TY - JOUR
T1 - Chemo-enzymatic route for (R)-terbutaline hydrochloride based on microbial asymmetric reduction of a substituted α-chloroacetophenone derivative
AU - Taketomi, Shohei
AU - Asano, Masayoshi
AU - Higashi, Toshinori
AU - Shoji, Mitsuru
AU - Sugai, Takeshi
N1 - Funding Information:
This work was supported by “SORST: Solution-Oriented Research for Science and Technology” of Japan Science and Technology Corporation , and we express our sincere thanks to Professors Keisuke Suzuki, Takashi Matsumoto, Ken Ohmori of Tokyo Institute of Technology. This work was also supported by “High-Tech Research Center” Project for Private Universities: matching fund subsidy 2006–2011 from the Ministry of Education, Culture, Sports, Science and Technology, Japan, and acknowledged with thanks. We acknowledge Novozymes Japan for the generous gift of Novozym 435. M. A. thanks Japan Student Service Organization, for the exemption from repayment upon graduation for graduate school students with outstanding results (2007).
PY - 2012/12
Y1 - 2012/12
N2 - To synthesize (R)-terbutaline hydrochloride, a potent β 2- adrenoceptor-stimulating agent, asymmetric reduction of a substituted α-chloroacetophenone derivative with cultured whole-cell biocatalyst of the yeast Williopsis californica JCM 3600 was developed as the key reaction. The reduction proceeded by a si-facial attack of hydride in a highly enantioselective manner. Co-factor generation was enhanced by applying glycerol as the carbon source.
AB - To synthesize (R)-terbutaline hydrochloride, a potent β 2- adrenoceptor-stimulating agent, asymmetric reduction of a substituted α-chloroacetophenone derivative with cultured whole-cell biocatalyst of the yeast Williopsis californica JCM 3600 was developed as the key reaction. The reduction proceeded by a si-facial attack of hydride in a highly enantioselective manner. Co-factor generation was enhanced by applying glycerol as the carbon source.
KW - Asymmetric reduction
KW - Hydrolysis
KW - Lipase
KW - Yeast
UR - http://www.scopus.com/inward/record.url?scp=84866431759&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84866431759&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2012.01.020
DO - 10.1016/j.molcatb.2012.01.020
M3 - Article
AN - SCOPUS:84866431759
SN - 1381-1177
VL - 84
SP - 83
EP - 88
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
ER -