Limonene-1,2-epoxide hydrolase (LEH)

Limonene-1,2-epoxide hydrolase (LEH) is a specialized bacterial enzyme, primarily characterized in Rhodococcus erythropolis, that catalyzes the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol [1, 5]. It is a key component of the microbial limonene degradation pathway, allowing certain bacteria to utilize monoterpenes as a primary carbon and energy source [8, 29]. Structurally, LEH is distinct from the more common alpha/beta-hydrolase fold family of epoxide hydrolases, possessing a unique fold and employing a novel one-step catalytic mechanism that does not involve a covalent enzyme-substrate intermediate [8, 18]. While the Rhodococcus enzyme is widely used as a biocatalyst in industrial green chemistry for the synthesis of chiral building blocks [14, 15], its homolog in Mycobacterium tuberculosis (EphG) has been identified as a potential therapeutic target for anti-tubercular drug development [34, 35]. The enzyme is notably inhibited by the anticonvulsant drug valpromide, which has been utilized in structural studies to map the active site and understand its substrate specificity [8, 19]. Research into LEH and its homologs continues to explore their roles in bacterial detoxification and their potential as targets for novel antimicrobial agents [34, 39].

Other names

Limonene oxide hydrolaseLimonene-1,2-hydrolaselimAEphG

Inhibition of epoxide hydrolase activity