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Heterologous pathway for the production of L-phenylglycine from glucose by E. coli.
Liu, Shuang Ping; Liu, Rui Xia; El-Rotail, Ashraf A M M; Ding, Zhong Yang; Gu, Zheng Hua; Zhang, Liang; Shi, Gui Yang.
Afiliación
  • Liu SP; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China. Electronic address: liushuangping668@126.com.
  • Liu RX; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China.
  • El-Rotail AA; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China.
  • Ding ZY; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China.
  • Gu ZH; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China.
  • Zhang L; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China. Electronic address: zhangl@jiangnan.edu.cn.
  • Shi GY; The Key Laboratory of Industrial Biotechnology, Ministry of Education, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China. Electronic address: gyshi@jiangnan.edu.cn.
J Biotechnol ; 186: 91-7, 2014 Sep 30.
Article en En | MEDLINE | ID: mdl-25011099
The aproteinogenic amino acid L-phenylglycine (L-Phg) is an important side chain building block for the preparation of several antibiotics and taxol. To biosynthesis L-Phg from glucose, an engineered Escherichia coli containing L-Phg synthetic genes was firstly developed by an L-phenylalanine producing chassis supplying phenylpyruvate. The enzymes HmaS (L-4-hydroxymandelate synthase), Hmo (L-4-hydroxymandelate oxidase) and HpgT (L-4-hydroxyphenylglycine transaminase) from Amycolatopsis orientalis as well as Streptomyces coelicolor were heterologously expressed in E. coli and purified to evaluate their abilities on L-Phg formation. HpgT conversing phenylglyoxylate to L-Phg uses an unusual amino donor L-phenylalanine, which releases another phenylpyruvate as the substrate of HmaS. Thus, a recycle reaction was developed to maximize the utilization of precursor phenylpyruvate. To amplify the accumulation of L-Phg, the effects of attenuating L-phenylalanine transamination was investigated. After deletion of tyrB and aspC, L-Phg yield increased by 12.6-fold. The limiting step in the L-Phg biosynthesis was also studied; the L-Phg yield was further improved by 14.9-fold after enhancing hmaS expression. Finally, by optimizing expression of hmaS, hmo and hpgT and attenuation of L-phenylalanine transamination, the L-Phg yield was increased by 224-fold comparing with the original strain.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Recombinantes / Escherichia coli / Glicina / Transaminasas Idioma: En Revista: J Biotechnol Asunto de la revista: BIOTECNOLOGIA Año: 2014 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Recombinantes / Escherichia coli / Glicina / Transaminasas Idioma: En Revista: J Biotechnol Asunto de la revista: BIOTECNOLOGIA Año: 2014 Tipo del documento: Article Pais de publicación: Países Bajos