In biological systems, gaseous alkanes are oxidized to epoxides by monooxygenases. Without detoxification, these highly reactive metabolites can cause cellular damage by oxidizing membrane lipids and alkylating proteins and nucleic acids. Gaseous alkene-metabolizing bacteria have diverse epoxide-degrading mechanisms. Mycobacterium sp. ELW1 grows on isobutylene, the simplest branched alkene, and is one of the few bacteria in which epoxide hydrolysis is involved in metabolism. The enzyme responsible for epoxide hydrolysis in strain ELW1 is an epoxide hydrolase (EphA). In this study, we heterologously expressed EphA and have explored the structural and catalytic features of the enzyme.