Structural highlights
Function
[CYC2_STRCO] Tow-domain protein where the N-terminal domain catalyzes the cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture of the sesquiterpene alcohol germacradienol and the sesquiterpene hydrocarbon germacrene D. The C-terminal domain partially converts the germacradienol formed into geosmin, the characteristic odoriferous ('earthy aroma') constituent of Streptomyces species.[1] [2] [3] [4]
References
- ↑ Cane DE, Watt RM. Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1547-51. Epub 2003 Jan 29. PMID:12556563 doi:http://dx.doi.org/10.1073/pnas.0337625100
- ↑ Gust B, Challis GL, Fowler K, Kieser T, Chater KF. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1541-6. Epub 2003 Jan 31. PMID:12563033 doi:http://dx.doi.org/10.1073/pnas.0337542100
- ↑ He X, Cane DE. Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2). J Am Chem Soc. 2004 Mar 10;126(9):2678-9. PMID:14995166 doi:http://dx.doi.org/10.1021/ja039929k
- ↑ Jiang J, He X, Cane DE. Geosmin biosynthesis. Streptomyces coelicolor germacradienol/germacrene D synthase converts farnesyl diphosphate to geosmin. J Am Chem Soc. 2006 Jun 28;128(25):8128-9. PMID:16787064 doi:http://dx.doi.org/10.1021/ja062669x
