3 years ago

Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate-2-Kinase

Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate-2-Kinase
Markus Obkircher, Wolfgang R. Streit, Bernhard Schoenenberger, Roland Wohlgemuth, Jennifer Chow, Birhanu M. Kinfu, Norman Hardt
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. Quicker and cleaner: Recombinant glycerate-2-kinase from T. maritima showed excellent selectivity towards phosphorylation of the d-enantiomer of glyceric acid, with no phosphorylation of the l-enantiomer. This straightforward phosphorylation reaction and subsequent product isolation enables the central glycolytic metabolite d-glycerate 2-phosphate to be prepared in fewer reaction steps and with higher purity than chemical routes.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/cbic.201700201

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