An Immobilized Marine Glycosyltransferase Acts as a Stabilized Biocatalyst for the Synthesis of Mannosylated Phosphoisoprenoids

Abstract

Glycosylated phosphoisoprenoids constitute valuable bioactive molecules and starting materials for complex glycosylation cascades. Herein we report the identification and the functional characterization of a newly identified polyprenyl phosphomannose synthase from the marine microorganism Rhodococcus erythropolis PR4. This enzyme, normally unstable in its free form, is significantly stabilized by immobilization and can be reused up to four times for sustainable phosphoisoprenoid derivatization.