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Desaturases: emerging models for understanding functional diversification of diiron-containing enzymes Shanklin J; Guy JE; Mishra G; Lindqvist YJ Biol Chem 2009[Jul]; 284 (28): 18559-63Desaturases and related enzymes perform O(2)-dependent dehydrogenations initiated at unactivated C-H groups with the use of a diiron active site. Determination of the long-sought oxidized desaturase crystal structure facilitated structural comparison of the active sites of disparate diiron enzymes. Experiments on the castor desaturase are discussed that provide experimental support for a hypothesized ancestral oxidase enzyme in the context of the evolution of the diiron enzyme diverse functionality. We also summarize recent analysis of a castor mutant desaturase that provides valuable insights into the relationship of proposed substrate-binding modes with respect to a range of catalytic outcomes.|Animals[MESH]|Binding Sites[MESH]|Biochemistry/methods[MESH]|Catalysis[MESH]|Catalytic Domain[MESH]|Cell Membrane/metabolism[MESH]|Enzymes/chemistry[MESH]|Fatty Acids/chemistry[MESH]|Humans[MESH]|Iron/*chemistry[MESH]|Models, Biological[MESH]|Molecular Conformation[MESH]|Mutation[MESH]|Stearoyl-CoA Desaturase/*chemistry/physiology[MESH]|Substrate Specificity[MESH] |
