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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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
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: Jun 7, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

The p-type ATPase superfamily.

Henry Chan1, Vartan Babayan, Elya Blyumin

  • 1Division of Biological Sciences, University of California at San Diego, La Jolla, CA, USA.

Journal of Molecular Microbiology and Biotechnology
|October 22, 2010
PubMed
Summary

P-type ATPases are vital across all life, with prokaryotes favoring heavy metal transporters and eukaryotes preferring ion/phospholipid transporters. This study reveals distinct evolutionary paths and horizontal gene transfer patterns for these essential enzymes.

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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

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Last Updated: Jun 7, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • P-type ATPases are crucial for cellular homeostasis in eukaryotes and are found in all domains of life.
  • Previous research classified eukaryotic P-type ATPases into characterized and functionally uncharacterized (FUPA) families.
  • A comprehensive analysis of prokaryotic P-type ATPases is needed for comparative insights.

Purpose of the Study:

  • To analyze P-type ATPases across major prokaryotic phyla.
  • To compare prokaryotic P-type ATPase distribution and evolution with those in eukaryotes.
  • To identify conserved functional motifs and evolutionary patterns, including horizontal gene transfer.

Main Methods:

  • Bioinformatic analysis of P-type ATPases in available prokaryotic genome sequences.
  • Comparative analysis with previously reported eukaryotic P-type ATPase data.
  • Identification and characterization of conserved functional motifs and gene fusion events.

Main Results:

  • Prokaryotes predominantly feature topological type I (heavy metal) P-type ATPases, while eukaryotes favor type II (ion/phospholipid) ATPases.
  • Distinct P-type ATPase families are exclusive to either prokaryotes (e.g., Kdp-type) or eukaryotes (e.g., phospholipid flippases).
  • Frequent horizontal gene transfer is observed in prokaryotes, with notable exceptions in certain bacterial phyla; transfer is rare between eukaryotes and prokaryotes.

Conclusions:

  • P-type ATPase distribution and evolution differ significantly between prokaryotes and eukaryotes, reflecting distinct functional adaptations.
  • Conserved functional motifs across families, rather than organisms, aid in predicting the function of uncharacterized ATPases.
  • P-type ATPases likely play a key role in protecting prokaryotes and unicellular eukaryotes from environmental stress.