Abo M, Tachibana M, Okubo A, Yamazaki S
Department of Applied Biological Chemistry, University of Tokyo, Japan.
Bioorg Med Chem. 1995 Feb;3(2):109-12. doi: 10.1016/0968-0896(95)00004-z.
The substrate specificity and enantioselectivity of DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans were studied on a series of alkyl aryl sulfoxides as substrate. The enzyme was found to catalyze deoxygenation of (S)-sulfoxides predominantly. (R)-Sulfoxides were recovered with a high enantiomeric excess.
以一系列烷基芳基亚砜为底物,研究了脱氮红假单胞菌中DMSO还原酶的底物特异性和对映体选择性。发现该酶主要催化(S)-亚砜的脱氧反应。回收得到的(R)-亚砜具有很高的对映体过量值。