Title : Enhancing the enantioselectivity of an epoxide hydrolase by directed evolution - Reetz_2004_Org.Lett_6_177 |
Author(s) : Reetz MT , Torre C , Eipper A , Lohmer R , Hermes M , Brunner B , Maichele A , Bocola M , Arand M , Cronin A , Genzel Y , Archelas A , Furstoss R |
Ref : Org Lett , 6 :177 , 2004 |
Abstract :
[reaction: see text] The epoxide hydrolase (EH) from Aspergillus niger, which shows a selectivity factor of only E = 4.6 in the hydrolytic kinetic resolution of glycidyl phenyl ether, has been subjected to directed evolution for the purpose of enhancing enantioselectivity. After only one round of error-prone polymerase chain reaction (epPCR), enantioselectivity was more than doubled (E = 10.8). The improved mutant enzyme contains three amino acid exchanges, two of which are spatially far from the catalytically active center. |
PubMedSearch : Reetz_2004_Org.Lett_6_177 |
PubMedID: 14723522 |
Gene_locus related to this paper: aspni-hyl1 |
Substrate | Glycidyl-phenyl-ether |
Gene_locus | aspni-hyl1 |
Reetz MT, Torre C, Eipper A, Lohmer R, Hermes M, Brunner B, Maichele A, Bocola M, Arand M, Cronin A, Genzel Y, Archelas A, Furstoss R (2004)
Enhancing the enantioselectivity of an epoxide hydrolase by directed evolution
Org Lett
6 :177
Reetz MT, Torre C, Eipper A, Lohmer R, Hermes M, Brunner B, Maichele A, Bocola M, Arand M, Cronin A, Genzel Y, Archelas A, Furstoss R (2004)
Org Lett
6 :177