Highly active mutants of carbonyl reductase S1 with inverted coenzyme specificity and production of optically active alcohols

…, T Nakai, Y Yasohara, H Nanba, N Kizaki…

Index: Morikawa, Souichi; Nakai, Takahisa; Yasohara, Yoshihiko; Nanba, Hirokazu; Kizaki, Noriyuki; Hasegawa, Junzo Bioscience, Biotechnology and Biochemistry, 2005 , vol. 69, # 3 p. 544 - 552

Full Text: HTML

Citation Number: 29

Abstract

A wild type NADPH-dependent carbonyl reductase from Candida magnoliae (reductase S1) has been found not to utilize NADH as a coenzyme. A mutation to exchange the coenzyme specificity in reductase S1 has been designed by computer-aided methods, including three- dimensional structure modeling and in silico screening of enzyme mutants. Site-directed mutagenesis has been used to introduce systematic substitutions of seven or eight amino ...