title: Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.
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).
authors.affiliation: Department of Chemistry and the Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford, UK.
authors.forename: Monica
authors.initials: M
authors.lastname: Mantri
authors.forename: Zhihong
authors.initials: Z
authors.lastname: Zhang
authors.forename: Michael A
authors.initials: MA
authors.lastname: McDonough
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D005296:Ferrous Compounds / Q000378:metabolism; D006900:Hydroxylation; D007656:Ketoglutaric Acids / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism
chemical_list: D005296:Ferrous Compounds; D007656:Ketoglutaric Acids; D012097:Repressor Proteins; D006899:Mixed Function Oxygenases; D010105:Oxygenases; C084087:2,4-dichlorophenoxyacetate-alpha-ketoglutarate dioxygenase; C439790:HIF1AN protein, human; D000594:Amino Acid Oxidoreductases; C059460:1-aminocyclopropane-1-carboxylic acid oxidase