Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases

FEBS J. 2012 May;279(9):1563-75. doi: 10.1111/j.1742-4658.2012.08496.x. Epub 2012 Feb 20.

Abstract

Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase).

Publication types

  • Review

MeSH terms

  • Amino Acid Oxidoreductases / metabolism*
  • Ferrous Compounds / metabolism
  • Hydroxylation
  • Ketoglutaric Acids / metabolism*
  • Mixed Function Oxygenases / metabolism
  • Models, Molecular
  • Oxidation-Reduction
  • Oxygenases / metabolism*
  • Repressor Proteins / metabolism

Substances

  • Ferrous Compounds
  • Ketoglutaric Acids
  • Repressor Proteins
  • Mixed Function Oxygenases
  • Oxygenases
  • 2,4-dichlorophenoxyacetate-alpha-ketoglutarate dioxygenase
  • HIF1AN protein, human
  • Amino Acid Oxidoreductases
  • 1-aminocyclopropane-1-carboxylic acid oxidase