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Clostridial glutamate dehydrogenase mutants with the 5 Trp residues in turn replaced by Phe showed the importance of Trp 64 and 449 in cooperativity with glutamate at pH 9. These mutants are examined here for their behaviour with NAD + at pH 7.0 and 9.0. The wild-type enzyme displays negative NAD + cooperativity at both pH values. At pH 7.0 W243F gives Michaelis–Menten kinetics, and...
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