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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...
Primary Active Transport01:47

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they...
Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...

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Related Experiment Video

Updated: May 30, 2026

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses
08:34

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses

Published on: May 9, 2021

Pumping ions.

Ronald J Clarke1, Xiaochen Fan

  • 1School of Chemistry, University of Sydney, New South Wales, Australia. r.clarke@chem.usyd.edu.au

Clinical and Experimental Pharmacology & Physiology
|August 19, 2011
PubMed
Summary
This summary is machine-generated.

This review details the Na+/K+-ATPase, a vital ion pump. Research shows it has one ATP site, acting catalytically or allosterically, and functions as protomers, not diprotomers, influencing enzyme kinetics.

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Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone
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Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone

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On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids
10:32

On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids

Published on: March 2, 2012

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Last Updated: May 30, 2026

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses
08:34

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses

Published on: May 9, 2021

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone
08:06

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone

Published on: February 23, 2017

On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids
10:32

On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids

Published on: March 2, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Membrane Transport

Background:

  • The Na+/K+-ATPase is crucial for maintaining ion gradients across animal cell membranes.
  • Its discovery and characterization span over 150 years, from early observations to structural insights.
  • Understanding its mechanism is key to comprehending cellular energy transduction.

Purpose of the Study:

  • To review the historical development and mechanistic understanding of the Na+/K+-ATPase.
  • To present the authors' contributions regarding the allosteric role of ATP and enzyme quaternary structure.
  • To resolve the protomer versus diprotomer controversy in P-type ATPases.

Main Methods:

  • Historical literature review.
  • Analysis of kinetic data.
  • Interpretation of structural information.

Main Results:

  • The Na+/K+-ATPase possesses a single ATP binding site, exhibiting dual catalytic and allosteric functions.
  • The enzyme exists and functions as αβ protomers, dissociating from (αβ)2 diprotomers upon ATP binding.
  • Protein-protein interactions within diprotomers modulate enzymatic turnover, with one protomer potentially hindering the other.

Conclusions:

  • The Na+/K+-ATPase mechanism is clarified, highlighting a single ATP site and protomeric function.
  • ATP-induced dissociation resolves the protomer/diprotomer debate for this enzyme.
  • Enzyme kinetics are significantly influenced by the quaternary structure and inter-protomer interactions.