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 journalReviewResearchpeer-review

Harvard

Palmgren, M 2023, 'P-type ATPases: Many more enigmas left to solve', Journal of Biological Chemistry, vol. 299, no. 11, 105352. https://doi.org/10.1016/j.jbc.2023.105352

APA

Palmgren, M. (2023). P-type ATPases: Many more enigmas left to solve. Journal of Biological Chemistry, 299(11), [105352]. https://doi.org/10.1016/j.jbc.2023.105352

Vancouver

Palmgren M. P-type ATPases: Many more enigmas left to solve. Journal of Biological Chemistry. 2023;299(11). 105352. https://doi.org/10.1016/j.jbc.2023.105352

Author

Palmgren, Michael. / P-type ATPases : Many more enigmas left to solve. In: Journal of Biological Chemistry. 2023 ; Vol. 299, No. 11.

Bibtex

@article{850943d67dc849299ed55896334d0dd7,
title = "P-type ATPases: Many more enigmas left to solve",
abstract = "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.",
keywords = "Adenosine Triphosphatases/metabolism, P-type ATPases/metabolism",
author = "Michael Palmgren",
note = "Copyright {\textcopyright} 2023 The Author. Published by Elsevier Inc. All rights reserved.",
year = "2023",
doi = "10.1016/j.jbc.2023.105352",
language = "English",
volume = "299",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "11",

}

RIS

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