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Related Concept Videos

Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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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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Cofactors and Coenzymes01:24

Cofactors and Coenzymes

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
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Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Shared function and moonlighting proteins in molybdenum cofactor biosynthesis.

Silke Leimkühler1

  • 1.

Biological Chemistry
|March 12, 2017
PubMed
Summary

Molybdenum cofactor (Moco) biosynthesis is conserved across life. Proteins involved in Moco synthesis also participate in iron-sulfur cluster assembly and tRNA modification, revealing shared cellular pathways and novel protein functions.

Keywords:
FeS clustermolybdenum cofactormolybdoenzymesmoonlightingsulfur transfertRNA thiolation

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Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples
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Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples
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Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Molybdenum cofactor (Moco) is essential for numerous enzymes across bacteria, archaea, and eukaryotes.
  • Moco biosynthesis involves forming a pyranopterin cofactor, followed by molybdenum insertion.
  • Bacterial and archaeal Moco biosynthesis includes an additional nucleotide modification step.

Purpose of the Study:

  • To review Moco biosynthesis pathways in bacteria and humans.
  • To highlight conserved proteins and their roles in Moco synthesis.
  • To explore the connections between Moco biosynthesis and other cellular pathways, including shared protein components and moonlighting functions.

Main Methods:

  • Literature review of conserved Moco biosynthesis pathways.
  • Analysis of protein homology and shared functions across different cellular processes.
  • Identification of moonlighting roles for proteins involved in Moco biosynthesis.

Main Results:

  • Moco biosynthesis proteins are highly conserved across diverse phyla.
  • Key Moco biosynthesis proteins are shared with iron-sulfur cluster assembly and tRNA thio-modification pathways.
  • Proteins involved in Moco biosynthesis exhibit moonlighting activities in other cellular contexts.

Conclusions:

  • Moco biosynthesis is intricately linked to other fundamental cellular processes through shared protein machinery.
  • The discovery of shared functions and moonlighting roles provides new insights into cellular network organization and protein versatility.
  • Understanding these connections is crucial for comprehending cellular metabolism and developing targeted therapeutic strategies.