Metalloenzymes are the metals which can affect function directly by involving participation in the catalysis which appear to have ligand active sites which can be differentiated from those of metals which alters the function indirectly through its modulation of protein structure. Thus, E. coli alkaline phosphatase and as well as equine liver alcohol dehydrogenase, metals placed at the active site interact selectively with chelating agents, and undergo isotope exchange, and display its distinctive physical chemical characteristics. Such active site metals which may have an irregular geometry, and which facilitates their catalytic role. In contrast to the nonactive site metals shows physical properties similar to those of simple, bidentate model complexes; they frequently appear to stabilize structure subunit interactions as shown by their other effects on sedimentation or hydrogen exchange rates of proteins. Such structural metals may function importantly in control mechanisms for biochemical reactions.

  • Recombinant protein expression
  • Biomimetic aspects
  • Protein domains
  • Signal transduction
  • Labile coordination site

Related Conference of Metalloenzymes

Metalloenzymes Conference Speakers