8B25

Dihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga - stemmadenine acetate bound structure

8B25 の概要

• エントリーDOI: 10.2210/pdb8b25/pdb
• 分子名称: Dihydroprecondylocarpine acetate synthase 2, stemmadenine acetate, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: alcohol dehydrogenase, cytosolic protein
• 由来する生物種: Tabernanthe iboga
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79988.48

構造登録者

Langley, C.,Basquin, J.,Caputi, L.,O'Connor, S.E. (登録日: 2022-09-13, 公開日: 2022-10-19, 最終更新日: 2024-01-31)

主引用文献

Langley, C.,Tatsis, E.,Hong, B.,Nakamura, Y.,Paetz, C.,Stevenson, C.E.M.,Basquin, J.,Lawson, D.M.,Caputi, L.,O'Connor, S.E.
Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.
Angew.Chem.Int.Ed.Engl., 61:e202210934-e202210934, 2022

PubMed Abstract: 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.

PubMed: 36198083
DOI: 10.1002/anie.202210934

実験手法

X-RAY DIFFRACTION (2.24 Å)