614-03-9Relevant articles and documents
Enantioselective synthesis of (S)-phenylephrine by recombinant Escherichia coli cells expressing the short-chain dehydrogenase/reductase gene from Serratia quinivorans BCRC 14811
Peng, Guan-Jhih,Cho, Yen-Ching,Fu, Tze-Kai,Yang, Ming-Te,Hsu, Wen-Hwei
, p. 1509 - 1515 (2013)
Background An amino alcohol dehydrogenase gene (RE-AADH) from Rhodococcus erythropolis BCRC 10909 has been used for the conversion of 1-(3-hydroxyphenyl)- 2-(methylamino) ethanone (HPMAE) to (S)-phenylephrine [(S)-PE]. However RE-AADH uses NADPH as cofactor, and only limited production of (S)-PE from HPMAE is achieved. Methods A short-chain dehydrogenase/reductase gene (SQ-SDR) from Serratia quinivorans BCRC 14811 was expressed in Escherichia coli BL21 (DE3) for the conversion of HPMAE to (S)-PE. Results The SQ-SDR enzyme was capable of converting HPMAE to (S)-PE in the presence of NADH and NADPH, with specific activities of 26.5 ± 2.3 U/mg protein and 0.24 ± 0.01 U/mg protein, respectively, at 30 C and at a pH of 7.0. The E. coli BL21 (DE3), expressing NADH-preferring SQ-SDR, converted HPMAE to (S)-PE with more than 99% enantiomeric excess, a conversion yield of 86.6% and a productivity of 20.2 mmol/l h, which was much higher than our previous report using E. coli NovaBlue expressing NADPH-dependent RE-AADH as the biocatalyst. Conclusion The SQ-SDR enzyme with its high catalytic activity and strong preference for NADH as a cofactor provided a significant advantage in bioreduction.
Enantioselective synthesis of (S)-phenylephrine by whole cells of recombinant Escherichia coli expressing the amino alcohol dehydrogenase gene from Rhodococcus erythropolis BCRC 10909
Lin, Wei-De,Chen, Chien-Yu,Chen, Huei-Chung,Hsu, Wen-Hwei
experimental part, p. 1529 - 1536 (2011/12/15)
(R)-phenylephrine [(R)-PE] is an α1-adrenergic receptor agonist that is widely used in over-the-counter drugs to treat the common cold. We found that Rhodococcus erythropolis BCRC 10909 can convert detectable level of 1-(3-hydroxyphenyl)-2-(methylamino) ethanone (HPMAE) to (S)-PE by high performance liquid chromatography tandem mass spectrometry analysis. An amino alcohol dehydrogenase gene (RE_AADH) which possesses the ability to convert HPMAE to (S)-PE was then isolated from R. erythropolis BCRC 10909 and expressed in Escherichia coli NovaBlue. The purified RE_AADH, tagged with 6×His, had a molecular mass of approximately 30kDa and exhibited a specific activity of 0.19μU/mg to HPMAE in the presence of NADPH, indicating this enzyme could be categorized as NADP+-dependent short-chain dehydrogenase reductase. E. coli NovaBlue cell expressing the RE_AADH gene was able to convert HPMAE to (S)-PE with more than 99% enantiomeric excess (ee), 78% yield and a productivity of 3.9mmol(S)-PE/Lh in 12h at 30°C and pH 7. The (S)-PE, recovered from reaction mixture by precipitation at pH 11.3, could be converted to (R)-PE (ee>99%) by Walden inversion reaction. This is the first reported biocatalytic process for the production of (S)-PE from HPMAE.
PROCESS FOR THE PREPARATION OF OPTICALLY ACTIVE 2-AMINO-1-PHENYLETHANOLS
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Page/Page column 10-11, (2008/12/06)
Optically active 2-amino-l-phenylethanols of formula (I) or its mirror image, wherein R1 is hydrogen, C1-6alkyl or aryl-substituted C1-6alkyl and R2 through R6 are independently hydrogen, hydroxy or C1-6alkoxy, or salts thereof are prepared by asymmetric hydrogenation of the corresponding 2-aminoacetophenones in the presence of a ruthenium complex catalyst comprising a chiral phosphine ligand.
