1-Amino-1,3-dicarboxycyclohexane (cycloglutamic acid). New glutamic acid analog and a substrate of glutamine synthetase

Biochemistry ◽  
1970 ◽  
Vol 9 (4) ◽  
pp. 842-846 ◽  
Author(s):  
Jerald D. Gass ◽  
Alton Meister
Keyword(s):  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Acid Analog

A Glutamic Acid Analog Bearing an Ethylenediamine Moiety Promotes the Cytosolic Delivery of TAT Peptides

2017 ◽  
Vol 46 (6) ◽  
pp. 889-891
Author(s):  
Tadashi Umemoto ◽  
Kotaro Sakamoto ◽  
Yasunori Fukuda ◽  
Yusuke Adachi ◽  
Akiyoshi Tani ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Cytosolic Delivery ◽  
Tat Peptides ◽  
Acid Analog

Differential effects of exogenous L-glutamine, L-glutamic acid, sodium glutamate, and casamino acids on glutamine synthetase and nitrate reductase in isolated pea roots cultured with or without sucrose

1981 ◽  
Vol 59 (7) ◽  
pp. 1121-1127 ◽  
Author(s):  
J. Sahulka ◽  
L. Lisá
Keyword(s):  
Nitrate Reductase ◽  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Sodium Salt ◽  
Sodium Glutamate ◽  
Negative Effect ◽  
Isolated Roots ◽  
Pea Roots ◽  
Casamino Acids ◽  
Glutamic Acid Sodium

Exogenous L-glutamine, the sodium salt of L-glutamic acid, and casamino acids do not decrease glutamine synthetase (GS) level in isolated pea (Pisum sativum L. cv. Jupiter and cv. Proteus) roots cultured with 20 g∙L−1 sucrose while L-glutamic acid does decrease it. The effect of L-glutamic acid is stronger in solutions lacking nitrate. By contrast, only the exogenous sodium salt of L-glutamic acid does not enhance the decrease in GS level caused by sugar starvation in isolated roots cultured without any sugar while, the other compounds tested do enhance this decrease. These facts confirm our earlier conclusion that sugar availability and the concentration of H+ ions are more important for GS level regulation in pea roots than nitrogen substrate availability and the presence of the end products. Nitrate reductase (NR) level is depressed by exogenous L-glutamine, the sodium salt of L-glutamic acid, casamino acids, and a low (0.2 mM) concentration of L-glutamic acid whereas it is increased by higher (0.8 and 1.0 mM) concentrations of L-glutamic acid, by α-ketoglutaric acid (0.4 to 0.6 mM), and by nitric acid (0.2 to 0.4 mM) added to saturating concentration (10 mM) of nitrate present in the form of potassium and calcium salts. The negative effect of L-glutamine, sodium glutamate, and casamino acids can be reversed by L-glutamic acid. This suggests that more mechanisms may be involved in NR regulation by these compounds and that the mechanism controlled by increased concentration of H+ ions is of great importance.

Inhibition of rat liver glutamine synthetase by phosphonic analogues of glutamic acid

1981 ◽  
Vol 37 (5) ◽  
pp. 461-462 ◽  
Author(s):  
B. Lejczak ◽  
H. Starzemska ◽  
P. Mastalerz
Keyword(s):  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Rat Liver

Kainic acid as conformationally constrained glutamic acid analog in peptide synthesis

1995 ◽  
Vol 36 (51) ◽  
pp. 9309-9312 ◽  
Author(s):  
Florinda Artuso ◽  
Giovanni Sindona ◽  
Constantinos Athanassopoulos ◽  
George Stavropoulos ◽  
Dionissios Papaioannou
Keyword(s):  
Glutamic Acid ◽  
Kainic Acid ◽  
Peptide Synthesis ◽  
Conformationally Constrained ◽  
Acid Analog

scholarly journals Design and Synthesis of a New Orthogonally Protected Glutamic Acid Analog and Its Use in the Preparation of High Affinity Polo-like Kinase 1 Polo-box Domain – binding Peptide Macrocycles

2021 ◽  
Author(s):  
David Hymel ◽  
Kohei Tsuji ◽  
Robert A. Grant ◽  
Ramesh M. Chingle ◽  
Dominique L. Kunciw ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Binding Peptide ◽  
Design And Synthesis ◽  
High Affinity ◽  
Acid Analog ◽  
Therapeutic Development

Targeting protein – protein interactions (PPIs) has emerged as important area of discovery for anticancer therapeutic development. In the case of phospho-dependent PPIs, such as the polo-like kinase 1 (Plk1)...

scholarly journals Some Properties of Glutamine Synthetase From the Nitrifying Bacterium Nitrosomonas Euro Paea

1981 ◽  
Vol 34 (6) ◽  
pp. 527 ◽  
Author(s):  
Basant Bhandari ◽  
DJD Nicholas
Keyword(s):  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Glutamate Dehydrogenase ◽  
Glutamate Synthase ◽  
Nitrosomonas Europaea ◽  
Main Route

Nitrosomonas europaea oxidizes ammonia to nitrite, thereby deriving energy for growth. Glutamate dehydrogenase (NADP+) (EC 1.4.1.4) is the main route for the incorporation of ammonia into glutamic acid, because glutamate synthase (NADPH) (EC 1.4.1.13) was not detected in cell-free extracts of N. europaea.

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