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Related Concept Videos

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...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
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...
Stomach pH Regulation01:21

Stomach pH Regulation

The human body carefully regulates the internal pH of different organs to maintain homeostasis. For example, while the blood plasma maintains a neutral pH of 7, the stomach lumen has an acidic pH of 1.5 - 3.5. The low pH of stomach lumen helps kill pathogens in the food and break down complex food molecules.
The acid-secreting gastric mucosal epithelial cells (parietal cells) lining the stomach lumen maintain the low pH in the lumen. Numerous ion transporters and channels on these parietal...
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...

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Related Experiment Video

Updated: Jul 4, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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

The gastric HK-ATPase: structure, function, and inhibition.

Jai Moo Shin1, Keith Munson, Olga Vagin

  • 1Department of Physiology, David Geffen School of Medicine, University of California at Los Angeles and VA Greater Los Angeles Healthcare System, Los Angeles, CA 90073, USA.

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Summary

The gastric H,K-ATPase proton pump facilitates acid secretion via conformational changes. Its inhibition by proton pump inhibitors offers a therapeutic strategy for acid-related diseases.

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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

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Last Updated: Jul 4, 2026

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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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
07:38

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • The gastric H,K-ATPase is a P(2)-type ATPase crucial for gastric acid secretion.
  • It comprises alpha,beta subunits, with the alpha subunit containing transmembrane segments involved in ion binding.

Purpose of the Study:

  • To elucidate the structure-function relationship of the gastric H,K-ATPase.
  • To understand the mechanism of proton translocation and its regulation.

Main Methods:

  • Comparative analysis with SERCA pump structure.
  • Site-directed mutagenesis.
  • Molecular modeling.
  • Analysis of N-linked glycosylation roles.

Main Results:

  • Identified key carboxylic amino acids in transmembrane segments as part of the ion binding domain.
  • Proposed a mechanism involving lysine 791 movement for proton expulsion.
  • Highlighted the role of KCNQ1/KCNE2 and Clic6 in potassium transport and enzyme resetting.

Conclusions:

  • Gastric H,K-ATPase utilizes conformational changes (E1 to E2) for acid secretion.
  • N-glycosylation is vital for enzyme maturation and sorting.
  • The enzyme's unique mechanism is a target for proton pump inhibitors in treating acid-related disorders.