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Hydrolysis of ATP

Hydrolysis of ATP

The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...

ATP Driven Pumps I: An Overview

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...

ATP Energy Storage and Release

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...

ATP and Energy Production

ATP and Energy Production

Adenosine triphosphate (ATP) is a critical molecule that functions as the main energy carrier in cells. Structurally, ATP consists of an adenosine molecule—comprising adenine and ribose—bonded to three phosphate groups. The high-energy bonds between these phosphate groups store significant amounts of potential energy. This energy is released during hydrolysis, wherein ATP is converted to adenosine diphosphate (ADP) or adenosine monophosphate (AMP), driving a variety of essential...

ATP Synthase: Structure

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...

Coupled Reactions

Coupled Reactions

Cellular processes such as building and breaking down complex molecules occur through stepwise chemical reactions. Some of these chemical reactions are spontaneous and release energy, whereas others require energy to proceed. Cells often couple the energy-releasing reaction with the energy-requiring one to carry out important cell functions.
Energy in adenosine triphosphate or ATP molecules is easily accessible to do work. ATP powers the majority of energy-requiring cellular reactions....

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Related Experiment Video

Updated: Mar 2, 2026

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

ATP as a biological hydrotrope.

Avinash Patel¹, Liliana Malinovska¹, Shambaditya Saha¹

¹Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.

Science (New York, N.Y.)

|May 20, 2017

Summary

Adenosine triphosphate (ATP) functions as a biological hydrotrope, preventing and dissolving protein aggregates at high cellular concentrations. This property helps maintain protein solubility, complementing its role as an energy source.

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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

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Measuring In Vitro ATPase Activity for Enzymatic Characterization

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Related Experiment Videos

Last Updated: Mar 2, 2026

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

Published on: August 17, 2019

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

Hydrotropes are low-cooperativity molecules that solubilize hydrophobic compounds in aqueous solutions at molar concentrations.
Classical surfactants differ from hydrotropes in their aggregation behavior and concentration dependence.
Adenosine triphosphate (ATP) is primarily known as the cell's energy currency, typically found in micromolar concentrations for metabolic reactions.

Purpose of the Study:

To investigate whether adenosine triphosphate (ATP) exhibits hydrotropic properties.
To determine if ATP can influence the solubility and aggregation state of proteins.
To explore the potential role of ATP's hydrotropic activity in maintaining protein homeostasis within cells.

Main Methods:

Assessed the ability of ATP to prevent de novo protein aggregation under specific conditions.
Evaluated ATP's capacity to dissolve pre-formed protein aggregates.
Measured ATP concentrations in relation to its observed hydrotropic effects.

Main Results:

Adenosine triphosphate (ATP) demonstrated hydrotropic characteristics by preventing protein aggregate formation.
ATP was also effective in dissolving existing protein aggregates.
These hydrotropic effects were observed at physiological millimolar concentrations (5-10 mM) of ATP.

Conclusions:

Adenosine triphosphate (ATP) functions as a biological hydrotrope, in addition to its role as an energy source.
The hydrotropic properties of ATP at millimolar concentrations may contribute to maintaining protein solubility in cells.
This finding offers a potential explanation for the high intracellular concentrations of ATP.