Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2-generating fusion protein systems

Sarah Matthews, Kang Lan Tee, Nicholas Rattray, Kirsty Mclean, David Leys, David Parker, Richard Blankley, Andrew Munro

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    Abstract

    Jeotgalicoccus sp. 8456 OleTJE (CYP152L1) is a fatty acid decarboxylase cytochrome P450 that uses hydrogen peroxide (H2O2 ) to catalyse production of terminal alkenes, which are industrially important chemicals with biofuel applications. We report enzyme fusion systems in which Streptomyces coelicolor alditol oxidase (AldO) is linked to OleTJE . AldO oxidizes polyols (including glycerol), generating H2O2 as a coproduct and facilitating its use for efficient OleTJE -dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H2O2 supply to minimize oxidative inactivation of OleTJE and prolong activity for increased alkene production. We also use these fusion systems to generate novel products from secondary turnover of 2-OH and 3-OH myristic acid primary products, expanding the catalytic repertoire of OleTJE .
    Original languageEnglish
    Pages (from-to)737-750
    Number of pages14
    JournalFEBS Letters
    Volume591
    Issue number5
    Early online date21 Feb 2017
    DOIs
    Publication statusPublished - Mar 2017

    Keywords

    • OleT
    • cytochrome P450
    • alkene production
    • fusion protein
    • alditol oxidase
    • hemoprotein
    • fatty acid hydroxylation
    • fatty acid decarboxylation
    • hydrogen peroxide
    • novel products
    • peroxygnease

    Research Beacons, Institutes and Platforms

    • Biotechnology
    • Manchester Energy

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