28030-16-2Relevant articles and documents
Wheeler,Hoffman,Johnson
, p. 157 (1912)
Chemoenzymatic synthesis of L-3,4-dimethoxyphenyl-alanine and its analogues using aspartate aminotransferase as a key catalyst
Yu, Jinhai,Li, Jing,Cao, Shuangyan,Wu, Ting,Zeng, Shuiyun,Zhang, Hongjuan,Liu, Junzhong,Jiao, Qingcai
, p. 28 - 32 (2018/11/26)
In this study, a chemoenzymatic synthesis method for the production of L-3,4-dimethoxyphenyl-alanine and its analogues from phenylpyruvate derivatives was developed. The aspartate aminotransferase from Escherichia coli was engineered by error prone PCR and the improved variants were identified. When 3, 4-dimethoxy phenylpyruvate was added by fed-batch on a preparative scale, L-3,4-dimethoxyphenyl-alanine was formed in 95.4% conversion and > 99% ee with the best aspartate aminotransferase variant as the catalyst. This study provided an efficient method for the production of methoxy substituted phenylalanines using the engineered aspartate aminotransferase.
Synthesis and antiproliferative activity of marine bromotyrosine purpurealidin I and its derivatives
Bhat, Chinmay,Ilina, Polina,Tilli, Irene,Vorá?ová, Manuela,Bruun, Tanja,Barba, Victoria,Hribernik, Nives,Lillsunde, Katja-Emilia,M?ki-Lohiluoma, Eero,Rüffer, Tobias,Lang, Heinrich,Yli-Kauhaluoma, Jari,Kiuru, Paula,Tammela, P?ivi
, (2018/12/13)
The first total synthesis of the marine bromotyrosine purpurealidin I (1) using trifluoroacetoxy protection group and its dimethylated analog (29) is reported along with 16 simplified bromotyrosine derivatives lacking the tyramine moiety. Their cytotoxici