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P-type ATPase
The P-type ATPases, also known as E1-E2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. They are α-helical bundle primary transporters referred to as ''P-type'' ATPases because they catalyze auto- (or self-) phosphorylation of a key conserved aspartate residue within the pump. In addition, they all appear to interconvert between at least two different conformations, denoted by E1 and E2.
Most members of this transporter family are specific for the pumping of a large array of cations, however one subfamily is involved in flipping phospholipids to maintain the asymmetric nature of the biomembrane.
Prominent examples of P-type ATPases are the sodium-potassium pump (Na+,K+-ATPase), the plasma membrane proton pump (H+-ATPase), the proton-potassium pump (H+,K+-ATPase), and the calcium pump (Ca2+-ATPase).
== Discovery ==
The first P-type ATPase discovered was the Na+,K+-ATPase, which Nobel laureate Jens Christian Skou isolated in 1957. The Na+,K+-ATPase was only the first member of a large and still-growing protein family, which in May 2013 had around 500 confirmed and unique members in Swiss-Prot ((Prosite motif PS00154 )).
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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