Chin. J. Org. Chem. ›› 1993, Vol. 13 ›› Issue (5): 486-489. Previous Articles     Next Articles

Original Articles

酶催化反式肉桂酸类似物的不对称氨化反应

赵健身;杨顺楷;蒋耀忠   

  1. 中国科学院成都生物研究所.成都(610041);中国科学院成都有机化学研究所.成 都(610041)
  • 发布日期:1993-10-25

The asymmetric amination of trans-cinnamic acid analogs via enzyme

Zhao Jianshen;Yang Shunkai;Jiang Yaozhong   

  1. Chengdu Inst of Biology, CAS.Chengdu(610041);Chengdu Inst Organ Chem, CAS.Chengdu(610041)
  • Published:1993-10-25

Investigation on the amination to olefinic bond catalysed by Phenylalanine ammonialyase (PAL, EC 4.3.1.5) contained in Rhodotorula rubra (AS 2.166) whole cells, showed that only the two compounds, i.e. , 3-(2-furyl) acrylic acid (2i), 3-(3-methoxy-4-hydroxyphenyl) acrylic acid (2e), among the eight synthetic analogs of trans-Cinnamic acid: α-methyl-, β-methyl-, 4-nitro-, 4-methoxy-, 4-N, N-dimethylamino-, 4-methyl-Cinnamic acid and 2i, 2e, had been transformed into the corresponding optically pure L-isomer of α-amino acids, i.e., 3-(2- furyl) alanine (3i) and 3-(3-methoxy-4-hydroxyphenyl) alanine (3e). The chemical yields of 3i and 3e were 14.0% and 9.3% respectively, which are lower than that (44.8%) of L-Phenylalanine under the same conditions.

Key words: CINNAMYLIC ACID, RHODOTORULA, ENZYME CATALYSIS, PHENYLALANINE, ASYMMETRY

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