Functional expression and characterization of eryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of l-Erythritol-4-phosphate

The eryA gene of the bacterial pathogen Brucella abortus has been functionally expressed in Escherichia coli. The resultant EryA was shown to catalyze the ATP-dependent conversion of erythritol to l-erythritol-4-phosphate ( l-E4P). The steady state kinetic parameters of this reaction were determined and the enzyme was used to prepare l-E4P which was shown to be a weak inhibitor of 2- C-methyl- d-erythritol-4-phosphate cytidyltransferase (YgbP). The eryA gene has been functionally expressed in Escherichia coli, and the resultant EryA was shown to catalyze the ATP-dependent conversion of erythritol ( 1) to l-erythritol-4-phosphate ( 2, l-E4P).