Alteration of the quaternary structure of glutamate dehydrogenase from Clostridium symbiosum by a single mutation distant from the subunit interfaces.
X-ray crystallographic studies have previously shown that glutamate dehydrogenase from Clostridium symbiosum is a homohexamer. Mutation of the active-site aspartate-165 to histidine causes an alteration in the structural properties of the enzyme. The mutant enzyme, D165H exists predominantly as a si...
Main Authors: | Dean, J, Cölfen, H, Harding, SE, Rice, D, Engel, P |
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Format: | Journal article |
Language: | English |
Published: |
1997
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