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Journal articles on the topic 'Peroxygenase'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Di, Siyu, Shengxian Fan, Fengjie Jiang, and Zhiqi Cong. "A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective." Antioxidants 11, no. 3 (2022): 529. http://dx.doi.org/10.3390/antiox11030529.

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Cytochrome P450 monooxygenases (P450s) are promising versatile oxidative biocatalysts. However, the practical use of P450s in vitro is limited by their dependence on the co-enzyme NAD(P)H and the complex electron transport system. Using H2O2 simplifies the catalytic cycle of P450s; however, most P450s are inactive in the presence of H2O2. By mimicking the molecular structure and catalytic mechanism of natural peroxygenases and peroxidases, an artificial P450 peroxygenase system has been designed with the assistance of a dual-functional small molecule (DFSM). DFSMs, such as N-(ω-imidazolyl fatt

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2

Zámocký, Marcel, and Jana Harichová. "Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches." Antioxidants 11, no. 5 (2022): 1011. http://dx.doi.org/10.3390/antiox11051011.

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We reconstructed the molecular phylogeny of heme containing peroxygenases that are known as very versatile biocatalysts. These oxidoreductases capable of mainly oxyfunctionalizations constitute the peroxidase–peroxygenase superfamily. Our representative reconstruction revealed a high diversity but also well conserved sequence motifs within rather short protein molecules. Corresponding genes coding for heme thiolate peroxidases with peroxygenase activity were detected only among various lower eukaryotes. Most of them originate in the kingdom of fungi. However, it seems to be obvious that these

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3

Willot, Tieves, Girhard, Urlacher, Hollmann, and de Gonzalo. "P450BM3-Catalyzed Oxidations Employing Dual Functional Small Molecules." Catalysts 9, no. 7 (2019): 567. http://dx.doi.org/10.3390/catal9070567.

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A set of dual functional small molecules (DFSMs) containing different amino acids has been synthesized and employed together with three different variants of the cytochrome P450 monooxygenase P450BM3 from Bacillus megaterium in H2O2-dependent oxidation reactions. These DFSMs enhance P450BM3 activity with hydrogen peroxide as an oxidant, converting these enzymes into formal peroxygenases. This system has been employed for the catalytic epoxidation of styrene and in the sulfoxidation of thioanisole. Various P450BM3 variants have been evaluated in terms of activity and selectivity of the peroxyge

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4

Munro, Andrew W., Kirsty J. McLean, Job L. Grant, and Thomas M. Makris. "Structure and function of the cytochrome P450 peroxygenase enzymes." Biochemical Society Transactions 46, no. 1 (2018): 183–96. http://dx.doi.org/10.1042/bst20170218.

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The cytochromes P450 (P450s or CYPs) constitute a large heme enzyme superfamily, members of which catalyze the oxidative transformation of a wide range of organic substrates, and whose functions are crucial to xenobiotic metabolism and steroid transformation in humans and other organisms. The P450 peroxygenases are a subgroup of the P450s that have evolved in microbes to catalyze the oxidative metabolism of fatty acids, using hydrogen peroxide as an oxidant rather than NAD(P)H-driven redox partner systems typical of the vast majority of other characterized P450 enzymes. Early members of the pe

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5

Blée, Elizabeth. "Effect of the Safener Dichlormid on Maize Peroxygenase and Lipoxygenase." Zeitschrift für Naturforschung C 46, no. 9-10 (1991): 920–25. http://dx.doi.org/10.1515/znc-1991-9-1033.

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Abstract S-Ethyl-N,N-dipropylthiocarbamate (EPTC) was oxidized into its corresponding sulfoxide by microsomal fractions from etiolated maize seedlings. This reaction is catalyzed by a hydroperoxide-dependent enzyme, identified as a peroxygenase. The hydroperoxides formed from fatty acids by a lipoxygenase are efficient co-substrates of the EPTC sulfoxidation. The effects of the safener dichlormid on the peroxygenase and lipoxygenase activities were studied in vitro and in vivo. In vitro, the safener is not an inhibitor of these enzymes. Dichlormid seems to act, in vivo, by modulating the amoun

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6

Hofrichter, Martin, Harald Kellner, Robert Herzog, et al. "Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases." Antioxidants 11, no. 1 (2022): 163. http://dx.doi.org/10.3390/antiox11010163.

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Unspecific peroxygenases (UPOs), whose sequences can be found in the genomes of thousands of filamentous fungi, many yeasts and certain fungus-like protists, are fascinating biocatalysts that transfer peroxide-borne oxygen (from H2O2 or R-OOH) with high efficiency to a wide range of organic substrates, including less or unactivated carbons and heteroatoms. A twice-proline-flanked cysteine (PCP motif) typically ligates the heme that forms the heart of the active site of UPOs and enables various types of relevant oxygenation reactions (hydroxylation, epoxidation, subsequent dealkylations, deacyl

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7

BLEE, ELIZABETH, and FRANCIS SCHUBER. "Properties of plant peroxygenase." Biochemical Society Transactions 20, no. 2 (1992): 223S. http://dx.doi.org/10.1042/bst020223s.

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8

Bassanini, Ivan, Erica Elisa Ferrandi, Marta Vanoni, et al. "Peroxygenase-Catalyzed Enantioselective Sulfoxidations." European Journal of Organic Chemistry 2017, no. 47 (2017): 7186–89. http://dx.doi.org/10.1002/ejoc.201701390.

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9

Carro, Juan, Elena Fernández-Fueyo, Carmen Fernández-Alonso, et al. "Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural." Biotechnology for Biofuels 11, no. 1 (2018): 86. https://doi.org/10.1186/s13068-018-1091-2.

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<strong>Background: </strong>2,5-Furandicarboxylic acid is a renewable building block for the production of polyfurandicarboxylates, which are biodegradable polyesters expected to substitute their classical counterparts derived from fossil resources. It may be produced from bio-based 5-hydroxymethylfurfural or 5-methoxymethylfurfural, both obtained by the acidic dehydration of biomass-derived fructose. 5-Methoxymethylfurfural, which is produced in the presence of methanol, generates less by-products and exhibits better storage stability than 5-hydroxymethylfurfural being, therefore, the indust

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10

Pesic, Milja, Sébastien Jean-Paul Willot, Elena Fernández-Fueyo, Florian Tieves, Miguel Alcalde, and Frank Hollmann. "Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions." Zeitschrift für Naturforschung C 74, no. 3-4 (2019): 101–4. http://dx.doi.org/10.1515/znc-2018-0137.

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Abstract There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we

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11

Hanano, Abdulsamie, Ibrahem Almousally, Mouhnad Shaban, and Elizabeth Blee. "A Caleosin-Like Protein with Peroxygenase Activity Mediates Aspergillus flavus Development, Aflatoxin Accumulation, and Seed Infection." Applied and Environmental Microbiology 81, no. 18 (2015): 6129–44. http://dx.doi.org/10.1128/aem.00867-15.

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ABSTRACTCaleosins are a small family of calcium-binding proteins endowed with peroxygenase activity in plants. Caleosin-like genes are present in fungi; however, their functions have not been reported yet. In this work, we identify a plant caleosin-like protein inAspergillus flavusthat is highly expressed during the early stages of spore germination. A recombinant purified 32-kDa caleosin-like protein supported peroxygenase activities, including co-oxidation reactions and reduction of polyunsaturated fatty acid hydroperoxides. Deletion of the caleosin gene prevented fungal development. Alterna

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12

González-Benjumea, Alejandro, Juan Carro, Chantal Renau-Mínguez, et al. "Correction: Fatty acid epoxidation by Collariella virescens peroxygenase and heme-channel variants." Catalysis Science & Technology 10, no. 6 (2020): 1952. http://dx.doi.org/10.1039/d0cy90018d.

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13

González-Benjumea, Alejandro, Juan Carro, Chantal Renau-Mínguez, et al. "Fatty acid epoxidation by Collariella virescens peroxygenase and heme-channel variants." Catalysis Science & Technology 10, no. 3 (2020): 717–25. http://dx.doi.org/10.1039/c9cy02332a.

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14

Peng, Lei, Ulla Wollenberger, Matthias Kinne, et al. "Peroxygenase based sensor for aromatic compounds." Biosensors and Bioelectronics 26, no. 4 (2010): 1432–36. http://dx.doi.org/10.1016/j.bios.2010.07.075.

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15

Shoji, Osami, and Yoshihito Watanabe. "Peroxygenase reactions catalyzed by cytochromes P450." JBIC Journal of Biological Inorganic Chemistry 19, no. 4-5 (2014): 529–39. http://dx.doi.org/10.1007/s00775-014-1106-9.

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16

Peng, Lei, Ulla Wollenberger, Martin Hofrichter, René Ullrich, Katrin Scheibner, and Frieder W. Scheller. "Bioelectrocatalytic properties of Agrocybe aegerita peroxygenase." Electrochimica Acta 55, no. 27 (2010): 7809–13. http://dx.doi.org/10.1016/j.electacta.2009.12.065.

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17

Blée, Elizabeth. "Biosynthesis of phytooxylipins: the Peroxygenase pathway." Lipid - Fett 100, no. 4-5 (1998): 121–27. http://dx.doi.org/10.1002/(sici)1521-4133(19985)100:4/5<121::aid-lipi121>3.0.co;2-4.

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18

Ni, Yan, Elena Fernández-Fueyo, Alvaro Gomez Baraibar, et al. "Peroxygenase-katalysierte Oxyfunktionalisierung angetrieben durch Methanoloxidation." Angewandte Chemie 128, no. 2 (2015): 809–12. http://dx.doi.org/10.1002/ange.201507881.

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19

Salazar, Oriana, Patrick C. Cirino, and Frances H. Arnold. "Thermostabilization of a Cytochrome P450 Peroxygenase." ChemBioChem 4, no. 9 (2003): 891–93. http://dx.doi.org/10.1002/cbic.200300660.

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20

König, Rosalie, Jan Kiebist, Johannes Kalmbach, et al. "Novel Unspecific Peroxygenase from Truncatella angustata Catalyzes the Synthesis of Bioactive Lipid Mediators." Microorganisms 10, no. 7 (2022): 1267. http://dx.doi.org/10.3390/microorganisms10071267.

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Lipid mediators, such as epoxidized or hydroxylated eicosanoids (EETs, HETEs) of arachidonic acid (AA), are important signaling molecules and play diverse roles at different physiological and pathophysiological levels. The EETs and HETEs formed by the cytochrome P450 enzymes are still not fully explored, but show interesting anti-inflammatory properties, which make them attractive as potential therapeutic target or even as therapeutic agents. Conventional methods of chemical synthesis require several steps and complex separation techniques and lead only to low yields. Using the newly discovere

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21

Karich, Alexander, Fabian Salzsieder, Martin Kluge, Miguel Alcalde, René Ullrich, and Martin Hofrichter. "Conversion of Unsaturated Short- to Medium-Chain Fatty Acids by Unspecific Peroxygenases (UPOs)." Applied Microbiology 3, no. 3 (2023): 826–40. http://dx.doi.org/10.3390/applmicrobiol3030057.

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Eighteen short- to medium-chain monounsaturated fatty acids were screened for hydroxylation and epoxidation using eleven different peroxygenase preparations. Most of these unspecific peroxygenases (UPOs) are secreted by fungal species of the dark-spored basidiomycetous families Psathyrellaceae and Strophariaceae, two belonged to the white-spored genus Marasmius (Marasmiaceae), and one belonged to the ascomycetous family Chaetomiaceae. The fatty acids (FAs) studied were categorized into three groups based on the position of the double bond: (i) terminal unsaturated FAs (between ω and ω-1), (ii)

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22

Lin, Yen-Ting, and Sam P. de Visser. "Product Distributions of Cytochrome P450 OleTJE with Phenyl-Substituted Fatty Acids: A Computational Study." International Journal of Molecular Sciences 22, no. 13 (2021): 7172. http://dx.doi.org/10.3390/ijms22137172.

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There are two types of cytochrome P450 enzymes in nature, namely, the monooxygenases and the peroxygenases. Both enzyme classes participate in substrate biodegradation or biosynthesis reactions in nature, but the P450 monooxygenases use dioxygen, while the peroxygenases take H2O2 in their catalytic cycle instead. By contrast to the P450 monooxygenases, the P450 peroxygenases do not require an external redox partner to deliver electrons during the catalytic cycle, and also no external proton source is needed. Therefore, they are fully self-sufficient, which affords them opportunities in biotech

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23

Matsunaga, Isamu, Tatsuo Sumimoto, Minoru Ayata, and Hisashi Ogura. "Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes." FEBS Letters 528, no. 1-3 (2002): 90–94. http://dx.doi.org/10.1016/s0014-5793(02)03261-1.

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24

Bissaro, Bastien, Bennett Streit, Ingvild Isaksen, et al. "Molecular mechanism of the chitinolytic peroxygenase reaction." Proceedings of the National Academy of Sciences 117, no. 3 (2020): 1504–13. http://dx.doi.org/10.1073/pnas.1904889117.

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Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of monocopper enzymes broadly distributed across the tree of life. Recent reports indicate that LPMOs can use H2O2 as an oxidant and thus carry out a novel type of peroxygenase reaction involving unprecedented copper chemistry. Here, we present a combined computational and experimental analysis of the H2O2-mediated reaction mechanism. In silico studies, based on a model of the enzyme in complex with a crystalline substrate, suggest that a network of hydrogen bonds, involving both the enzyme and the substrate, brings H2

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25

Nguyen, Thi, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (2021): 603. http://dx.doi.org/10.3390/app11020603.

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Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by biocatalysts using enzymes and whole-cell biotransformation is more desirable than chemical synthesis. It is more eco-friendly and can increase the yield of desired products. In this study, we have found an enzymatic strategy of P450 enzymes for highly efficient sy

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26

Nguyen, Thi Huong Ha, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (2021): 603. http://dx.doi.org/10.3390/app11020603.

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Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by biocatalysts using enzymes and whole-cell biotransformation is more desirable than chemical synthesis. It is more eco-friendly and can increase the yield of desired products. In this study, we have found an enzymatic strategy of P450 enzymes for highly efficient sy

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27

Nintzel, Friederike E. H., Yinqi Wu, Matteo Planchestainer, Martin Held, Miguel Alcalde, and Frank Hollmann. "An alginate-confined peroxygenase-CLEA for styrene epoxidation." Chemical Communications 57, no. 47 (2021): 5766–69. http://dx.doi.org/10.1039/d1cc01868j.

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An alginate-confined peroxygenase-CLEA has been prepared for the stereoselective epoxidation of cis-β-methylstyrene under non-aqueous reaction conditions. Product titres of up to 48 mM and excellent enzyme turnovers of 96 000 have been achieved.

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28

Wang, Jian-bo, Richard Lonsdale, and Manfred T. Reetz. "Exploring substrate scope and stereoselectivity of P450 peroxygenase OleTJEin olefin-forming oxidative decarboxylation." Chemical Communications 52, no. 52 (2016): 8131–33. http://dx.doi.org/10.1039/c6cc04345c.

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The substrate scope of the mild olefin-forming oxidative decarboxylation of straight-chain C<sub>4</sub>–C<sub>22</sub>carboxylic acids catalyzed by P450 peroxygenase OleT<sub>JE</sub>has been extended to include structurally diverse carboxylic acids.

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29

Kuo, H. H., and A. G. Mauk. "Indole peroxygenase activity of indoleamine 2,3-dioxygenase." Proceedings of the National Academy of Sciences 109, no. 35 (2012): 13966–71. http://dx.doi.org/10.1073/pnas.1207191109.

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30

Ullrich, RenÃ©, Christiane Liers, Sylvia Schimpke, and Martin Hofrichter. "Purification of homogeneous forms of fungal peroxygenase." Biotechnology Journal 4, no. 11 (2009): 1619–26. http://dx.doi.org/10.1002/biot.200900076.

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31

Horst, A., S. Bormann, J. Schrader, and D. Holtmann. "Oxyfunktionalisierungen mit der unspezifischen Peroxygenase ausAgrocybe aegerita." Chemie Ingenieur Technik 88, no. 9 (2016): 1254. http://dx.doi.org/10.1002/cite.201650327.

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32

Ramirez-Ramirez, Joaquin, Javier Martin-Diaz, Nina Pastor, Miguel Alcalde, and Marcela Ayala. "Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I." International Journal of Molecular Sciences 21, no. 16 (2020): 5734. http://dx.doi.org/10.3390/ijms21165734.

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Unspecific peroxygenases (UPOs) are fungal heme-thiolate enzymes able to catalyze a wide range of oxidation reactions, such as peroxidase-like, catalase-like, haloperoxidase-like, and, most interestingly, cytochrome P450-like. One of the most outstanding properties of these enzymes is the ability to catalyze the oxidation a wide range of organic substrates (both aromatic and aliphatic) through cytochrome P450-like reactions (the so-called peroxygenase activity), which involves the insertion of an oxygen atom from hydrogen peroxide. To catalyze this reaction, the substrate must access a channel

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33

Schramm, Marina, Stephanie Friedrich, Kai-Uwe Schmidtke, et al. "Cell-Free Protein Synthesis with Fungal Lysates for the Rapid Production of Unspecific Peroxygenases." Antioxidants 11, no. 2 (2022): 284. http://dx.doi.org/10.3390/antiox11020284.

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Unspecific peroxygenases (UPOs, EC 1.11.2.1) are fungal biocatalysts that have attracted considerable interest for application in chemical syntheses due to their ability to selectively incorporate peroxide-oxygen into non-activated hydrocarbons. However, the number of available and characterized UPOs is limited, as it is difficult to produce these enzymes in homologous or hetero-logous expression systems. In the present study, we introduce a third approach for the expression of UPOs: cell-free protein synthesis using lysates from filamentous fungi. Biomass of Neurospora crassa and Aspergillus

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34

Qin, Xiangquan, Yiping Jiang, Jie Chen, et al. "Co-Crystal Structure-Guided Optimization of Dual-Functional Small Molecules for Improving the Peroxygenase Activity of Cytochrome P450BM3." International Journal of Molecular Sciences 23, no. 14 (2022): 7901. http://dx.doi.org/10.3390/ijms23147901.

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We recently developed an artificial P450–H2O2 system assisted by dual-functional small molecules (DFSMs) to modify the P450BM3 monooxygenase into its peroxygenase mode, which could be widely used for the oxidation of non-native substrates. Aiming to further improve the DFSM-facilitated P450–H2O2 system, a series of novel DFSMs having various unnatural amino acid groups was designed and synthesized, based on the co-crystal structure of P450BM3 and a typical DFSM, N-(ω-imidazolyl)-hexanoyl-L-phenylalanine, in this study. The size and hydrophobicity of the amino acid residue in the DFSM drastical

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35

Martin‐Diaz, Javier, Patricia Molina‐Espeja, Martin Hofrichter, Frank Hollmann, and Miguel Alcalde. "Directed evolution of unspecific peroxygenase in organic solvents." Biotechnology and Bioengineering 118, no. 8 (2021): 3002–14. http://dx.doi.org/10.1002/bit.27810.

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36

Tonin, Fabio, Florian Tieves, Sébastien Willot, et al. "Pilot-Scale Production of Peroxygenase from Agrocybe aegerita." Organic Process Research & Development 25, no. 6 (2021): 1414–18. http://dx.doi.org/10.1021/acs.oprd.1c00116.

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37

Molina-Espeja, Patricia, Paloma Santos-Moriano, Eva García-Ruiz, Antonio Ballesteros, Francisco Plou, and Miguel Alcalde. "Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase." International Journal of Molecular Sciences 20, no. 7 (2019): 1627. http://dx.doi.org/10.3390/ijms20071627.

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Unspecific peroxygenases (UPOs) are highly promiscuous biocatalyst with self-sufficient mono(per)oxygenase activity. A laboratory-evolved UPO secreted by yeast was covalently immobilized in activated carriers through one-point attachment. In order to maintain the desired orientation without compromising the enzyme’s activity, the S221C mutation was introduced at the surface of the enzyme, enabling a single disulfide bridge to be established between the support and the protein. Fluorescence confocal microscopy demonstrated the homogeneous distribution of the enzyme, regardless of the chemical n

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38

Zenser, Terry V., Vijaya M. Lakshmi, Fong Fu Hsu, and Bernard B. Davis. "Peroxygenase Metabolism ofN-Acetylbenzidine by Prostaglandin H Synthase." Journal of Biological Chemistry 274, no. 21 (1999): 14850–56. http://dx.doi.org/10.1074/jbc.274.21.14850.

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Molina-Espeja, Patricia, Eva Garcia-Ruiz, David Gonzalez-Perez, René Ullrich, Martin Hofrichter, and Miguel Alcalde. "Directed Evolution of Unspecific Peroxygenase from Agrocybe aegerita." Applied and Environmental Microbiology 80, no. 11 (2014): 3496–507. http://dx.doi.org/10.1128/aem.00490-14.

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ABSTRACTUnspecific peroxygenase (UPO) represents a new type of heme-thiolate enzyme with self-sufficient mono(per)oxygenase activity and many potential applications in organic synthesis. With a view to taking advantage of these properties, we subjected theAgrocybe aegeritaUPO1-encoding gene to directed evolution inSaccharomyces cerevisiae. To promote functional expression, several different signal peptides were fused to the mature protein, and the resulting products were tested. Over 9,000 clones were screened using anad hocdual-colorimetric assay that assessed both peroxidative and oxygen tra

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40

Ullrich, René, Marzena Poraj-Kobielska, Steffi Scholze, et al. "Side chain removal from corticosteroids by unspecific peroxygenase." Journal of Inorganic Biochemistry 183 (June 2018): 84–93. http://dx.doi.org/10.1016/j.jinorgbio.2018.03.011.

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41

Willot, Sébastien J. P., Elena Fernández-Fueyo, Florian Tieves, et al. "Expanding the Spectrum of Light-Driven Peroxygenase Reactions." ACS Catalysis 9, no. 2 (2018): 890–94. http://dx.doi.org/10.1021/acscatal.8b03752.

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42

Pecyna, Marek J., René Ullrich, Britta Bittner, et al. "Molecular characterization of aromatic peroxygenase from Agrocybe aegerita." Applied Microbiology and Biotechnology 84, no. 5 (2009): 885–97. http://dx.doi.org/10.1007/s00253-009-2000-1.

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43

Olmedo, Andrés, José C. del Río, Jan Kiebist, et al. "Fatty Acid Chain Shortening by a Fungal Peroxygenase." Chemistry - A European Journal 23, no. 67 (2017): 16985–89. http://dx.doi.org/10.1002/chem.201704773.

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44

Li, Yuanying, Pengpeng Zhang, Zhoutong Sun, et al. "Peroxygenase-Catalyzed Selective Synthesis of Calcitriol Starting from Alfacalcidol." Antioxidants 11, no. 6 (2022): 1044. http://dx.doi.org/10.3390/antiox11061044.

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Calcitriol is an active analog of vitamin D3 and has excellent physiological activities in regulating healthy immune function. To synthesize the calcitriol compound, the concept of total synthesis is often adopted, which typically involves multiple steps and results in an overall low yield. Herein, we envisioned an enzymatic approach for the synthesis of calcitriol. Peroxygenase from Agrocybe aegerita (AaeUPO) was used as a catalyst to hydroxylate the C-H bond at the C-25 position of alfacalcidol and yielded the calcitriol in a single step. The enzymatic reaction yielded 80.3% product formatio

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45

Peter, Sebastian, Matthias Kinne, Xiaoshi Wang, et al. "Selective hydroxylation of alkanes by an extracellular fungal peroxygenase." FEBS Journal 278, no. 19 (2011): 3667–75. http://dx.doi.org/10.1111/j.1742-4658.2011.08285.x.

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46

Barková, Kateřina, Matthias Kinne, René Ullrich, Lothar Hennig, Annett Fuchs, and Martin Hofrichter. "Regioselective hydroxylation of diverse flavonoids by an aromatic peroxygenase." Tetrahedron 67, no. 26 (2011): 4874–78. http://dx.doi.org/10.1016/j.tet.2011.05.008.

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Yamazaki, Shin-ichi, Chiyuki Morioka, and Shinobu Itoh. "Kinetic Evaluation of Catalase and Peroxygenase Activities of Tyrosinase†." Biochemistry 43, no. 36 (2004): 11546–53. http://dx.doi.org/10.1021/bi048908f.

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Fernández-Fueyo, Elena, Yan Ni, Alvaro Gomez Baraibar, Miguel Alcalde, Lukas M. van Langen, and Frank Hollmann. "Towards preparative peroxygenase-catalyzed oxyfunctionalization reactions in organic media." Journal of Molecular Catalysis B: Enzymatic 134 (December 2016): 347–52. http://dx.doi.org/10.1016/j.molcatb.2016.09.013.

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Yarman, Aysu, Lei Peng, Yunhua Wu, et al. "Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors." Bioanalytical Reviews 3, no. 2-4 (2011): 67–94. http://dx.doi.org/10.1007/s12566-011-0023-4.

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Hrycay, Eugene G., and Stelvio M. Bandiera. "The monooxygenase, peroxidase, and peroxygenase properties of cytochrome P450." Archives of Biochemistry and Biophysics 522, no. 2 (2012): 71–89. http://dx.doi.org/10.1016/j.abb.2012.01.003.

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