Emerging of lysine demethylases (KDMs): From pathophysiological insights to novel therapeutic opportunities

Biomed Pharmacother. 2020 Sep:129:110392. doi: 10.1016/j.biopha.2020.110392. Epub 2020 Jun 20.

Abstract

In recent years, there have been remarkable scientific advancements in the understanding of lysine demethylases (KDMs) because of their demethylation of diverse substrates, including nucleic acids and proteins. Novel structural architectures, physiological roles in the gene expression regulation, and ability to modify protein functions made KDMs the topic of interest in biomedical research. These structural diversities allow them to exert their function either alone or in complex with numerous other bio-macromolecules. Impressive number of studies have demonstrated that KDMs are localized dynamically across the cellular and tissue microenvironment. Their dysregulation is often associated with human diseases, such as cancer, immune disorders, neurological disorders, and developmental abnormalities. Advancements in the knowledge of the underlying biochemistry and disease associations have led to the development of a series of modulators and technical compounds. Given the distinct biophysical and biochemical properties of KDMs, in this review we have focused on advances related to the structure, function, disease association, and therapeutic targeting of KDMs highlighting improvements in both the specificity and efficacy of KDM modulation.

Keywords: 2-Oxoglutaric acid; Amino oxidase; Biological functions; Demethylase; Diseases; Lysine; Small-molecule; Structures; Targeting; Therapeutics.

Publication types

  • Review

MeSH terms

  • Animals
  • Cellular Microenvironment
  • DNA Demethylation
  • Enzyme Inhibitors / therapeutic use
  • Histone Demethylases / antagonists & inhibitors
  • Histone Demethylases / chemistry
  • Histone Demethylases / metabolism*
  • Histones / metabolism*
  • Humans
  • Molecular Targeted Therapy
  • Protein Domains
  • Protein Processing, Post-Translational
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Histones
  • Histone Demethylases