Regiodivergent Baeyer–Villiger oxidation of fused ketone substrates by recombinant whole-cells expressing two monooxygenases from Brevibacterium

Mihovilovic, Marko D.; Kapitán, Peter

doi:10.1016/j.tetlet.2004.02.036

Cited by 41 publications

(18 citation statements)

References 30 publications

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“…Surprisingly, when the homologous enzyme was purified from S. avermitilis it carried out a Baeyer-Villiger ring expansion but with oxygen insertion on the other side of the ketone to give neopentalenolactone D. This is noncanonical since the more electron rich C-C bond generally migrates as the Criegee-type tetrahedral adduct breaks down in chemical and other enzymatic Baeyer-Villiger insertions. 91 It may be that steric crowding dictates formation of the alternate lactone regioisomer in this case.…”

Section: Biosynthetic Niches For Flavoprotein Oxidoreductases: the mentioning

confidence: 96%

Flavoenzymes: Versatile catalysts in biosynthetic pathways

2013

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Riboflavin-based coenzymes, tightly bound to enzymes catalyzing substrate oxidations and reductions, enable an enormous range of chemical transformations in biosynthetic pathways. Flavoenzymes catalyze substrate oxidations involving amine and alcohol oxidations and desaturations to olefins, the latter setting up Diels-Alder cyclizations in lovastatin and solanapyrone biosyntheses. Both C4a and N5 of the flavin coenzymes are sites for covalent adduct formation. For example, the reactivity of dihydroflavins with molecular oxygen leads to flavin-4a-OOH adducts which then carry out a diverse range of oxygen transfers, including Baeyer-Villiger type ring expansions, olefin epoxidations, halogenations via transient HOCl generation, and an oxidative Favorskii rerrangement during enterocin assembly.

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Section: Biosynthetic Niches For Flavoprotein Oxidoreductases: the mentioning

confidence: 96%

Flavoenzymes: Versatile catalysts in biosynthetic pathways

2013

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“…[25] CHMO-type proteins displayed a clean resolution that led to the formation of regioisomeric lactones 4 and 5 in approximately 1:1 ratio and with high optical purities. By contrast, CPMO Coma and CHMO Brevi2 (CPMOtype enzymes) yielded predominantly "normal" lactone 4 in nearly racemic form.…”

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confidence: 99%

Family Clustering of Baeyer–Villiger Monooxygenases Based on Protein Sequence and Stereopreference

et al. 2005

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Die Identifizierung von Enzympaaren mit überlappender Substratspezifität und enantiokomplementären Transformationen ist eine zentrale Herausforderung der Biokatalyse. Enantio‐ und regiodivergente Baeyer‐Villiger‐Oxidationen gelangen mit einer kleinen Bibliothek rekombinanter Escherichia‐coli‐Stämme, die Monooxygenasen unterschiedlichen mikrobiellen Ursprungs exprimieren (siehe Bild). Die auf der Stereopräferenz basierende Gruppenbildung von Enzymen stimmt gut mit der phylogenetischen Nähe überein.

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“…Proposed origin of regiodivergent biooxidation by BVMOs. [54,121]. On these substrates, CHMO-type proteins yield approximately equal amounts of "normal" and "abnormal" lactones in good enantioselectivities for both products.…”

Section: Regiodivergent Transformationsmentioning

confidence: 97%

Enzyme Mediated Baeyer-Villiger Oxidations

Mihovilovic

2006

COC

149

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Oxygenation reactions of ketones to esters are referred to as Baeyer-Villiger oxidations and represent a powerful methodology in synthesis to break carbon-carbon bonds in an oxygen insertion process. Since the seminal work by Adolf Baeyer and Victor Villiger in 1899 substantial progress has been made to understand the mechanism, to predict migratory preference, and to apply this conversion in preparative chemistry. Stereoselective Baeyer-Villiger oxidation of cyclic ketones allows rapid access to chiral lactones as valuable intermediates in enantioselective synthesis. Together with organometal catalysts, biocatalysis offers a "green chemistry" methodology for this transformation. Several organisms have been identified to catalyze this reaction in the course of their metabolic pathways and an increasing number of flavin dependent monooxygenases is reported to accept a multitude of non-natural substrates. Such biocatalysts are used in synthetic chemistry either as isolated enzymes in combination with appropriate cofactor recycling systems or as living whole-cells in native or recombinant form. This review gives an overview of the most abundantly utilized enzymes and the corresponding substrate profiles together with applications in natural product and bioactive compound synthesis. The article focuses on recent developments in biocatalytic Baeyer-Villiger oxidation with promising applications in synthetic chemistry. Complementing these aspects, recent advances in characterizing the biochemistry of Baeyer-Villiger monooxygenases and novel approaches to modify and predict the catalytic performance of these enzymes, which have an impact on the potential as stereoselective catalytic entities, are discussed.Dedicated to Prof. Fritz Sauter on the occasion of his 75th birthday.

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Regiodivergent Baeyer–Villiger oxidation of fused ketone substrates by recombinant whole-cells expressing two monooxygenases from Brevibacterium

Cited by 41 publications

References 30 publications

Flavoenzymes: Versatile catalysts in biosynthetic pathways

Flavoenzymes: Versatile catalysts in biosynthetic pathways

Family Clustering of Baeyer–Villiger Monooxygenases Based on Protein Sequence and Stereopreference

Enzyme Mediated Baeyer-Villiger Oxidations

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