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Related Concept Videos

The Supercomplexes in the Crista Membrane01:41

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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Enzymes02:34

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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.
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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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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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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.’
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Related Experiment Video

Updated: May 23, 2025

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Evidence supporting multienzyme complexes as metabolons: A review.

Hebah Al-Tamimi1, Aidil Abdul Hamid1, Mohamed Yusuf Mohamed Nazir2

  • 1Department on Biological Sciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600, UKM, Bangi, Selangor, Malaysia.

International Journal of Biological Macromolecules
|March 8, 2025
PubMed
Summary

This review explores fungal multienzyme complexes, focusing on their isolation and potential classification as metabolons. While substrate channeling is evident, dynamic assembly needs further investigation for a complete understanding.

Keywords:
BN-PAGECryo-EMFungiIsolationLC-MS/MSMetabolonMultienzyme complexPurification

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Area of Science:

  • Biochemistry
  • Mycology
  • Molecular Biology

Background:

  • Fungi possess intricate multienzyme systems vital for numerous biochemical pathways.
  • Multienzyme complexes play a critical role in cellular metabolic efficiency.
  • Understanding these complexes aids in deciphering fungal physiology and biotechnological applications.

Purpose of the Study:

  • To systematically review research on the isolation and identification of fungal multienzyme complexes.
  • To evaluate the criteria for classifying these complexes as metabolons.
  • To identify research gaps and suggest future directions in the field.

Main Methods:

  • Systematic literature review adhering to PRISMA guidelines.
  • Searches conducted in Medline, Web of Science, and ScienceDirect databases (2013-2023).
  • Qualitative analysis of 13 selected studies after initial screening of 2313 papers.

Main Results:

  • Diverse purification methods exist for fungal multienzyme complexes, each with specific advantages.
  • Isolation and characterization of these complexes present considerable challenges.
  • Evidence supports substrate channeling and the role of stabilizing proteins, but dynamic assembly remains less understood.

Conclusions:

  • Fungal multienzyme complexes are crucial but challenging to isolate and characterize.
  • Classification as metabolons requires meeting criteria of substrate channeling, functional coupling, and dynamic assembly.
  • Future research should focus on advanced isolation techniques, real-time dynamics monitoring, and elucidating molecular mechanisms.