Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12

Varování

Publikace nespadá pod Lékařskou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	SCHUITEN Eva D. BADENHORST Christoffel P. S. PALM Gottfried J. BERNDT Leona LAMMERS Michael MIČAN Jan BEDNÁŘ David DAMBORSKÝ Jiří BORNSCHEUER Uwe T.
Rok publikování	2021
Druh	Článek v odborném periodiku
Časopis / Zdroj	ACS Catalysis
Fakulta / Pracoviště MU	Přírodovědecká fakulta
Citace
www	https://pubs.acs.org/doi/10.1021/acscatal.1c00851
Doi	http://dx.doi.org/10.1021/acscatal.1c00851
Klíčová slova	catalytic promiscuity; Corynebacterium; epoxide hydrolase; haloalkane dehalogenase; dual activity
Popis	Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an S(N)2 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 mu mol 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.