23295-92-3Relevant academic research and scientific papers
Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate-2-Kinase
Hardt, Norman,Kinfu, Birhanu M.,Chow, Jennifer,Schoenenberger, Bernhard,Streit, Wolfgang R.,Obkircher, Markus,Wohlgemuth, Roland
, p. 1518 - 1522 (2017)
The efficient synthesis of pure d-glycerate-2-phosphate is of great interest due to its importance as an enzyme substrate and metabolite. Therefore, we investigated a straightforward one-step biocatalytic phosphorylation of glyceric acid. Glycerate-2-kinase from Thermotoga maritima was expressed in Escherichia coli, allowing easy purification. The selective glycerate-2-kinase-catalyzed phosphorylation was followed by 31P NMR and showed excellent enantioselectivity towards phosphorylation of the d-enantiomer of glyceric acid. This straightforward phosphorylation reaction and subsequent product isolation enabled the preparation of enantiomerically pure d-glycerate 2-phosphate. This phosphorylation reaction, using recombinant glycerate-2-kinase, yielded d-glycerate 2-phosphate in fewer reaction steps and with higher purity than chemical routes.
