9E9J
L-allo-threonine aldolase from Thermotoga maritima, N308E-Y87A-R122G-P121D Mutant
Summary for 9E9J
| Entry DOI | 10.2210/pdb9e9j/pdb |
| Related | 9E97 |
| Descriptor | L-allo-threonine aldolase, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | pyridoxal-5-phosphate, plp, enzyme, inhibitor complex, lyase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 4 |
| Total formula weight | 154053.18 |
| Authors | Wang, S.,Jeffrey, P.D.,Sorigue, D.,Hyster, T.K. (deposition date: 2024-11-08, release date: 2025-07-23, Last modification date: 2025-08-06) |
| Primary citation | Ouyang, Y.,Wang, S.,Sorigue, D.,Hyster, T.K. Nucleophilic alpha-Functionalization of Benzyl Amines Using an Engineered Threonine Aldolase. J.Am.Chem.Soc., 147:25184-25190, 2025 Cited by PubMed Abstract: Chiral amines are ubiquitous in pharmaceuticals and agrochemicals, making their efficient and selective synthesis a significant synthetic challenge. Threonine aldolases synthesize chiral amines via stereoselective C-C bond formation; however, they are restricted to small amino acids as pro-nucleophiles, limiting their utility in chemical synthesis. Here, we report an engineered threonine aldolase capable of α-functionalizing benzylamines. The evolved enzyme has excellent catalytic efficiency and accepts a broad range of (heterocyclic)benzyl amines and structurally diverse aldehydes to yield single-enantiomers of 1,2-amino alcohols in high-yield and diastereoselectivity. Mechanistic and crystallographic studies provide a rationale for how these mutations enable this previously unknown function. Moreover, beneficial mutations can be transferred to a related pyridoxal-dependent protein, highlighting the generality of these insights. PubMed: 40631863DOI: 10.1021/jacs.5c04097 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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