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Synthesis of 3-Phenylserine by a Two-enzyme Cascade System with PLP Cofactor.
Xu, Mengjiao; Tan, Zhuotao; Qi, Siyu; Na, Qi; Zhang, Xiaowang; Zhuang, Wei; Zhu, Chenjie; Ying, Hanjie; Shen, Tao.
Affiliation
  • Xu M; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Tan Z; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Qi S; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Na Q; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Zhang X; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Zhuang W; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Zhu C; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Ying H; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
  • Shen T; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China.
Chemistry ; 30(10): e202302959, 2024 Feb 16.
Article in En | MEDLINE | ID: mdl-38012090
ABSTRACT
A two-enzyme cascade system containing ω-transaminase (ω-TA) and L-threonine aldolase (L-ThA) was reported for the synthesis of 3-Phenylserine starting from benzylamine, and PLP was utilized as the only cofactor in these both two enzymes reaction system. Based on the transamination results, benzylamine was optimized as an advantageous amino donor as confirmed by MD simulation results. This cascade reaction system could not only facilitate the in situ removal of the co-product benzaldehyde, enhancing the economic viability of the reaction, but also establish a novel pathway for synthesizing high-value phenyl-serine derivatives. In our study, nearly 95 % of benzylamine was converted, yielding over 54 % of 3-Phenylserine under the optimized conditions cascade reaction.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Serine / Glycine Hydroxymethyltransferase Language: En Journal: Chemistry Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: China

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Serine / Glycine Hydroxymethyltransferase Language: En Journal: Chemistry Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: China