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

Identification of histidyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5′-monophosphate in an ADP regulatory site of glutamate dehydrogenase

1989 ◽  
Vol 270 (1) ◽  
pp. 277-285 ◽  
Author(s):  
Surendra P. Batra ◽  
Richard H. Lark ◽  
Roberta F. Colman
Keyword(s):  
Glutamate Dehydrogenase ◽  
Regulatory Site

Identification of Adenine Binding Domain Peptides of the ADP Regulatory Site within Glutamate Dehydrogenase†

1996 ◽  
Vol 7 (3) ◽  
pp. 302-310 ◽  
Author(s):  
Michael T. Shoemaker ◽  
Boyd E. Haley
Keyword(s):  
Glutamate Dehydrogenase ◽  
Binding Domain ◽  
Regulatory Site

Modification of the ADP regulatory site of glutamate dehydrogenase by PLP-AMP

1988 ◽  
Vol 16 (5) ◽  
pp. 861-862
Author(s):  
ELLIS BELL
Keyword(s):  
Glutamate Dehydrogenase ◽  
Regulatory Site

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

Cassette Mutagenesis and Photoaffinity Labeling of Adenine Binding Domain of ADP Regulatory Site within Human Glutamate Dehydrogenase†

Biochemistry ◽  
2002 ◽  
Vol 41 (21) ◽  
pp. 6817-6823 ◽  
Author(s):  
Hye-Young Yoon ◽  
Eun-Young Lee ◽  
Sung-Woo Cho
Keyword(s):  
Glutamate Dehydrogenase ◽  
Photoaffinity Labeling ◽  
Binding Domain ◽  
Regulatory Site

scholarly journals Allosteric discrimination at the NADH/ADP regulatory site of glutamate dehydrogenase

2019 ◽  
Vol 28 (12) ◽  
pp. 2080-2088 ◽  
Author(s):  
Omneya M. Nassar ◽  
Ka‐Yiu Wong ◽  
Gillian C. Lynch ◽  
Thomas J. Smith ◽  
B. Montgomery Pettitt
Keyword(s):  
Glutamate Dehydrogenase ◽  
Regulatory Site

Activation of Bovine Liver Glutamate Dehydrogenase by Covalent Reaction of Adenosine 5'-O-[S-(4-Bromo-2,3-dioxobutyl)thiophosphate] with Arginine-459 at an ADP Regulatory Site

Biochemistry ◽  
1994 ◽  
Vol 33 (38) ◽  
pp. 11544-11553 ◽  
Author(s):  
Kazimierz O. Wrzeszczynski ◽  
Roberta F. Colman
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
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.

Properties of glutamate dehydrogenase from developing maize endosperm

1990 ◽  
Vol 80 (2) ◽  
pp. 238-242 ◽  
Author(s):  
Vesna Hadzi-TaskovicSukalovic
Keyword(s):  
Glutamate Dehydrogenase ◽  
Maize Endosperm
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