Substrate Specificity via Ternary Complex Formation with Glutamate Dehydrogenase
- 1 September 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 79 (1) , 85-92
- https://doi.org/10.1111/j.1432-1033.1977.tb11786.x
Abstract
Very little discrimination is observed in the binary binding of dicarboxylic acid substrate analogs to [bovine liver] glutamate dehydrogenase as monitored by PNMR. Variation in length, charge, bulkiness and conformational rigidity resulted in only a factor of 5 variation in Kd and apparent relaxation time, T2. Upon titration of the binary enzyme-ligand complex with coenzyme to form the ternary enzyme-ligand-coenzyme complex strong discrimination is observed. Coenzyme binds tightly only when the correct substrate is present, otherwise it binds 10-150 times more weakly.This publication has 17 references indexed in Scilit:
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