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Enzyme Biosynthesis: Comparison
Please note this is a comparison between Version 2 by Yu Peng and Version 1 by Yu Peng.

Enzyme biosynthesis is the cellular production and maturation of enzyme molecules. Protein-enzyme synthesis begins with translation of an encoding messenger RNA, followed by formation of the molecular features needed for catalysis. For iron–sulfur enzymes, specialized machinery assembles the cluster on a scaffold before transfer to the protein [1][2]. Cofactor insertion and protein maturation are coordinated processes involving multiple accessory components [3]. Enzymes entering the secretory pathway undergo folding, assembly, and modifications in the endoplasmic reticulum, including disulfide-bond formation or glycosylation where appropriate [4]. Organellar enzymes can also undergo proteolytic removal of targeting sequences or other maturation segments after transport [5]. These reactions convert the newly synthesized polypeptide into its functional molecular form and establish the catalytic groups, subunit contacts, and cellular location required for activity [2].

  • enzyme production
  • translation
  • protein maturation
  • cofactor assembly

Enzyme Production and Characterization·Biotechnology·Biochemistry, Genetics and Molecular Biology·Life Sciences

References

  1. Deborah C. Johnson; Dennis R. Dean; Archer D. Smith; Michael K. Johnson; Structure Function, and Formation of Biological Iron-sulfur Clusters. Annu. Rev. Biochem. 2005, 74, 247-281. [CrossRef]
  2. Alfred M. Lentzsch; Jae Ho Lee; Shu-Ou Shan; Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome. J. Mol. Biol. 2025, 437, 169056. [CrossRef]
  3. Roland Lill; Function and Biogenesis of Iron–sulphur Proteins. Nature 2009, 460, 831-838. [CrossRef]
  4. Ineke Braakman; Neil J. Bulleid; Protein Folding and Modification in the Mammalian Endoplasmic Reticulum. Annu. Rev. Biochem. 2011, 80, 71-99. [CrossRef]
  5. Klaas J. van Wijk; Protein Maturation and Proteolysis in Plant Plastids, Mitochondria, and Peroxisomes. Annu. Rev. Plant Biol. 2015, 66, 75-111. [CrossRef]
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