P-type ATPases: Many more enigmas left to solve
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P-type ATPases : Many more enigmas left to solve. / Palmgren, Michael.
In: Journal of Biological Chemistry, Vol. 299, No. 11, 105352, 2023.Research output: Contribution to journal › Review › Research › peer-review
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TY - JOUR
T1 - P-type ATPases
T2 - Many more enigmas left to solve
AU - Palmgren, Michael
N1 - Copyright © 2023 The Author. Published by Elsevier Inc. All rights reserved.
PY - 2023
Y1 - 2023
N2 - P-type ATPases constitute a large ancient super-family of primary active pumps that have diverse substrate specificities ranging from H+ to phospholipids. The significance of these enzymes in biology cannot be overstated. They are structurally related, and their catalytic cycles alternate between high- and low-affinity conformations that are induced by phosphorylation and dephosphorylation of a conserved aspartate residue. In the year 1988, all P-type sequences available by then were analyzed and five major families, P1 to P5, were identified. Since then, a large body of knowledge has accumulated concerning the structure, function, and physiological roles of members of these families, but only one additional family, P6 ATPases, has been identified. However, much is still left to be learned. For each family a few remaining enigmas are presented, with the intention that they will stimulate interest in continued research in the field. The review is by no way comprehensive and merely presents personal views with a focus on evolution.
AB - P-type ATPases constitute a large ancient super-family of primary active pumps that have diverse substrate specificities ranging from H+ to phospholipids. The significance of these enzymes in biology cannot be overstated. They are structurally related, and their catalytic cycles alternate between high- and low-affinity conformations that are induced by phosphorylation and dephosphorylation of a conserved aspartate residue. In the year 1988, all P-type sequences available by then were analyzed and five major families, P1 to P5, were identified. Since then, a large body of knowledge has accumulated concerning the structure, function, and physiological roles of members of these families, but only one additional family, P6 ATPases, has been identified. However, much is still left to be learned. For each family a few remaining enigmas are presented, with the intention that they will stimulate interest in continued research in the field. The review is by no way comprehensive and merely presents personal views with a focus on evolution.
KW - Adenosine Triphosphatases/metabolism
KW - P-type ATPases/metabolism
U2 - 10.1016/j.jbc.2023.105352
DO - 10.1016/j.jbc.2023.105352
M3 - Review
C2 - 37838176
VL - 299
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 11
M1 - 105352
ER -
ID: 381511972