7XG6
Crystal structure of an (R)-selective omega-transaminase mutant from Aspergillus terreus with covalently bound PLP
Summary for 7XG6
| Entry DOI | 10.2210/pdb7xg6/pdb |
| Descriptor | omega-transaminase (2 entities in total) |
| Functional Keywords | transferase, llp |
| Biological source | Aspergillus terreus (strain NIH 2624 / FGSC A1156) |
| Total number of polymer chains | 2 |
| Total formula weight | 72040.42 |
| Authors | |
| Primary citation | Wu, S.,Xiang, C.,Zhou, Y.,Khan, M.S.H.,Liu, W.,Feiler, C.G.,Wei, R.,Weber, G.,Hohne, M.,Bornscheuer, U.T. A growth selection system for the directed evolution of amine-forming or converting enzymes. Nat Commun, 13:7458-7458, 2022 Cited by PubMed Abstract: Fast screening of enzyme variants is crucial for tailoring biocatalysts for the asymmetric synthesis of non-natural chiral chemicals, such as amines. However, most existing screening methods either are limited by the throughput or require specialized equipment. Herein, we report a simple, high-throughput, low-equipment dependent, and generally applicable growth selection system for engineering amine-forming or converting enzymes and apply it to improve biocatalysts belonging to three different enzyme classes. This results in (i) an amine transaminase variant with 110-fold increased specific activity for the asymmetric synthesis of the chiral amine intermediate of Linagliptin; (ii) a 270-fold improved monoamine oxidase to prepare the chiral amine intermediate of Cinacalcet by deracemization; and (iii) an ammonia lyase variant with a 26-fold increased activity in the asymmetric synthesis of a non-natural amino acid. Our growth selection system is adaptable to different enzyme classes, varying levels of enzyme activities, and thus a flexible tool for various stages of an engineering campaign. PubMed: 36460668DOI: 10.1038/s41467-022-35228-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
Download full validation report
