Journal Article

Substrate specificity and stereospecificity of limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14; an enzyme showing sequential and enantioconvergent substrate conversion

de Bont, J. A. M., Faber, K., Osprian, I., Swarts, H. J., van der Werf, M. J., Orru, R. V. A., Overkamp, K. M., Steinreiber, A.

1999

Overview

Limonene-1,2-epoxide hydrolase (LEH) from Rhodococcus erythropolis DCL14, an enzyme involved in the limonene degradation pathway of this microlorganism, has a narrow substrate specificity. Of the compounds tested, the natural substrate, limonene-1,2-epoxide, and several alicyclic and 2-methyl-1,2-epoxides (e.g. 1-methylcyclohexene oxide and indene oxide), were substrates for the enzyme. When LEH was incubated with a diastereomeric mixture of limonene-1,2-epoxide, the sequential hydrolysis of first the (1R,2S)- and then the (1S,2R)-isomer was observed. The hydrolysis of (4R)- and (4S)-limonene-1,2-epoxide resulted in, respectively, (1S,2S,4R)- and (1R,2R,4S)-limonene-1,2-diol as the sole product with a diastereomeric excess of over 98%. With all other substrates, LEH showed moderate to low enantioselectivities (E ratios between 34 and 3).

• Publisher: Springer,Springer Nature B.V
• Subject: Bacteria / Biological and medical sciences / Biology of microorganisms of confirmed or potential industrial interest / Biotechnology / Enzymes / Epoxide hydrolase / Epoxides / Fundamental and applied biological sciences. Psychology / Hydrolysis / Indene / Industrial Microbiology / Industriële microbiologie / Limonene / limonene-1,2-epoxide hydrolase / Microbiology / Miscellaneous / Mission oriented research / Rhodococcus / Rhodococcus erythropolis / Stereospecificity / Substrate specificity / Substrates / VLAG