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Related Concept Videos

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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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...
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ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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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...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

16.8K
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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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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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...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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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...
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Related Experiment Video

Updated: Mar 14, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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Decoding P4-ATPase substrate interactions.

Bartholomew P Roland1, Todd R Graham1

  • 1a Department of Biological Sciences , Vanderbilt University , 1161 21st Ave South , Nashville , TN , USA.

Critical Reviews in Biochemistry and Molecular Biology
|October 5, 2016
PubMed
Summary
This summary is machine-generated.

Phospholipid flippases (P4-ATPases) maintain cell membrane asymmetry by controlling lipid distribution. Understanding their substrate specificity is key to unlocking their roles in membrane organization and cell signaling.

Keywords:
P4-ATPasemembrane asymmetrymembrane biologyphospholipid flippasephospholipid transportprotein engineering

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Area of Science:

  • Cellular biology
  • Biochemistry
  • Membrane biophysics

Background:

  • Cellular membranes rely on specific lipid and protein compositions for function.
  • Phospholipid (PL) asymmetry across the plasma membrane is crucial for membrane bending and signal transduction.
  • P4-ATPases are essential for establishing and maintaining this PL gradient.

Purpose of the Study:

  • To review the role of P4-ATPases in membrane biology.
  • To present current understanding of P4-ATPase substrate specificity.
  • To discuss how P4-ATPase enzymology can advance cell membrane studies.

Main Methods:

  • Review of existing literature on P4-ATPases.
  • Analysis of P4-ATPase substrate specificity mechanisms.
  • Discussion of potential for mutationally tuning P4-ATPase specificity.

Main Results:

  • P4-ATPases are key transporters regulating phospholipid asymmetry.
  • Substrate specificity of P4-ATPases dictates membrane organization.
  • Understanding these mechanisms offers avenues for experimental manipulation.

Conclusions:

  • P4-ATPase substrate specificity is fundamental to membrane organization and cell biology.
  • Decoding P4-ATPase structure-function relationships can reveal insights into membrane dynamics.
  • Targeted studies of P4-ATPases can enhance understanding of cellular membrane functions.