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Issue 5, 2018
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Isolation, expression and biochemical characterization of recombinant hyoscyamine-6β-hydroxylase from Brugmansia sanguinea – tuning the scopolamine production

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Abstract

Hyoscyamine-6β-hydroxylase (H6H, EC 1.14.11.11) is a plant enzyme that catalyses the last two steps in the biosynthesis of the anticholinergic drug scopolamine, i.e. the hydroxylation of hyoscyamine to 6β-hydroxyhyoscyamine (anisodamine) and subsequent oxidative ring-closure to the 6,7-β-epoxide. A H6H gene homologue was isolated from the plant Brugmansia sanguinea (BsH6H) and recombinantly cloned into Escherichia coli, expressed and purified using an effective SUMO-fusion procedure. Enzymatic activity is approximately 40-fold higher for the first reaction step and the substrate affinity is comparable to other characterized H6H homologues (Km ∼ 60 μM). Truncation of an H6H enzyme flexible N-terminal region yields an active and stable yet more compact enzyme version.

Graphical abstract: Isolation, expression and biochemical characterization of recombinant hyoscyamine-6β-hydroxylase from Brugmansia sanguinea – tuning the scopolamine production

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Publication details

The article was received on 15 Feb 2018, accepted on 25 Apr 2018 and first published on 02 May 2018


Article type: Research Article
DOI: 10.1039/C8MD00090E
Citation: Med. Chem. Commun., 2018,9, 888-892
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    Isolation, expression and biochemical characterization of recombinant hyoscyamine-6β-hydroxylase from Brugmansia sanguinea – tuning the scopolamine production

    C. Fischer, M. Kwon, D. Ro, M. J. van Belkum and J. C. Vederas, Med. Chem. Commun., 2018, 9, 888
    DOI: 10.1039/C8MD00090E

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