phosphorus-radioisotopes and 2-phosphoglycerate

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

Topics: Biocatalysis; Endopeptidases; Escherichia coli; Glyceric Acids; Kinetics; Magnetic Resonance Spectroscopy; Maltose-Binding Proteins; Phosphorus Radioisotopes; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor); Recombinant Fusion Proteins; Stereoisomerism; Thermotoga maritima