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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, FEBS Journal, March 2001, Wiley,
DOI: 10.1046/j.1432-1327.2001.01949.x.
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