Dehydrogenases glutamate dehydrogenase

Inhibits alcohol dehydrogenase, glutamate dehydrogenase, glutamic dehydrogenase, Upid peroxidation, malate ddiydrogenase, oxidative phosphorylation, thyroid transaminase. 

CS causes alkylation of sulfhydryl-containing enzymes and inhibits lactic dehydrogenase, glutamic dehydrogenase, pyruvic decarboxy-. lase, and alpha-glycerophosphate dehydrogenase.24,40 it reacts with a number of nucleophilic compounds, such as glutathione, plasma protein, and lipoic acid.24... 

Zn Carbonic anhydrase. carboxypeptidase. alcohol dehydrogenase, glutamic dehydrogenase, acylase ... 

For glyceraldehyde-3-phosphate dehydrogenase, glutamate dehydrogenase, and the NADP-linked oxidative decarboxylases, which have three substrates in one direction, initial rate measurements with a fixed concentration of any one of the three substrates also conform to Eq. (1). This again rules out any form of enzyme-substitution mechanism in which free product is formed before all the substrates have combined with the enzyme and indicates the involvement of a quaternary enzyme complex. The appropriate generalized form of Eq. (1) is... 

Aspartate aminotransferase Gamma glutamyl transferase Omidiine carbamoyl transferase Omidiine decarboxylase s Sorbitol dehydrogenase Glutamate dehydrogenase ... 

Of the various dehydrogenases, glutamate dehydrogenase (GLDH) can be a good indicator for mitochondrial damage in juvenile rats. However, this measurement has less value in older rats, where there is greater inter- and intra-individual variability (O Brien et al. 2002). 

Fig. 2. Reaction of 3 -p-fluorosulfonylbenzoyladenosine with bovine liver glutamate dehydrogenase. Glutamate dehydrogenase (021 mg/ml) was incubated with 3 -FSBA (0.496 mil/) at 24° in 0.01 M sodium barbital buffer (pH 8) containing 0.43 M KCl and 5% ethanol. At each indicated time, an aliquot was withdrawn, diluted 20-fold with Tris-0.1 M acetate buffer (pH 8) at 0°, and assayed (A) in the absence and (B) in the presence of 100 yM ADP. Inset Determination of the pseudo first-order rate constant from the decrease in activation by ADP. (Ft and Fo are the enzymic velocities measured in the presence of ADP and the given and zero time, respectively, and F > is the constant velocity at the end of the reaction. The pseudo first-order rate constant calculated is 0D351 min. ) Data are taken from P. K. Pal, W. J. Wechter, and R. F. Colman, Biochemistry 14, 707 (1975).

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