Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.

Autor: Langley C; Department of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany., Tatsis E; Chinese Academy of Sciences Centre for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, 300 Feng Lin Road, Shanghai, 200032, China., Hong B; Department of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany., Nakamura Y; Department of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany.; Research Group Biosynthesis and NMR, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany., Paetz C; Research Group Biosynthesis and NMR, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany., Stevenson CEM; Department of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK., Basquin J; Department of Structural Cell Biology, Max-Planck Institute for Biochemistry, Am Klopferspitz 18, Martinsried, 82152, Planegg, Germany., Lawson DM; Department of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK., Caputi L; Department of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany., O'Connor SE; Department of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Hans-Knöll Straße 8, Jena, 07745, Germany.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2022 Nov 25; Vol. 61 (48), pp. e202210934. Date of Electronic Publication: 2022 Oct 26.
DOI: 10.1002/anie.202210934
Abstrakt: Medium-chain alcohol dehydrogenases (ADHs) comprise a highly conserved enzyme family that catalyse the reversible reduction of aldehydes. However, recent discoveries in plant natural product biosynthesis suggest that the catalytic repertoire of ADHs has been expanded. Here we report the crystal structure of dihydroprecondylocarpine acetate synthase (DPAS), an ADH that catalyses the non-canonical 1,4-reduction of an α,β-unsaturated iminium moiety. Comparison with structures of plant-derived ADHs suggest the 1,4-iminium reduction does not require a proton relay or the presence of a catalytic zinc ion in contrast to canonical 1,2-aldehyde reducing ADHs that require the catalytic zinc and a proton relay. Furthermore, ADHs that catalysed 1,2-iminium reduction required the presence of the catalytic zinc and the loss of the proton relay. This suggests how the ADH active site can be modified to perform atypical carbonyl reductions, providing insight into how chemical reactions are diversified in plant metabolism.
(© 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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