Glutamate dehydrogenase modification

Chen, S.S., and Engel, PC. (1975) The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5 -phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity. Biochem. J. 147, 351-358. 

The same 2-BDB-TeA 2, 5 -DP was also found to inactivate the NADP -specific glutamate dehydrogenase from Salmonella typhimurium. The rate of inactivation exhibited a nonlinear dependence on the reagent concentration, indicative of reversible binding prior to irreversible modification (J9). The presence of NADPH or NADP in the reaction mixture completely prevented inactivation, suggesting that 2-BDB-TcA 2, 5 -DP also functioned as an affinity label of the coenzyme site in this NADP -specific dehydrogenase. 

Glutamate dehydrogenase After modification of 2 Trp-residues, the association between the subunits is strongly reduced, while activity is only slightly reduced the modification is followed also by MCD polyalkylation of the indole nucleus occurs 444)... 

WiTZEMANN, V., R. Koberstein, H. Sund, I. Rasched, H. Jornvall, and K. Noack Studies on Glutamate Dehydrogenase Chemical Modification and Quantitative Determination of Tryptophan Residues. Eur. J. Biochem. 43, 319-325 (1974). 

Johnson, A.R., and Dekker, E.E. (1996) Woodward s reagent K inactivation of Escherichia coli L-threo-nine dehydrogenase Increased absorbance at 340-350 nm is due to modification of cysteine and histidine residues, not aspartate or glutamate carboxyl groups. Protein Sci. 5, 382-390. 

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