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Highly efficient preparation of active S-phenyl-L-cysteine with tryptophan synthase using a chemoenzymatic method.
BMC Biotechnology ( IF 3.5 ) Pub Date : 2019-07-18 , DOI: 10.1186/s12896-019-0538-2
Lisheng Xu 1 , Xingtao Zhang 1 , Guizhen Gao 1 , Sun Yue 1
Affiliation  

BACKGROUND S-Phenyl-L-cysteine is regarded as having potential applicability as an antiretroviral/protease inhibitor for human immunodeficiency virus (HIV). In the present study, optically active S-phenyl-L-cysteine was prepared in a highly efficient manner from inexpensive bromobenzene using tryptophan synthase through a chemoenzymatic method. RESULTS The chemoenzymatic method used a four-step reaction sequence. The process started with the reaction of magnesium and bromobenzene, followed by a Grignard reaction, and then hydrolysis and enzymatic synthesis using tryptophan synthase. Through this approach, S-phenyl-L-cysteine was chemoenzymatically synthesized using tryptophan synthase from thiophenol and L-serine as the starting material. CONCLUSIONS High-purity, optically active S-phenyl-L-cysteine was efficiently and inexpensively obtained in a total yield of 81.3% (> 99.9% purity).

中文翻译:

色氨酸合酶使用化学酶法高效制备活性S-苯基-L-半胱氨酸。

背景技术S-苯基-L-半胱氨酸被认为具有潜在的适用性,可作为人类免疫缺陷病毒(HIV)的抗逆转录病毒/蛋白酶抑制剂。在本研究中,旋光活性S-苯基-L-半胱氨酸是通过使用色氨酸合酶通过化学酶法从廉价的溴苯中高效制备的。结果化学酶法采用四步反应序列。该过程开始于镁和溴苯的反应,然后进行格氏反应,然后使用色氨酸合酶进行水解和酶促合成。通过这种方法,使用色氨酸合酶从苯硫酚和L-丝氨酸为起始原料,化学合成了S-苯基-L-半胱氨酸。结论高纯度
更新日期:2019-07-18
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