Schuiten_2021_ACS.Catal_11_6113

Reference

Title : Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12 - Schuiten_2021_ACS.Catal_11_6113
Author(s) : Schuiten ED , Badenhorst CPS , Palm GJ , Berndt L , Lammers M , Mican J , Bednar D , Damborsky J , Bornscheuer UT
Ref : ACS Catal , 11 :6113 , 2021
Abstract :

Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an SN2 attack on their substrates. Despite their mechanistic similarities, no enzymes are known that exhibit both epoxide hydrolase and dehalogenase activity. We screened a subset of epoxide hydrolases, closely related to dehalogenases, for dehalogenase activity and found that the epoxide hydrolase CorEH from Corynebacterium sp. C12 exhibits promiscuous dehalogenase activity. Compared to the hydrolysis of epoxides like cyclohexene oxide (1.41 micromol min-1 mg-1), the dehalogenation of haloalkanes like 1-bromobutane (0.25 nmol min-1 mg-1) is about 5000-fold lower. In addition to the activity with 1-bromobutane, dehalogenase activity was detected with other substrates like 1-bromohexane, 1,2-dibromoethane, 1-iodobutane, and 1-iodohexane. This study shows that dual epoxide hydrolase and dehalogenase activity can be present in one naturally occurring protein scaffold.

PubMedSearch : Schuiten_2021_ACS.Catal_11_6113
PubMedID:
Gene_locus related to this paper: corsp-cEH

Related information

Gene_locus corsp-cEH
Structure 7AC0

Citations formats

Schuiten ED, Badenhorst CPS, Palm GJ, Berndt L, Lammers M, Mican J, Bednar D, Damborsky J, Bornscheuer UT (2021)
Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12
ACS Catal 11 :6113

Schuiten ED, Badenhorst CPS, Palm GJ, Berndt L, Lammers M, Mican J, Bednar D, Damborsky J, Bornscheuer UT (2021)
ACS Catal 11 :6113