9N43

Crystal structure of none-heme iron enzyme (TqaM) from Trichoderma atroviride bound with iron

9N43 の概要

• エントリーDOI: 10.2210/pdb9n43/pdb
• 分子名称: Class II aldolase/adducin N-terminal domain-containing protein, FE (III) ION (3 entities in total)
• 機能のキーワード: oxidative decarboxylase, metal binding protein
• 由来する生物種: Trichoderma atroviride
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 125018.31

構造登録者

Liu, S.,Zheng, Y.-C.,Chang, W.-C. (登録日: 2025-02-01, 公開日: 2026-01-28, 最終更新日: 2026-02-04)

主引用文献

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

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: 39849356
DOI: 10.1021/jacs.4c16716

実験手法

X-RAY DIFFRACTION (2.6 Å)