57793-74-5Relevant academic research and scientific papers
Directed Evolution of a Tryptophan 2,3-Dioxygenase for the Diastereoselective Monooxygenation of Tryptophans
Bai, Wen-Ju,Jiang, Shengsheng,Li, Qiuchun,Lu, Chen,Wang, Xiqing,Wei, Yanxin,Zhang, Yanyan
, p. 3043 - 3047 (2020)
Herein, we report an engineered enzyme that can monooxygenate unprotected tryptophan into the corresponding 3a-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid (HPIC) in a single, scalable step with excellent turnover number and diastereoselectivity. Taking advantage of directed evolution, we analyzed the stepwise oxygen-insertion mechanism of tryptophan 2,3-dioxygenases, and transformed tryptophan 2,3-dioxygenase from Xanthomonas campestris into a monooxygenase for oxidative cyclization of tryptophans. It was revealed that residue F51 is vital in determining the product ratio of HPIC to N′-formylkynurenine. Our reactions and purification procedures use no organic solvents, resulting in an eco-friendly method to prepare HPICs for further applications.
DYE-SENSITIZED PHOTOOXYGENATION OF TRYPTOPHAN: 3a-HYDROPEROXYPYRROLOINDOLE AS A LABILE PRECURSOR OF FORMYLKYNURENINE
Nakagava, Masako,Kato, Shiro,Kataoka, Shigehiro,Kodato, Shinichi,Watanabe, Hideyuki,et al.
, p. 1013 - 1026 (2007/10/02)
The isolation, structure determination, and reactivity of the tricyclic labile hydroperoxides 10 and 2 obtained by dye-sensitized photooxygenation of L-, D-, and DL-tryptophan and Nb-methoxycarbonyltryptophan ester are reported.The tricyclic hydroperoxide 10, under apprpopiate conditions, was easily convertible to formylkynurenine.Plausible mechanisms for these transformations are discussed.Keywords-tryptophan and its derivatives; dye-sensitized photooxygenation; formylkynurenine; hydroperoxypyrroloindoles; 3-hydroperoxyindolenines; 1,3-benzoxazines; CD spectra; rearrangement; ring-chain tautomerism; biological oxidation
