1idf: Difference between revisions

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{{STRUCTURE_1idf|  PDB=1idf  |  SCENE=  }}  
{{STRUCTURE_1idf|  PDB=1idf  |  SCENE=  }}  


'''ISOCITRATE DEHYDROGENASE K230M MUTANT APO ENZYME'''
===ISOCITRATE DEHYDROGENASE K230M MUTANT APO ENZYME===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7761851}}


==About this Structure==
==About this Structure==
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[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
[[Category: Sweet, R M.]]
[[Category: Sweet, R M.]]
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