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  • protein
  • Although several studies have attempted to characterize the enzyme kinetically, efforts have been thwarted by the apparent inactivation of the purified protein. (auburn.edu)
  • residues
  • The metal center of CDO is bound by a facial triad composed entirely of histidine residues in contrast to the previously ubiquitous 2-His/1-carboxylate facial triad found in other ferrous-dependent enzymes. (auburn.edu)
  • catalytic
  • The purpose of these studies is to probe the cause of inactivation of purified CDO and to determine how the 3-His facial triad and Cys-Tyr crosslink affect the catalytic properties of the enzyme. (auburn.edu)
  • Structural
  • Publication of the three-dimensional structure of several mammalian CDO enzymes revealed two unusual structural attributes that had previously not been identified in other mononuclear ferrous-dependent enzymes. (auburn.edu)
  • active
  • To determine which isoform represented the physiologically active enzyme, a two-fold approach was taken. (auburn.edu)
  • study
  • To study CDO containing the thioether linkage, a method was developed to isolate the enzyme in the homogenously crosslinked isoform. (auburn.edu)