Identification of amino acids modified by the bifunctional affinity label 5'-(p-(fluorosulfonyl)benzoyl)-8-azidoadenosine in the reduced coenzyme regulatory site of bovine liver glutamate dehydrogenase

Biochemistry ◽  
1992 ◽  
Vol 31 (15) ◽  
pp. 3785-3793 ◽  
Author(s):  
Kenneth E. Dombrowski ◽  
Yu Chu Huang ◽  
Roberta F. Colman
Keyword(s):  
Amino Acids ◽  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Regulatory Site ◽  
Affinity Label

Affinity labeling of a regulatory site of bovine liver glutamate dehydrogenase

Biochemistry ◽  
1975 ◽  
Vol 14 (4) ◽  
pp. 707-715 ◽  
Author(s):  
Pranab K. Pal ◽  
William J. Wechter ◽  
Roberta F. Colman
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Affinity Labeling ◽  
Regulatory Site

scholarly journals Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits

1984 ◽  
Vol 222 (3) ◽  
pp. 621-626 ◽  
Author(s):  
S E H Syed ◽  
P C Engel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chemical Modification ◽  
Glutamate Dehydrogenase ◽  
Activity Ratio ◽  
Regulatory Site ◽  
Constant Ratio ◽  
Active Centre ◽  
Catalytic Sites ◽  
The Relationship

The effect of pyridoxal 5′-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5′-phosphate. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5′-phosphate, indicating that glutamate activity is lost more rapidly than alanine activity. A mixture of NADH, GTP and 2-oxoglutarate completely protected the alanine and glutamate activities against inactivation by pyridoxal 5′-phosphate. The activity of glutamate dehydrogenase towards glutamate and leucine decreased steadily in a constant ratio in the presence of pyridoxal 5′-phosphate. The effect of leucine on the alanine and glutamate activities as a function of inactivation by pyridoxal 5′-phosphate was studied. The results are interpreted to suggest that the subunits of glutamate dehydrogenase hexamer are kinetically non-equivalent with regard to activity towards the two monocarboxylic amino acids as well as glutamate, and that all three substrates share the same active centre. However, leucine is also able to bind at a separate regulatory site.

scholarly journals Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase.

1981 ◽  
Vol 256 (22) ◽  
pp. 11866-11872
Author(s):  
K.V. Saradambal ◽  
R.A. Bednar ◽  
R.F. Colman
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Inhibitory Site

scholarly journals Sequence of Bovine Liver Glutamate Dehydrogenase

1971 ◽  
Vol 246 (8) ◽  
pp. 2374-2399 ◽  
Author(s):  
Michael Landon ◽  
Dennis Piszkiewicz ◽  
Emil L. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver

scholarly journals Sequence of Bovine Liver Glutamate Dehydrogenase

1973 ◽  
Vol 248 (9) ◽  
pp. 3067-3081 ◽  
Author(s):  
Dennis Piszkiewicz ◽  
Michael Landon ◽  
Emil L. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver

scholarly journals Sequence of Bovine Liver Glutamate Dehydrogenase

1971 ◽  
Vol 246 (8) ◽  
pp. 2400-2418 ◽  
Author(s):  
William J. Brattin ◽  
Emil L. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver

scholarly journals Glutamate dehydrogenase: Structure of a hyperinsulinism mutant, corrections to the atomic model, and insights into a regulatory site

2018 ◽  
Vol 87 (1) ◽  
pp. 41-50 ◽  
Author(s):  
Omneya M. Nassar ◽  
Changhong Li ◽  
Charles A. Stanley ◽  
B. Montgomery Pettitt ◽  
Thomas J. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Atomic Model ◽  
Regulatory Site
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