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作 者:Riad Nadi Eduardo Mateo-Bonmati Lucia Juan-Vicente Jose Luis Micol
机构地区:[1]Instituto de Bioingenieria, Universidad Miguel Hern&ndez, Campus de Elche, 03202 Elche, Spain
出 处:《Molecular Plant》2018年第10期1222-1224,共3页分子植物(英文版)
摘 要:The 2-oxoglutarate and Fe (ll)-dependent dioxygenase (2OGD) superfamily includes oxidative enzymes with an active site con- taining two histidines and (in most cases) one aspartic or glutamic acid residue. This conserved motif is termed the 2-His-1-carboxylate facial triad, chelates iron, and is housed within a double-stranded β-helix fold, also known as the DSBH, jelly-roll, cupin, or Jumonji C fold (Martinez and Hausinger, 2015). The reactions catalyzed by 2OGDs (also called 2ODDs, 2ODQs, and 2OGXs) include but are not limited to demethylation, demethylenation, hydroxytation, halogenation, desaturation, ring cleavage, ring closure, and epimerization (Farrow and Facchini, 2014).The 2-oxoglutarate and Fe (ll)-dependent dioxygenase (2OGD) superfamily includes oxidative enzymes with an active site con- taining two histidines and (in most cases) one aspartic or glutamic acid residue. This conserved motif is termed the 2-His-1-carboxylate facial triad, chelates iron, and is housed within a double-stranded β-helix fold, also known as the DSBH, jelly-roll, cupin, or Jumonji C fold (Martinez and Hausinger, 2015). The reactions catalyzed by 2OGDs (also called 2ODDs, 2ODQs, and 2OGXs) include but are not limited to demethylation, demethylenation, hydroxytation, halogenation, desaturation, ring cleavage, ring closure, and epimerization (Farrow and Facchini, 2014).
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