitochondrial respiratory complex II.

Biosynthesis

Regarding the biosynthesis of aureothin, the biosynthetic pathway would be begun with chorismic acid. P-nitrobenzoate is derived from p-aminobenzoate by an N-oxygenase, which is encoded by aurF. The aurF is one of the aureothin biosynthetic enzymes and it is referred to as a nonheme diiron oxygenase that is responsible for converting p-aminobenzoate to p-nitrobenzoate. Moreover, the aurF catalyzes a reaction of a complete six-electron oxidation utilizing two equivalents of dioxygen and two exogenous electrons in order to convert p-aminobenzoate to p-nitrobenzoate. Then, three type I Polyketide Synthases (PKSs), which is encoded by aurA, aurB, and aurC, generates the a polyketide chain using p-nitrobenzoate as a starter unit for the biosynthesis of aureothin. At this point, the repetition that one molecule catalyzes two successive cycles of chain extension would occur in the reaction of the type I Polyketide Synthase (PKS). In particular, the two consecutive cycles containing four times of methylmalonyl-CoA and one time of malonyl-CoA occur during the type I Polyketide Synthase (PKS). After O-methylation is activated by a methyltransferase, which is encoded by aurI, the tetrahydrofuran ring formation is produced by a monooxygenase that is encoded by aurH. Therefore, the final product, aureothin, is produced as a result of the monooxygenase encoded by aurH.

Figure 1: The biosynthetic pathway of Aureothin

References

  1. ^ "Aureothin". Pubchem.
  2. ^ Issues in Chemistry and General Chemical Research (2011 ed.). ScholarlyEditions. 9 January 2012. p. 442. ISBN 978-1-4649-6334-6.
  3. ^ He, Jing; Hertweck, Christian (1 March 2004). "Biosynthetic Origin of the Rare Nitroaryl Moiety of the Polyketide Antibiotic Aureothin: Involvement of an Unprecedented N-Oxygenase". Journal of the American Chemical Society. 126 (12): 3694–3695. doi:10.1021/ja039328t. PMID 15038705.
  4. Hirata, Yoshimasa; Nakata, Hisao; Yamada, Kiyoyuki; Okuhara, Kunio; Naito, Takayuki (January 1961). "The structure of aureothin, a nitro compound obtained from Streptomyces thioluteus". Tetrahedron. 14 (3–4): 252–274. doi:10.1016/S0040-4020(01)92175-1.
  5. Oishi, H.; Hosokawa, T.; Okutomi, T.; Suzuki, K. (1969). "Pesticidal Activity of Aureothin". Agricultural and Biological Chemistry. 33 (12): 1790–1791. doi:10.1080/00021369.1969.10859541.
  6. Friedrich, T; Van Heek, P; Leif, H; Ohnishi, T; Forche, E; Kunze, B; Jansen, R; Trowitzsch-Kienast, W; Hofle, G; Reichenhach, H (1994). "Two binding sites of inhibitors in NADH: ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase". Eur. J. Biochem. 219 (1): 691–698. doi:10.1111/j.1432-1033.1994.tb19985.x. PMID 8307034.
  7. He, Jing; Hertweck, Christian (2004). "Biosynthetic Origin of the Rare Nitroaryl Moiety of the Polyketide Antibiotic Aureothin: Involvement of an Unprecedented N-Oxygenase". J. Am. Chem. Soc. 126 (12): 3694–3695. doi:10.1021/ja039328t. PMID 15038705.
  8. ^ Tsunematsu, Yuta; Hirayama, Yuichiro; Masuya, Takahiro; Watanabe, Kenji (2020). "Oxidative Modification Enzymes in Polyketide Biosynthetic Pathways". Comprehensive Natural Products III (Third Edition). 1: 479–505. doi:10.1016/B978-0-12-409547-2.14637-2. ISBN 9780081026915. S2CID 201202729.
  9. He, Jing; Hertweck, Christian (2005). "Functional Analysis of the Aureothin Iterative Type I Polyketide Synthase". ChemBioChem. 6 (5): 908–912. doi:10.1002/cbic.200400333. PMID 15812854. S2CID 27585538.
  10. He, Jing; Hertweck, Christian (2004). "Biosynthetic Origin of the Rare Nitroaryl Moiety of the Polyketide Antibiotic Aureothin: Involvement of an Unprecedented N-Oxygenase". J. Am. Chem. Soc. 126 (12): 3694–3695. doi:10.1021/ja039328t. PMID 15038705.
  11. Sugimoto, Yuki; Ishida, Keishi; Traitcheva, Nelly; Busch, Benjamin; Dahse, Hans-Martin; Hertweck, Christian. "Freedom and Constraint in Engineered Noncolinear Polyketide Assembly Lines". ChemBioChem. 10 (7): 1225–1232.
  12. Sakuda, Shohei; Kimura, Makoto (2010). "Toxins of Microorganisms". Comprehensive Natural Products II. 4: 411–455. doi:10.1016/B978-008045382-8.00102-7. ISBN 9780080453828.

Further reading

  • Natural Product Biosynthesis by Microorganisms and Plants Part C. Academic Press. 31 December 2012. p. 216. ISBN 978-0-12-404617-7.
  • Strategies and Tactics in Organic Synthesis. Elsevier. 4 October 2016. p. 120. ISBN 978-0-08-100762-4.
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