What is the catalytic mechanism of P-type ATPases?
The catalytic mechanism of P-type ATPases involves a series of highly coordinated steps. Initially, the enzyme binds to the ion and ATP. ATP is hydrolyzed to ADP, leading to the phosphorylation of a conserved aspartate residue in the enzyme. This phosphorylation induces a conformational change that allows the ion to be translocated across the membrane. Subsequently, the enzyme is dephosphorylated, which resets it to its original conformation, ready for another cycle of ion transport.
