Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

Reisky, Lukas; Büchsenschütz, Hanna Christiane; Engel, Jennifer; Song, Tao; Schweder, Thomas; Hehemann, Jan‐Hendrik; Bornscheuer, Uwe T.

doi:10.1038/s41589-018-0005-8

Cited by 49 publications

(52 citation statements)

References 35 publications

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“…P450s are ubiquitous heme enzymes, catalyzing a wide range of redox reactions, and their potential role in biomass conversion remains obscure. Most interestingly, in 2018, Reisky et al described P450s catalyzing the oxidative demethylation of carbohydrates present in algal polysaccharides, likely decreasing the recalcitrance of this marine biomass (285). A role of P450s in lignocellulose conversion is plausible since they are more abundant in wood-decaying basidiomycetes than in non-wood-decaying relatives (286).…”

Section: Enzyme Production During Lignocellulose Depolymerizationmentioning

confidence: 99%

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Bissaro

Várnai

Røhr

et al. 2018

Microbiol Mol Biol Rev

240

246

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SUMMARYBiomass constitutes an appealing alternative to fossil resources for the production of materials and energy. The abundance and attractiveness of vegetal biomass come along with challenges pertaining to the intricacy of its structure, evolved during billions of years to face and resist abiotic and biotic attacks. To achieve the daunting goal of plant cell wall decomposition, microorganisms have developed many (enzymatic) strategies, from which we seek inspiration to develop biotechnological processes. A major breakthrough in the field has been the discovery of enzymes today known as lytic polysaccharide monooxygenases (LPMOs), which, by catalyzing the oxidative cleavage of recalcitrant polysaccharides, allow canonical hydrolytic enzymes to depolymerize the biomass more efficiently. Very recently, it has been shown that LPMOs are not classical monooxygenases in that they can also use hydrogen peroxide (H2O2) as an oxidant. This discovery calls for a revision of our understanding of how lignocellulolytic enzymes are connected since H2O2is produced and used by several of them. The first part of this review is dedicated to the LPMO paradigm, describing knowns, unknowns, and uncertainties. We then present different lignocellulolytic redox systems, enzymatic or not, that depend on fluxes of reactive oxygen species (ROS). Based on an assessment of these putatively interconnected systems, we suggest that fine-tuning of H2O2levels and proximity between sites of H2O2production and consumption are important for fungal biomass conversion. In the last part of this review, we discuss how our evolving understanding of redox processes involved in biomass depolymerization may translate into industrial applications.

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Section: Enzyme Production During Lignocellulose Depolymerizationmentioning

confidence: 99%

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Bissaro

Várnai

Røhr

et al. 2018

Microbiol Mol Biol Rev

240

246

View full text Add to dashboard Cite

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“…Oxygen‐activating heme enzymes catalyze a wide range of reactions with high selectivity and catalytic efficiency . Side reactions, if any, are reduced to a minimum owing to the role of the protein matrix, which regulates access/release of the substrate.…”

Section: Figurementioning

confidence: 99%

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

et al. 2018

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Rational design provides an attractive strategy to tune and control the reactivity of bioinspired catalysts. Although there has been considerable progress in the design of heme oxidase mimetics with active-site environments of ever-growing complexity and catalytic efficiency, their stability during turnover is still an open challenge. Herein, we show that the simple incorporation of two 2-aminoisobutyric acids into an artificial peptide-based peroxidase results in a new catalyst (Fe -MC6*a) with higher resistance against oxidative damage and higher catalytic efficiency. The turnover number of this catalyst is twice as high as that of its predecessor. These results point out the protective role exerted by the peptide matrix and pave the way to the synthesis of robust bioinspired catalysts.

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“…Use of the strictly regulated pBAD33 expression vector was the key factor for the production of CYP109Q5 from C. apiculatus DSM436. It turned out that the activity reconstitution was enabled using CamA/CamB as heterologous redox partners which are thus suitable to supply electrons to multiple P450s (Bell et al, 2010;Reisky et al, 2018). The enzyme displayed a wide range of catalysed reactions from diverse norisoprenoids, steroids, non-steroidal antiinflammatory drugs to mono-and sesquiterpenes (Fig.…”

Section: Discussionmentioning

confidence: 99%

Characterization and structure‐guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436

Klenk

Dubiel

Sharma

et al. 2018

Microbial Biotechnology

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Summary One of the major challenges in chemical synthesis is the selective oxyfunctionalization of non‐activated C‐H bonds, which can be enabled by biocatalysis using cytochrome P450 monooxygenases. In this study, we report on the characterization of the versatile CYP 109Q5 from Chondromyces apiculatus DSM 436, which is able to functionalize a wide range of substrates (terpenes, steroids and drugs), including the ring of β‐ionone in non‐allylic positions. The crystal structure of CYP 109Q5 revealed flexibility within the active site pocket that permitted the accommodation of bulky substrates, and enabled a structure‐guided approach to engineering the enzyme. Some variants of CYP 109Q5 displayed a switch in selectivity towards the non‐allylic positions of β‐ionone, allowing the simultaneous production of 2‐ and 3‐hydroxy‐β‐ionone, which are chemically challenging to synthesize and are important precursors for carotenoid synthesis. An efficient whole‐cell system finally enabled the production of up to 0.5 g l −1 hydroxylated products of β‐ionone; this system can be applied to product identification in further biotransformations. Overall, CYP 109Q5 proved to be highly evolvable and active. The studies in this work demonstrate that, using rational mutagenesis, the highly versatile CYP 109Q5 generalist can be progressively evolved to be an industrially valuable specialist for the synthesis of specific products.

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Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

Cited by 49 publications

References 35 publications

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design

Characterization and structure‐guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436

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