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Related Concept Videos

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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ATP Driven Pumps II: P-type Pumps01:34

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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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Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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The Citric Acid Cycle: Output01:28

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The citric acid cycle is termed an amphibolic pathway as it operates both anabolically and catabolically. The cyclic reactions balance the flux of the substrates to provide an optimal concentration of NADH and ATP to the cell.
Regulation of Citric Acid Cycle
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Allosteric Proteins-ATCase01:19

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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.
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Recycling Endosomes and Transcytosis00:58

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
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Related Experiment Video

Updated: May 30, 2025

Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors
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Building Localized NADP(H) Recycling Circuits to Advance Enzyme Cascadetronics.

Ryan A Herold1,2, Christopher J Schofield1,3, Fraser A Armstrong1

  • 1Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3QY, United Kingdom.

Angewandte Chemie (International Ed. in English)
|January 29, 2025
PubMed
Summary
This summary is machine-generated.

Enzymes in mesoporous electrodes use electrochemical cofactor recycling for controlled multi-step reactions. This method enables complex metabolic pathway analysis under ambient conditions, mimicking electronic circuits.

Keywords:
BiocatalysisCofactor RecyclingEnzyme CascadeHydrogen BorrowingNanoconfinement

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

  • Bioelectrochemistry
  • Enzyme catalysis
  • Nanomaterials

Background:

  • Enzyme cascades are crucial for metabolic processes.
  • Controlling enzyme activity electrochemically offers precise reaction management.
  • Nicotinamide cofactors (NAD(P)H) are vital electron carriers in biological redox reactions.

Purpose of the Study:

  • To demonstrate simultaneous electrochemical control and observation of enzyme cascades.
  • To utilize reversible electrochemical nicotinamide cofactor recycling for energy and control.
  • To showcase the ability to perform reactions under opposing conditions using hydrogen-borrowing enzymes.

Main Methods:

  • Confining enzyme cascades within mesoporous electrode materials.
  • Employing electrochemical nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) regeneration.
  • Incorporating a hydrogen-borrowing enzyme pair to oppose external voltage bias.
  • Utilizing a four-enzyme cascade including urease for pathway demonstration.

Main Results:

  • Efficient, reversible electrochemical NAD(P)(H) recycling was achieved.
  • Multi-step reactions were mediated in either direction with rapid response.
  • A reduction process was performed under overall oxidizing conditions, and vice versa.
  • Complex metabolic pathways were controlled and resolved, with real-time observation of urease activity under oxidizing potential.

Conclusions:

  • Confined enzyme cascades within electrodes can be energized and controlled electrochemically.
  • This system allows for the study of anaerobic enzymatic reactions under aerobic conditions.
  • The approach mimics electronic circuits, offering a powerful tool for bioelectrocatalysis and metabolic engineering.