Fucokinase, its anomeric specificity and mechanism of phosphate group transfer

Abstract

Fucokinase phosphorylates l-fucose at the anomeric position and, as such, might use either the α or β anomer as its substrate. Examination of the utilization of radiolabelled α and α,β mixtures established β- l-fucose as the required substrate. Phosphorylation at the anomeric center might involve either the loss or retention of the anomeric oxygen. The mechanism has been shown to involve anomeric oxygen retention through mass spectrometric analysis of the product phosphate derived from 18O-labelled l-fucose.