Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli
Author: Weaver, T.; Banaszak, L. Description: Fumarase C catalyzes the stereospecific interconversion of fumarate to l-malate as part of the metabolic citric acid or Kreb’s cycle. The recent three-dimensional structure of fumarase C from Escherichia coli has identified a binding site for anions which is generated by side chains from three of the four subunits within the tetramer. These same side chains are found in the three most highly conserved regions within the class II fumarase superfamily. The site was initially characterized by crystallographic studies through the binding of a…
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