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Phosphotransferases (EC 2.7) catalyze the transfer of phosphate groups from phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the substrate gains a phosphate group and a specific donor molecule provides a phosphate group. Biocatalytic phosphorylation has the advantage of mild reaction conditions and avoids additional reaction steps such as protection and deprotection of functional groups.

The figure shows the general reaction equation for biocatalytic phosphorylation

General reaction formula of biocatalytic phosphorylation

The main-category phosphotransferase is divided into subcategories based on the type of group that accepts the transfer. Functional groups that are classified as phosphate acceptors include: hydroxyl-, carboxyl groups such as nitrogenous and sulfurous groups. Important constituents of this subclass of transferases are various kinases which transfer a phosphate group from ATP to a substrate. So, ATP has to be added when working with kinases in stoichiometric quantities or alternatively regenerated using other energy-rich compounds like Phosphoenole pyruvate. In addition to that, there are additional phosphoryl donors in nature like pyrophosphate with varying energy level, availability, and specificity which can be used for biocatalytic phosphate group transfer. While the number of enzymes that catalyze the formation of -N–P–, -S–P–, and -C–P bonds is limited, a large number of phosphorylases, phosphatases, and phosphotransferases/kinases has been described for the biocatalytic -O-P- bond formation.

The figure shows the scheme of a kinase-catalyzed phosphorylation

Schematic of a kinase catalyzed phosphorylation