Biocatalytic Asymmetric Phosphorylation catalyzed by recombinant Glycerate‐2‐kinase

The efficient synthesis of pure D-glycerate-2-phosphate is of much interest due to its importance as enzyme substrate and metabolite. A straightforward one-step biocatalytic phosphorylation of glyceric acid has been investigated. Glycerate 2-kinase from Thermotoga maritima has been expressed in Escherichia coli allowing easy purification. The selective glycerate 2-kinase-catalyzed phosphorylation has been followed by 31P-NMR and showed excellent enantioselectivity towards the phosphorylation of the D-enantiomer of glyceric acid. This straightforward phosphorylation reaction and the subsequent product isolation has enabled the preparation of enantiomerically pure D-glycerate 2-phosphate. This phosphorylation reaction using recombinant glycerate 2-kinase is highly selective and sustainable, as it yields D-glycerate 2-phosphate in less reaction steps and with higher purity than chemical routes.