6P2I

Acyclic imino acid reductase (Bsp5) in complex with NADPH and D-Arg

6P2I の概要

• エントリーDOI: 10.2210/pdb6p2i/pdb
• 分子名称: Glycerate dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, D-ARGININE, ... (5 entities in total)
• 機能のキーワード: enzyme, complex, imine reductase, acyclic imine, biosynthetic protein, oxidoreductase
• 由来する生物種: Bacillus sp. 5mfcol3.1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74048.06

構造登録者

Guo, J.,Higgins, M.A.,Daniel-Ivad, P.,Ryan, K.S. (登録日: 2019-05-21, 公開日: 2019-07-24, 最終更新日: 2023-10-11)

主引用文献

Guo, J.,Higgins, M.A.,Daniel-Ivad, P.,Ryan, K.S.
An Asymmetric Reductase That Intercepts Acyclic Imino Acids Producedin Situby a Partner Oxidase.
J.Am.Chem.Soc., 141:12258-12267, 2019

PubMed Abstract: Acyclic imines are unstable in aqueous conditions. For this reason, known imine reductases, which enable the synthesis of chiral amines, mainly intercept stable cyclic imines. Here we report the detailed biochemical and structural characterization of Bsp5, an imino acid reductase from the d-2-hydroxyacid dehydrogenase family that reduces acyclic imino acids produced by a partner oxidase. We determine a 1.6 Å resolution structure of Bsp5 in complex with d-arginine and coenzyme NADPH. Combined with mutagenesis work, our study reveals the minimal structural constraints for its biosynthetic activity. Furthermore, we demonstrate that Bsp5 can intercept more complex products from an alternate oxidase partner, suggesting that this oxidase-imino acid reductase pair could be evolved for biocatalytic conversion of l-amino acids to d-amino acids.

PubMed: 31298853
DOI: 10.1021/jacs.9b03307

実験手法

X-RAY DIFFRACTION (1.63 Å)