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Oxygenation of Monoenoic Fatty Acids by CYP175A1, an Orphan Cytochrome P450 from Thermus thermophilus HB27

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 2012, 51, 40, 7880-7890
    Article

    Oxygenation of Monoenoic Fatty Acids by CYP175A1, an Orphan Cytochrome P450 from Thermus thermophilus HB27
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    Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India
    *Phone: +91 22 2278 2363, fax: +91 22 2280 4610, e-mail: [email protected], Web: http://www.tifr.res.in/∼shyamal/.
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    Biochemistry

    Cite this: Biochemistry 2012, 51, 40, 7880–7890
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    https://doi.org/10.1021/bi300514j
    Published August 31, 2012
    Copyright © 2012 American Chemical Society
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    Abstract

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    The catalytic activity of CYP175A1 toward monooxygenation of saturated and monounsaturated fatty acids of various chain lengths (C16–C24) has been investigated to assess the enzymatic properties of this orphan thermostable cytochrome P450 enzyme. The results showed that the enzyme could catalyze the reaction of monounsaturated fatty acids but not of saturated fatty acids. The product analyses using ESI-MS and GC-MS revealed an important regioselectivity in the CYP175A1 catalyzed monooxygenation of the monoenoic fatty acids depending on the ethylenic double bond (C═C) configuration. When the double bond was in cis-configuration, an epoxy fatty acid was found to be the major product and two allyl-hydroxy fatty acids were found to be the minor products. But when the double bond was in trans-configuration the product distribution was reversed. The oxygenation efficiency was found to be the highest for palmitoleic acid (chain length C16), but there was no direct correlation of the activity with the chain length or the position of unsaturation of the fatty acid. Molecular docking calculations showed that the “U”-type conformations of the monoenoic fatty acids are particularly responsible for their binding in the enzyme pocket, and that is also consistent with the observed regioselectivity in the oxygenation reaction. The present results provide evidence that CYP175A1 can catalyze the regioselective oxygenation reaction of several monoenoic fatty acids though it cannot catalyze the oxygenation of the corresponding saturated analogues. These studies may provide critical information on the nature of the enzyme pocket and of the possible natural substrate of this orphan enzyme.

    Copyright © 2012 American Chemical Society

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    Supporting Information

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    ESI-MS of CYP175A1, binding titration of various fatty acids with CYP175A1, ESI-mass spectra of the control reactions of 16C9, enzymatic reaction of 16C9 with CYP175A1 using reductive pathway, H2O2 dependent heme degradation, CID-MS/MS of enzymatic and standard products of 16C9, 18C6 and 18C11, TIC gas chromatogram of enzymatic and standard products of 16C9, GC-MS of enzymatic and standard products of 16C9, docking result of palmitoleic acid (16C9), Lineweaver–Burk plot for various fatty acid kinetics, and possible mechanism of fragmentation of epoxy- and different allyl-hydroxy fatty acids during CID/MS/MS study. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 14 publications.

    1. Mohd Taher, Kshatresh Dutta Dubey, Shyamalava Mazumdar. Computationally guided bioengineering of the active site, substrate access pathway, and water channels of thermostable cytochrome P450, CYP175A1, for catalyzing the alkane hydroxylation reaction. Chemical Science 2023, 33 https://doi.org/10.1039/D3SC02857G
    2. Srabani Karmakar, Sudip Kumar Nag, Mohd Taher, Bharat T. Kansara, Shyamalava Mazumdar. Enhanced Substrate Specificity of Thermostable Cytochrome P450 CYP175A1 by Site Saturation Mutation on Tyrosine 68. The Protein Journal 2022, 41 (6) , 659-670. https://doi.org/10.1007/s10930-022-10084-3
    3. Siyu Di, Shengxian Fan, Fengjie Jiang, Zhiqi Cong. A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective. Antioxidants 2022, 11 (3) , 529. https://doi.org/10.3390/antiox11030529
    4. Kim-Thoa Nguyen, Ngọc-Lan Nguyen, Nguyen Van Tung, Huy Hoang Nguyen, Mohammed Milhim, Thi-Thanh-Xuan Le, Thi-Hong-Nhung Lai, Thi-Tuyet-Minh Phan, Rita Bernhardt. A Novel Thermostable Cytochrome P450 from Sequence-Based Metagenomics of Binh Chau Hot Spring as a Promising Catalyst for Testosterone Conversion. Catalysts 2020, 10 (9) , 1083. https://doi.org/10.3390/catal10091083
    5. Rebecca N. Re, Johanna C. Proessdorf, James J. La Clair, Maeva Subileau, Michael D. Burkart. Tailoring chemoenzymatic oxidation via in situ peracids. Organic & Biomolecular Chemistry 2019, 17 (43) , 9418-9424. https://doi.org/10.1039/C9OB01814J
    6. Kurt L. Harris, Raine E.S. Thomson, Silja J. Strohmaier, Yosephine Gumulya, Elizabeth M.J. Gillam. Determinants of thermostability in the cytochrome P450 fold. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2018, 1866 (1) , 97-115. https://doi.org/10.1016/j.bbapap.2017.08.003
    7. J. K. Prasain, L. S. Wilson, A. Arabshahi, C. Grubbs, S. Barnes. Mass spectrometric evidence for the modification of small molecules in a cobalt‐60‐irradiated rodent diet. Journal of Mass Spectrometry 2017, 52 (8) , 507-516. https://doi.org/10.1002/jms.3950
    8. Maria Oszajca, Małgorzata Brindell, Łukasz Orzeł, Janusz M. Dąbrowski, Klaudyna Śpiewak, Przemysław Łabuz, Michał Pacia, Anna Stochel-Gaudyn, Wojciech Macyk, Rudi van Eldik, Grażyna Stochel. Mechanistic studies on versatile metal-assisted hydrogen peroxide activation processes for biomedical and environmental incentives. Coordination Chemistry Reviews 2016, 327-328 , 143-165. https://doi.org/10.1016/j.ccr.2016.05.013
    9. Shibdas Banerjee, Sandeep Goyal, Shyamalava Mazumdar. Role of substituents on the reactivity and product selectivity in reactions of naphthalene derivatives catalyzed by the orphan thermostable cytochrome P450, CYP175A1. Bioorganic Chemistry 2015, 62 , 94-105. https://doi.org/10.1016/j.bioorg.2015.08.003
    10. Kirsty J. McLean, David Leys, Andrew W. Munro. Microbial Cytochromes P450. 2015, 261-407. https://doi.org/10.1007/978-3-319-12108-6_6
    11. Osami Shoji, Yoshihito Watanabe. Monooxygenation of Small Hydrocarbons Catalyzed by Bacterial Cytochrome P450s. 2015, 189-208. https://doi.org/10.1007/978-3-319-16009-2_7
    12. Eugene G. Hrycay, Stelvio M. Bandiera. Monooxygenase, Peroxidase and Peroxygenase Properties and Reaction Mechanisms of Cytochrome P450 Enzymes. 2015, 1-61. https://doi.org/10.1007/978-3-319-16009-2_1
    13. . Fatty Acids. 2014, 1-39. https://doi.org/10.1039/9781782626350-00001
    14. Osami Shoji, Yoshihito Watanabe. Peroxygenase reactions catalyzed by cytochromes P450. JBIC Journal of Biological Inorganic Chemistry 2014, 19 (4-5) , 529-539. https://doi.org/10.1007/s00775-014-1106-9
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    Biochemistry

    Cite this: Biochemistry 2012, 51, 40, 7880–7890
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi300514j
    Published August 31, 2012
    Copyright © 2012 American Chemical Society
    Request reuse permissions

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