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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.

Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.[1]

References

  1. Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Bolduc, J.M., Dyer, D.H., Scott, W.G., Singer, P., Sweet, R.M., Koshland, D.E., Stoddard, B.L. Science (1995) [Pubmed]
 
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