Photochromic derivatives of indigo: historical overview of development, challenges and applications

• Gökhan Kaplan,
• Zeynel Seferoğlu and
• Daria V. Berdnikova

Beilstein J. Org. Chem. 2024, 20, 228–242, doi:10.3762/bjoc.20.23

• using heme-containing oxygenases (cytochrome P450 monooxygenases, styrene/indole monooxygenases, flavin-containing monooxygenases, Baeyer–Villiger monooxygenases, etc.) or non-heme iron oxygenases (naphthalene dioxygenases, multicomponent phenol hydroxylases) [5][6][7][8]. The synthetic approaches

Cytochrome P450 monooxygenase-mediated tailoring of triterpenoids and steroids in plants

• Karan Malhotra and
• Jakob Franke

Beilstein J. Org. Chem. 2022, 18, 1289–1310, doi:10.3762/bjoc.18.135

• steroids in plants as a starting point for future research. Keywords: biosynthesis; CYPs; cytochrome P450 monooxygenases; plants; steroid; sterol; triterpene; triterpenoid; Introduction Triterpenoids are a large class of natural products derived from precursors containing 30 carbon atoms and composed of

• steroids from plants lies in their extensive oxidative tailoring, which in many cases is carried out by cytochrome P450 monooxygenases (CYPs). CYPs represent one of the largest superfamilies of enzymes in plants; in many species, around 1% of all genes encode CYPs [6]. CYPs are well-known for their

• addition, readers might also be interested in other excellent reviews or resources providing a more general overview over plant CYPs or CYPs from other plant pathways [6][8][9][10][11][12][13]. Review Nomenclature Considering the enormous numbers of genes encoding cytochrome P450 monooxygenases in plants

A Streptomyces P450 enzyme dimerizes isoflavones from plants

• Run-Zhou Liu,
• Shanchong Chen and
• Lihan Zhang

Beilstein J. Org. Chem. 2022, 18, 1107–1115, doi:10.3762/bjoc.18.113

• [1][10][11][12][13][14]. In plants and fungi, laccases and cytochrome P450 monooxygenases play pivotal roles in the biaryl bond formation of various polyketide dimers [10][15][16]. In contrast, in bacteria, P450 enzymes are the dominant catalysts, but no laccases have been reported for dimerization

Phylogenomic analyses and distribution of terpene synthases among Streptomyces

• Lara Martín-Sánchez,
• Kumar Saurabh Singh,
• Mariana Avalos,
• Gilles P. van Wezel,
• Jeroen S. Dickschat and
• Paolina Garbeva

Beilstein J. Org. Chem. 2019, 15, 1181–1193, doi:10.3762/bjoc.15.115

• the recombinant enzyme from Streptomyces malaysiensis [43]. The diterpene 7 is a precursor to the lysophospholipase inhibitor cyclooctatin (20) formed by the action of two genetically clustered cytochrome P450 monooxygenases CotB3 and CotB4 (Scheme 4) [40][44], while no derivatives from 8 are

Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934

• Veronika Ulrich,
• Clara Brieke and
• Max J. Cryle

Beilstein J. Org. Chem. 2016, 12, 2849–2864, doi:10.3762/bjoc.12.284

• generation GPAs in clinical use are all entirely derived from in vivo biosynthesis [1][2]. The biosynthesis of GPAs is based around the initial synthesis of the linear heptapeptide by a type-I non-ribosomal peptide synthetase (NRPS) [5][6] and its subsequent modification by cytochrome P450 monooxygenases [7

A detailed view on 1,8-cineol biosynthesis by Streptomyces clavuligerus

• Jan Rinkel,
• Patrick Rabe,
• Laura zur Horst and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2016, 12, 2317–2324, doi:10.3762/bjoc.12.225

• representing various stereoisomers and constitutional isomers with different positioning of olefinic double bonds or alcohol functions are known just for sesquiterpenes [11]. The structural diversity of terpenoids can be further increased by the action of tailoring enzymes such as cytochrome P450

• monooxygenases and acyl transferases [12][13]. Very few cases are known in which terpene cyclases generate an achiral product as exemplified by the monoterpene 1,8-cineol (eucalyptol, 1) and the sesquiterpenes germacrene B (2) and α-humulene (3) (Figure 1). A direct 1,6-cyclisation of the monoterpene precursor

Biosynthesis of oxygen and nitrogen-containing heterocycles in polyketides

• Franziska Hemmerling and
• Frank Hahn

Beilstein J. Org. Chem. 2016, 12, 1512–1550, doi:10.3762/bjoc.12.148

• example epothilone A (119) and oleandomycin (120) (Figure 4) [123][124][125]. Epoxides result from oxidation of olefins by oxidoreductases, mostly cytochrome P450 monooxygenases or FMOs. Alternative mechanisms, such as reactions between carbenes and carbonyls (analogous to the synthetic Corey–Chaykovsky

Active site diversification of P450cam with indole generates catalysts for benzylic oxidation reactions

• Paul P. Kelly,
• Anja Eichler,
• Susanne Herter,
• David C. Kranz,
• Nicholas J. Turner and
• Sabine L. Flitsch

Beilstein J. Org. Chem. 2015, 11, 1713–1720, doi:10.3762/bjoc.11.186

• low cost starting materials [1]. One of the most attractive reagents in terms of cost and environmental impact for hydrocarbon oxidation is oxygen in the presence of a catalyst. In this context enzymatic oxidations are attractive, in particular cytochrome P450 monooxygenases (P450s or CYPs) due to

• Paul P. Kelly Anja Eichler Susanne Herter David C. Kranz Nicholas J. Turner Sabine L. Flitsch School of Chemistry & Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, M1 7DN, Manchester, United Kingdom 10.3762/bjoc.11.186 Abstract Cytochrome P450

• monooxygenases are useful biocatalysts for C–H activation, and there is a need to expand the range of these enzymes beyond what is naturally available. A panel of 93 variants of active self-sufficient P450cam[Tyr96Phe]-RhFRed fusion enzymes with a broad diversity in active site amino acids was developed by

Selective allylic hydroxylation of acyclic terpenoids by CYP154E1 from Thermobifida fusca YX

• Anna M. Bogazkaya,
• Clemens J. von Bühler,
• Sebastian Kriening,
• Alexandrine Busch,
• Alexander Seifert,
• Jürgen Pleiss,
• Sabine Laschat and
• Vlada B. Urlacher

Beilstein J. Org. Chem. 2014, 10, 1347–1353, doi:10.3762/bjoc.10.137

• terpenoids in plants represents the most prominent example [14]. Heme-containing cytochrome P450 monooxygenases (P450 or CYP) are predominantly responsible for structural and functional diversity of terpenoids: allylic hydroxylation of parental monoterpenes leads to further diversification via sequential