As recently reported, the olefin-forming oxidative decarboxylation of straight-chain C4-C22 carboxylic acids catalyzed by P450 peroxygenase OleTJE constitutes a mild alkene synthesis. The present study shows that structurally different carboxylic acids are also accepted, including those that generate di-substituted olefins. Exploratory mutational experiments lead to increased trans-selectivity.
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http://dx.doi.org/10.1039/c6cc04345c | DOI Listing |
Biotechnol Adv
December 2024
Department of Food Science and Biotechnology, Ewha Womans University, 52 Ewhayeodae-gil, Seodaemun-Gu, Seoul 03760, Republic of Korea.
The selective oxyfunctionalization of unsaturated fatty acids is difficult in chemical reactions, whereas regio- and stereoselective oxyfunctionalization is often performed in biocatalytic synthesis. Fatty acid oxygenases, including hydratases, lipoxygenases, dioxygenases, diol synthases, cytochrome P450 monooxygenases, peroxygenases, and 12-hydroxylases, are used to convert C16 and C18 unsaturated fatty acids to diverse regio- and stereoselective mono-, di-, and trihydroxy fatty acids via selective oxyfunctionalization. The formed hydroxy fatty acids or hydroperoxy fatty acids are metabolized to industrially important oxygenated chemicals such as lactones, green leaf volatiles, and bioplastic monomers, including ω-hydroxy fatty acids, α,ω-dicarboxylic acids, and fatty alcohols, by biocatalysts.
View Article and Find Full Text PDFChembiochem
December 2024
Department of Chemistry, The University of Adelaide, Adelaide, SA, 5005, Australia.
The heme enzymes of the cytochrome P450 superfamily (CYPs) catalyse the selective hydroxylation of unactivated C-H bonds in organic molecules. There is great interest in applying these enzymes as biocatalysts with a focus on self-sufficient CYP 'fusion' enzymes, comprising a single polypeptide chain with the electron transfer components joined to the heme domain. Here we elucidate the function of the self-sufficient CYP116B46 fusion enzyme, from the thermophilic bacterium Tepidiphilus thermophilus.
View Article and Find Full Text PDFAdv Sci (Weinh)
December 2024
Key Laboratory of Photoelectric Conversion and Utilization of Solar Energy, Qingdao New Energy Shandong Laboratory, CAS Key Laboratory of Biofuels, Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.
Amine oxidation is an important organic reaction for the production of high-value N-containing compounds. However, it is still challenging to control the reactivity of active N-centered radicals to selectively access N-oxidation products. Herein, this study reports the engineering of cytochrome P450BM3 into multifunctional N-oxidizing enzymes with the assistance of dual-functional small molecules (DFSM) to selectively produce N-oxygenation (i.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
November 2024
Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan 430071, China.
P450 peroxidase activities are valued for their ability to catalyze complex chemical transformations using economical HO; however, they have been largely underexplored compared to their monooxygenase and peroxygenase activities. In this study, we identified an unconventional P450 enzyme, PtmB, which catalyzes the dimerization of purine nucleobases and tryptophan-containing diketopiperazines (TDKPs), yielding C3-nucleobase pyrroloindolines and nucleobase-TDKP dimers. Unlike typical TDKP P450 enzymes reliant on NAD(P)H cofactors and electron transfer systems, PtmB, and its analogs exhibit remarkable peroxidase activity in synthesizing adenine and other modified 6-aminopurine nucleobase-TDKP dimers.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
October 2024
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095.
It is broadly recognized that intramolecular electric fields, produced by the protein scaffold and acting on the active site, facilitate enzymatic catalysis. This field effect can be described by several theoretical models, each of which is intuitive to varying degrees. In this contribution, we show that a fundamental effect of electric fields is to generate electrostatic potentials that facilitate the energetic alignment of reactant frontier orbitals.
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