Oxidative Decarboxylierung von kurzkettigen Fettsäuren zu 1‐Alkenen

Dennig, Alexander; Kühn, Melanie; Tassoti, Sebastian; Thiessenhusen, Anja; Gilch, Stefan; Bülter, Thomas; Haas, Thomas; Hall, Mélanie; Faber, Kurt

doi:10.1002/ange.201502925

Cited by 29 publications

(25 citation statements)

References 39 publications

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“…alone), in the presence of H 2 O 2 . Bacterial P450s are also known to decarboxylate fatty acids, but in this case n −1 terminal alkenes (Scheme d), instead of chain‐shortened fatty acids, are formed …”

Section: Figurementioning

confidence: 99%

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Olmedo

Río

Kiebist

et al. 2017

Chemistry A European J

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A recently discovered peroxygenase from the fungus Marasmius rotula (MroUPO) is able to catalyze the progressive one‐carbon shortening of medium and long‐chain mono‐ and dicarboxylic acids by itself alone, in the presence of H2O2. The mechanism, analyzed using H2 18O2, starts with an α‐oxidation catalyzed by MroUPO generating an α‐hydroxy acid, which is further oxidized by the enzyme to a reactive α‐keto intermediate whose decarboxylation yields the one‐carbon shorter fatty acid. Compared with the previously characterized peroxygenase of Agrocybe aegerita, a wider heme access channel, enabling fatty acid positioning with the carboxylic end near the heme cofactor (as seen in one of the crystal structures available) could be at the origin of the unique ability of MroUPO shortening carboxylic acid chains.

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Section: Figurementioning

confidence: 99%

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Olmedo

Río

Kiebist

et al. 2017

Chemistry A European J

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“…The CYP152A1 pET‐28(a)+ expression plasmid was prepared as described (internal plasmid number pEG301) …”

Section: Methodsmentioning

confidence: 99%

“…Due to the diversity of the enzyme family, no universal electron transfer system is known and the identification of a suitable electron transfer system for specific CYPs remains challenging . Alternatively, a few CYPs are able to utilize H 2 O 2 as oxygen and electron‐donor such as P450 peroxygenases from the CYP152 family . In this case, no electron transfer system is required and uncoupling reactions are avoided to a large extend …”

Section: Introductionmentioning

confidence: 99%

“…Unfortunately, the enzyme shows low activity and is poorly expressed . OleT (CYP152 L1) originates from Jeotgalicoccus species and performs predominantly oxidative decarboxylation besides α‐ and β‐hydroxylation or desaturation if branched carboxylic acids are used as substrates …”

Section: Introductionmentioning

confidence: 99%

“… Fatty acid (decanoic acid, C 10 ) hydroxylation by CYP152A1 variants using CamAB as electron transfer system and FDH/formate for cofactor recycling.…”

Section: Introductionmentioning

confidence: 99%

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Controlling the Regioselectivity of Fatty Acid Hydroxylation (C₁₀) at α‐ and β‐Position by CYP152A1 (P450Bsβ) Variants

et al. 2019

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Regioselective hydroxylation on inactivated C−H bonds is among the dream reactions of organic chemists. Cytochrome P450 enzymes (CYPs) perform this reaction in general with high regio‐ and stereoselectivity (e. g. for steroids as substrates). Furthermore, enzyme engineering may allow to tune the properties of the enzyme. Regioselective hydroxylation of shorter or linear molecules (fatty acids), however, remains challenging even with this enzyme class, due to the high similarity of the substrate's backbone carbons and their conformational flexibility. CYPs hydroxylating fatty acids selectively in the chemically more distinct α‐ or ω‐ position are well described. In contrast, selective in‐chain hydroxylation of fatty acids lacks precedence. The peroxygenase CYP152A1 (P450Bsβ) is a family member that displays fatty acid hydroxylation at both, the α‐ and β‐position, with preference for the α‐position. Herein we report the influence of hydrophobic active site residues on the hydroxylation pattern of this enzyme. By site directed mutagenesis and combination of the libraries, double and triple mutation variants were identified, which hydroxylated decanoic acid (C10) with improved regio‐selectivity in the β‐position. Variants were identified with a 10‐fold increase of the β‐regioselectivity (expressed as α/β‐ratio) compared to the wild type. In total 103 variants of CYP152A1 (P450Bsβ) were investigated.

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Cascade Biocatalysis for Sustainable Asymmetric Synthesis: From Biobased l‐Phenylalanine to High‐Value Chiral Chemicals

Zhou

2016

Angewandte Chemie

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Sustainable synthesis of useful and valuable chiral fine chemicals from renewable feedstocks is highly desirable but remains challenging.R eported herein is ad esigned and engineered set of unique non-natural biocatalytic cascades to achieve the asymmetric synthesis of chiral epoxide,d iols, hydroxy acid, and amino acid in high yield and with excellent ee values from the easily available biobased l-phenylalanine. Each of the cascades was efficiently performed in one pot by using the cells of asingle recombinant strain over-expressing 4-10 different enzymes.T he cascade biocatalysis approachi s promising for upgrading biobased bulk chemicals to highvalue chiral chemicals.Inaddition, combining the non-natural enzyme cascades with the natural metabolic pathway of the host strain enabled the fermentative production of the chiral fine chemicals from glucose.

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Oxidative Decarboxylierung von kurzkettigen Fettsäuren zu 1‐Alkenen

Cited by 29 publications

References 39 publications

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Controlling the Regioselectivity of Fatty Acid Hydroxylation (C₁₀) at α‐ and β‐Position by CYP152A1 (P450Bsβ) Variants

Cascade Biocatalysis for Sustainable Asymmetric Synthesis: From Biobased l‐Phenylalanine to High‐Value Chiral Chemicals

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Oxidative Decarboxylierung von kurzkettigen Fettsäuren zu 1‐Alkenen

Cited by 29 publications

References 39 publications

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Fatty Acid Chain Shortening by a Fungal Peroxygenase

Controlling the Regioselectivity of Fatty Acid Hydroxylation (C10) at α‐ and β‐Position by CYP152A1 (P450Bsβ) Variants

Cascade Biocatalysis for Sustainable Asymmetric Synthesis: From Biobased l‐Phenylalanine to High‐Value Chiral Chemicals

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Controlling the Regioselectivity of Fatty Acid Hydroxylation (C₁₀) at α‐ and β‐Position by CYP152A1 (P450Bsβ) Variants