9N43
Crystal structure of none-heme iron enzyme (TqaM) from Trichoderma atroviride bound with iron
Summary for 9N43
| Entry DOI | 10.2210/pdb9n43/pdb |
| Descriptor | Class II aldolase/adducin N-terminal domain-containing protein, FE (III) ION (3 entities in total) |
| Functional Keywords | oxidative decarboxylase, metal binding protein |
| Biological source | Trichoderma atroviride |
| Total number of polymer chains | 4 |
| Total formula weight | 125018.31 |
| Authors | Liu, S.,Zheng, Y.-C.,Chang, W.-C. (deposition date: 2025-02-01, release date: 2026-01-28, Last modification date: 2026-02-04) |
| Primary citation | Cheng, L.,Bo, Z.,Krohn-Hansen, B.,Yang, Y. Directed Evolution and Unusual Protonation Mechanism of Pyridoxal Radical C-C Coupling Enzymes for the Enantiodivergent Photobiocatalytic Synthesis of Noncanonical Amino Acids. J.Am.Chem.Soc., 147:4602-4612, 2025 Cited by PubMed Abstract: Visible light-driven pyridoxal radical biocatalysis has emerged as a new strategy for the stereoselective synthesis of valuable noncanonical amino acids in a protecting-group-free fashion. In our previously developed dehydroxylative C-C coupling using engineered PLP-dependent tryptophan synthases, an enzyme-controlled unusual α-stereochemistry reversal and pH-controlled enantiopreference were observed. Herein, through high-throughput photobiocatalysis, we evolved a set of stereochemically complementary PLP radical enzymes, allowing the synthesis of both l- and d-amino acids with enhanced enantiocontrol across a broad pH window. These newly engineered l- and d-amino acid synthases permitted the use of a broad range of organoboron substrates, including boronates, trifluoroborates, and boronic acids, with excellent efficiency. Mechanistic studies unveiled unexpected PLP racemase activity with our earlier PLP enzyme variants. This promiscuous racemase activity was abolished in our evolved amino acid synthases, shedding light on the origin of enhanced enantiocontrol. Further mechanistic investigations suggest a switch of proton donor to account for the stereoinvertive formation of d-amino acids, highlighting an unusual stereoinversion mechanism that is rare in conventional two-electron PLP enzymology. PubMed: 39849356DOI: 10.1021/jacs.4c16716 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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