6P2I
Acyclic imino acid reductase (Bsp5) in complex with NADPH and D-Arg
Summary for 6P2I
| Entry DOI | 10.2210/pdb6p2i/pdb |
| Descriptor | Glycerate dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, D-ARGININE, ... (5 entities in total) |
| Functional Keywords | enzyme, complex, imine reductase, acyclic imine, biosynthetic protein, oxidoreductase |
| Biological source | Bacillus sp. 5mfcol3.1 |
| Total number of polymer chains | 2 |
| Total formula weight | 74048.06 |
| Authors | Guo, J.,Higgins, M.A.,Daniel-Ivad, P.,Ryan, K.S. (deposition date: 2019-05-21, release date: 2019-07-24, Last modification date: 2023-10-11) |
| Primary citation | 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 Cited by 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: 31298853DOI: 10.1021/jacs.9b03307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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