4.6 Review

Enzymatic lysine oxidation as a posttranslational modification

Journal

FEBS JOURNAL
Volume 289, Issue 24, Pages 8020-8031

Publisher

WILEY
DOI: 10.1111/febs.16205

Keywords

histones; LOX; LOXL; lysine; oxidation; posttranslational modifications; transcription factor

Funding

  1. Instituto de Salud Carlos III (ISCIII) FIS/FEDER [PI12/01250, CP08/00223, PI16/00253, CB16/12/00449]
  2. MINECO
  3. La Caixa Foundation [LCF/PR/PR12/51070001]
  4. FERO Foundation
  5. [FPU14/04071]

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Oxidoreductases catalyze oxidation-reduction reactions and constitute a large and diverse group of enzymes. Carbonylation, particularly in lysine residues, is a significant oxidative modification in proteins that can impact protein structure and function.
Oxidoreductases catalyze oxidation-reduction reactions and comprise a very large and diverse group of enzymes, which can be subclassified depending on the catalytic mechanisms of the enzymes. One of the most prominent oxidative modifications in proteins is carbonylation, which involves the formation of aldehyde and keto groups in the side chain of lysines. This modification can alter the local macromolecular structure of proteins, thereby regulating their function, stability, and/or localization, as well as the nature of any protein-protein and/or protein-nucleic acid interactions. In this review, we focus on copper-dependent amine oxidases, which catalyze oxidative deamination of amines to aldehydes. In particular, we discuss oxidation reactions that involve lysine residues and that are regulated by members of the lysyl oxidase (LOX) family of proteins. We summarize what is known about the newly identified substrates and how this posttranslational modification regulates protein function in different contexts.

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