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One of a series of papers in which we tested subunit interaction in this hexameric, allosteric enzyme by making defined hybrids in which one active subunit was partnered by 5 inactive subunits. In this case the 'dead' subunits were still competent for binding of substrates but disabled for catalysis.

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This page is a summary of: Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalytically inert D165S, European Journal of Biochemistry, March 2001, Wiley,
DOI: 10.1046/j.1432-1327.2001.01949.x.
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