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  • substrates
  • Further classification into mono- and dioxygenases in based on whether the enzyme causes transfer of just one atom to the substrate (S) (eq. 1) or whether the whole molecule is incorporated into a single substrate (eq. 2a) or is shared by a pair of substrates (S, S′) (eq. 2b) ( 1, 2 ) 1 . (springer.com)
  • enzyme
  • the 1,2-CTD enzyme produced by Pseudomonas arvilla is the exception to this rule, containing two highly homologous subunits that can form either a homo- or hetero- dimer. (wikipedia.org)
  • iron
  • Most mononculear iron dioxygenases are members of the cupin superfamily in which the overall domain structure is described as a six-stranded β-barrel fold (or jelly roll motif). (wikipedia.org)
  • At the center this barrel structure is a metal ion, most commonly ferrous iron, whose coordination environment is frequently provided by residues in two partially conserved structural motifs: G(X)5HXH(X)3-4E(X)6G and G(X)5-7PXG(X)2H(X)3N. (wikipedia.org)
  • Extradiol members utilize ferrous iron as the active redox state, and this center is commonly coordinated octahedrally through a 2-His-1-Glu motif with labile water ligands occupying empty positions. (wikipedia.org)
  • Dioxygenase Model Studies: Reactionof Oxygen with Iron Catecholates", Lauffer, R. B. (umn.edu)
  • structure
  • Therefore, 1,2-CTD may bind to the cell lipid membrane via its terminal phospholipids and thus have greater access to the phenolic hydrocarbons vital in lipid membrane structure. (wikipedia.org)
  • Structure and Function of Dioxygenases. (umn.edu)
  • Structure of Nitrilotriacetato.3,5-di-tert-butylcatecholato. (umn.edu)
  • active site
  • Oxygen is bonded to the substrate through a series of trans influences and stabilizing hydrogen bonding between the substrate and other active site amino acid residues. (wikipedia.org)