Phosphotransferase

Phosphotransferase is an enzyme that catalyzes the transfer of a phosphate group from a donor molecule to an acceptor molecule. The process is known as phosphorylation. Phosphotransferases are a broad group of enzymes, each of which is specific for its donor and acceptor molecules, making them important for a wide range of cellular processes.

Function[edit | edit source]

Phosphotransferases play a crucial role in many biological processes, including metabolism, signal transduction, and protein regulation. They are involved in the transfer of phosphate groups in ATP to various substrates, which can activate or deactivate many metabolic pathways.

Classification[edit | edit source]

Phosphotransferases are classified under the EC number 2.7. This group is further divided into nine subclasses based on the type of group that accepts the phosphate. These include:

EC 2.7.1: The phosphate group is transferred to an alcohol
EC 2.7.2: The phosphate group is transferred to a carboxyl group
EC 2.7.3: The phosphate group is transferred to an amino group
EC 2.7.4: The phosphate group is transferred to a nitrogenous base
EC 2.7.7: The phosphate group is transferred to a nucleotide

Examples[edit | edit source]

Some examples of phosphotransferases include:

Kinase: This is the most common type of phosphotransferase, which transfers a phosphate group from ATP to a protein in a cell. It plays a key role in the regulation of cellular processes.
Polymerase: This enzyme catalyzes the polymerization of nucleotides, forming a nucleic acid polymer.
Phosphoglycerate kinase: This enzyme plays a key role in the process of glycolysis, where it catalyzes the transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate.