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Related Concept Videos

Enzymes02:34

Enzymes

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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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Enzyme Kinetics01:19

Enzyme Kinetics

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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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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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Enzyme Inhibition01:30

Enzyme Inhibition

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Introduction to Enzymes01:22

Introduction to Enzymes

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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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Restriction Enzymes01:11

Restriction Enzymes

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
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Related Experiment Video

Updated: Jan 30, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

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Enzyme-Enzyme Interactions in Monolignol Biosynthesis.

Jack P Wang1,2, Baoguang Liu2,3, Yi Sun2

  • 1Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC, United States.

Frontiers in Plant Science
|January 30, 2019
PubMed
Summary
This summary is machine-generated.

Enzyme interactions in the monolignol biosynthetic pathway are crucial for lignin formation in wood. New studies reveal protein complex formation and regulatory roles impacting plant stress responses.

Keywords:
BiFCco-immunoprecipitationenzyme kineticsligninmonolignol biosynthesisprotein-protein interaction

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Area of Science:

  • Biochemistry
  • Plant Biology
  • Molecular Biology

Background:

  • The monolignol biosynthetic pathway is key to lignin production, essential for wood formation.
  • Previous understanding often viewed this pathway as linear or a simple metabolic grid.
  • Enzymatic interactions within the pathway were poorly understood and fragmented.

Purpose of the Study:

  • To comprehensively investigate enzyme interactions within the monolignol biosynthetic pathway in a single plant species.
  • To explore the functional and regulatory significance of these interactions.
  • To examine the role of enzyme interactions in metabolic channeling and stress responses.

Main Methods:

  • Utilized Populus trichocarpa for extensive genomic, biochemical, chemical, and cellular experiments.
  • Employed techniques including enzyme activity assays, co-immunoprecipitation, chemical crosslinking, bimolecular fluorescence complementation, and yeast 2-hybrid screening.
  • Incorporated cell type-specific gene expression analysis via laser capture microdissection.

Main Results:

  • Demonstrated that enzyme interactions significantly affect the rate, direction, and specificity of hydroxylation steps.
  • Identified heterodimeric and heterotetrameric protein complexes formed by monolignol P450 mono-oxygenases.
  • Revealed regulatory interactions involving 4-coumarate CoA ligases and interactions between cinnamyl alcohol dehydrogenase and cinnamoyl-CoA reductase.

Conclusions:

  • Enzyme complex formation is integral to the monolignol biosynthetic pathway's function.
  • These interactions play critical roles in regulating lignin biosynthesis and potentially in plant stress adaptation.
  • Findings provide new insights into metabolic channeling and enzyme regulation in plants.