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Related Concept Videos

Enzymes02:34

Enzymes

96.2K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

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Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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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Introduction to Enzymes01:22

Introduction to Enzymes

33.7K
The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Nanosensors to Detect Protease Activity In Vivo for Noninvasive Diagnostics
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Enzymes as Sensors.

Maria Staiano1, Angela Pennacchio1, Antonio Varriale1

  • 1Institute of Food Science, CNR, Avellino, Italy.

Methods in Enzymology
|March 25, 2017
PubMed
Summary
This summary is machine-generated.

Advancements in biosensor technology, utilizing biomolecules like enzymes, offer sensitive and specific detection for diverse applications. Fluorescence spectroscopy is key for monitoring these biological interactions and biosensor responses.

Keywords:
BiosensorEnzymeFluorescenceProteinSensor

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Area of Science:

  • Biotechnology
  • Analytical Chemistry
  • Materials Science

Background:

  • Recent technological, material, and nanotechnology advancements have driven innovations in biological sensing devices.
  • Biosensors integrate biological recognition elements (proteins, enzymes, antibodies, aptamers) with signal transduction for target molecule detection.
  • Key advantages include specificity, low cost, rapidity, sensitivity, and multiplicity, driving commercial success.

Purpose of the Study:

  • To review innovations in biological sensing devices and their applications.
  • To highlight the role of biomolecules, particularly enzymes, as recognition elements in biosensors.
  • To emphasize the benefits of customized biosensor designs using enzyme forms and thermophile sources.

Main Methods:

  • Utilizing biomolecules like enzymes, antibodies, and aptamers for selective target molecule recognition.
  • Employing fluorescence spectroscopy to monitor biomolecular interactions and biosensor responses due to its high sensitivity.
  • Investigating both intrinsic protein fluorescence and extrinsic fluorescent labels for signal transduction.

Main Results:

  • Biomolecules exhibit high selectivity and specificity in binding target molecules, leading to detectable changes in their structure.
  • Fluorescence spectroscopy effectively monitors these interactions, correlating structural changes to biosensor output.
  • Enzymes are highlighted as superior recognition elements, with customized apo- or holo-enzyme forms offering enhanced potential.

Conclusions:

  • Biosensors represent a significant technological advancement with broad applications in health, environment, and industry.
  • Enzyme-based biosensors, especially those utilizing customized or thermophilic forms, offer promising avenues for sensitive and specific analyte detection.
  • The integration of advanced materials and fluorescence techniques continues to enhance biosensor performance and expand their utility.