5IXJ

Tryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active site

5IXJ の概要

• エントリーDOI: 10.2210/pdb5ixj/pdb
• 分子名称: Tryptophan synthase beta chain 1, THREONINE, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: substrate analog, lyase, plp, fold-type ii
• 由来する生物種: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 176108.62

構造登録者

Buller, A.R.,Herger, M.,Arnold, F.H. (登録日: 2016-03-23, 公開日: 2016-08-17, 最終更新日: 2023-11-15)

主引用文献

Herger, M.,van Roye, P.,Romney, D.K.,Brinkmann-Chen, S.,Buller, A.R.,Arnold, F.H.
Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.
J.Am.Chem.Soc., 138:8388-8391, 2016

PubMed Abstract: We report that l-threonine may substitute for l-serine in the β-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-β-methyltryptophan (β-MeTrp) in a single step. The trace activity of the wild-type β-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this increase is correlated with stabilization of the electrophilic aminoacrylate intermediate. The engineered biocatalyst also reacts with a variety of indole analogues and thiophenol for diastereoselective C-C, C-N, and C-S bond-forming reactions. This new activity circumvents the 3-enzyme pathway that produces β-MeTrp in nature and offers a simple and expandable route to preparing derivatives of this valuable building block.

PubMed: 27355405
DOI: 10.1021/jacs.6b04836

実験手法

X-RAY DIFFRACTION (1.54 Å)