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Search for "cytochrome P450s" in Full Text gives 5 result(s) in Beilstein Journal of Organic Chemistry.
Discovery and biosynthesis of bacterial drimane-type sesquiterpenoids from Streptomyces clavuligerus
Beilstein J. Org. Chem. 2024, 20, 815–822, doi:10.3762/bjoc.20.73
- analogs. This discovery not only broadens the known chemical diversity of DMTs from bacteria, but also provides new insights into DMT biosynthesis in bacteria. Keywords: bacterial terpenoid; cytochrome P450s; drimane-type sesquiterpenoid; Streptomyces clavuligerus; terpenoid biosynthesis; Introduction
- hydrolase domain to form drimenol [21]. Subsequently, this molecule undergoes further modifications by two cytochrome P450s monooxygenases (P450s, DrtC and DrtD) and one acyltransferase (DrtE) to produce calidoustene C [13]. This cyclization is similar with the course of AncC from Antrodia cinnamomea, which
Efficient production of clerodane and ent-kaurane diterpenes through truncated artificial pathways in Escherichia coli
Beilstein J. Org. Chem. 2022, 18, 881–888, doi:10.3762/bjoc.18.89
- cyclase) act on geranylgeranyl diphosphate (GGDP) to perform regio- and stereoselective cyclizations or skeleton rearrangement reactions via carbocation chemistry to form diverse and versatile carbon skeletons; and ii) multiple post-modification enzymes, most often cytochrome P450s, decorate the carbon
Bacterial terpene biosynthesis: challenges and opportunities for pathway engineering
Beilstein J. Org. Chem. 2019, 15, 2889–2906, doi:10.3762/bjoc.15.283
- ], vanadium-dependent bromoperoxidases [61][62], or methyltransferases [63]). In addition, enzymes typically classified as tailoring enzymes, such as flavin-dependent monooxygenases [64] and cytochrome P450s (CYPs) [65], were reported to be involved in noncanonical terpene cyclization. Furthermore, both
- number of bacterial genome sequences available and the development of advanced bioinformatics tools, more type II/I diterpene TC tandems are likely to be discovered. By applying the same combinatorial concept, it is expected that the diterpene chemical space can be significantly expanded. Cytochrome
- P450s CYPs have the ability to install functional groups at nonactivated C–H bonds with exceptional selectivity. In contrast to the common perception of enzymes being highly substrate-specific, many CYPs are able to modify non-natural substrates but retain their high stereo- and regiochemical
Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934
Beilstein J. Org. Chem. 2016, 12, 2849–2864, doi:10.3762/bjoc.12.284
- confirmed that the cytochrome P450s, known as the Oxy enzymes, are each responsible for the installation of a single ring in the GPA aglycones and that there is a conserved order of activity in both type-I and type-IV GPAs. In type-I GPA biosynthesis OxyB acts first to install the C-O-D ring (between
- teicoplanin (tei) X-domain; secondary structure was derived from the Xtei-OxyBtei complex (PDB ID: 4TX3) and is shown above the alignment (α-helices = blue, β-sheets = magenta); the residues crucial for interaction with cytochrome P450s are shown in orange and both the crossover I region (purple) and the
Hydrophobic analogues of rhodamine B and rhodamine 101: potent fluorescent probes of mitochondria in living C. elegans
Beilstein J. Org. Chem. 2012, 8, 2156–2165, doi:10.3762/bjoc.8.243
- xenobiotic detoxification enzymes, including cytochrome P450s, phase-II transferases, and efflux pumps such as P-glycoprotein [35], to reach target tissues [29]. Thus, compounds such as HRB 9 and HR101 10 that show high potency in this animal have passed through a stringent biological filter, providing a
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