7DL1
The mutant E310G/G323S structure of 3,5-DAHDHcca complex with NADPH
Summary for 7DL1
| Entry DOI | 10.2210/pdb7dl1/pdb |
| Descriptor | 3,5-diaminohexanoate dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | dehydrogenase, complex, nadph, oxidoreductase |
| Biological source | Cloacimonas acidaminovorans (strain Evry) |
| Total number of polymer chains | 4 |
| Total formula weight | 157950.72 |
| Authors | Liu, N.,Wu, L.,Zhu, D.M.,Zhou, J.H. (deposition date: 2020-11-25, release date: 2021-09-29, Last modification date: 2024-05-29) |
| Primary citation | Liu, N.,Wu, L.,Feng, J.,Sheng, X.,Li, J.,Chen, X.,Li, J.,Liu, W.,Zhou, J.,Wu, Q.,Zhu, D. Crystal Structures and Catalytic Mechanism of l-erythro-3,5-Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of beta-Amino Acids. Angew.Chem.Int.Ed.Engl., 60:10203-10210, 2021 Cited by PubMed Abstract: Amino acid dehydrogenases (AADHs) have shown considerable potential as biocatalysts in the asymmetric synthesis of chiral amino acids. However, compared to the widely studied α-AADHs, limited knowledge is available about β-AADHs that enable the synthesis of β-amino acids. Herein, we report the crystal structures of a l-erythro-3,5-diaminohexanoate dehydrogenase and its variants, the only known member of β-AADH family. Crystal structure analysis, site-directed mutagenesis studies and quantum chemical calculations revealed the differences in the substrate binding and catalytic mechanism from α-AADHs. A number of rationally engineered variants were then obtained with improved activity (by 110-800 times) toward various aliphatic β-amino acids without an enantioselectivity trade-off. Two β-amino acids were prepared by using the outstanding variants with excellent enantioselectivity (>99 % ee) and high isolated yields (86-87 %). These results provide important insights into the molecular mechanism of 3,5-DAHDH, and establish a solid foundation for further design of β-AADHs for the asymmetric synthesis of β-amino acids. PubMed: 33624917DOI: 10.1002/anie.202017225 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.72 Å) |
Structure validation
Download full validation report
