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

THE ACTIVATION OF GLUTAMIC ACID AND GLUTAMINE IN MAMMALIAN TISSUES

1963 ◽  
Vol 41 (5) ◽  
pp. 1135-1145 ◽  
Author(s):  
M. A. Alford ◽  
M. Brotman ◽  
M. A. Chudy ◽  
M. J. Fraser
Keyword(s):  
Amino Acid ◽  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Specific Enzyme ◽  
Ehrlich Ascites ◽  
Mammalian Tissues ◽  
Made In

Measurements of α-glutamyl-RNA synthetase and glutaminyl-RNA synthetase activities have been made in fractions derived from 105,000 × g supernatants of homogenates of rat liver and of mouse Ehrlich ascites carcinoma cells. Evidence is presented which indicates that each amino acid is activated by a specific enzyme. Both enzymes catalyze amino acid dependent ATP-32PP exchange. The α-glutamyl-RNA synthetase purified 42-fold from rat liver 105,000 × g supernatant is free of glutamine synthetase.

THE ACTIVATION OF GLUTAMIC ACID AND GLUTAMINE IN MAMMALIAN TISSUES

1963 ◽  
Vol 41 (1) ◽  
pp. 1135-1145 ◽  
Author(s):  
M. A. Alford ◽  
M. Brotman ◽  
M. A. Chudy ◽  
M. J. Fraser
Keyword(s):  
Amino Acid ◽  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Specific Enzyme ◽  
Ehrlich Ascites ◽  
Mammalian Tissues ◽  
Made In

Measurements of α-glutamyl-RNA synthetase and glutaminyl-RNA synthetase activities have been made in fractions derived from 105,000 × g supernatants of homogenates of rat liver and of mouse Ehrlich ascites carcinoma cells. Evidence is presented which indicates that each amino acid is activated by a specific enzyme. Both enzymes catalyze amino acid dependent ATP-32PP exchange. The α-glutamyl-RNA synthetase purified 42-fold from rat liver 105,000 × g supernatant is free of glutamine synthetase.

EFFECTS OF HYPOGLYCIN A ON THE METABOLISM OF AMINO ACIDS BY LIVER SLICES

1964 ◽  
Vol 42 (1) ◽  
pp. 139-142 ◽  
Author(s):  
S. J. Patrick ◽  
L. C. Stewart
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Inhibitory Effects ◽  
Liver Slices

The effects of hypoglycin A on the metabolism of L-leucine-C14, L-alanine-C14, and L-glutamic-acid-C14 by rat liver slices have been investigated. Hypoglycin exerted markedly inhibitory effects on the conversion of leucine-C14 to fatty acid, cholesterol, and CO2. Conversion of alanine-C14 and glutamic acid-C14 to fatty acids was also inhibited by hypoglycin. No effects of hypoglycin on the conversion of C14-amino acids into protein or glycogen were demonstrated.

A STUDY ON THE "IN VITRO" SYNTHESIS OF CITRULLINE: PART II. EFFECT OF GLUTAMIC ACID AND DERIVATIVES IN THE PRESENCE OF FUMARIC ACID

1964 ◽  
Vol 42 (9) ◽  
pp. 1325-1330 ◽  
Author(s):  
René Charbonneau ◽  
Louis Berlinguet
Keyword(s):  
Glutamic Acid ◽  
Rat Liver ◽  
Fumaric Acid ◽  
Liver Homogenate ◽  
Particulate Fraction ◽  
In Vitro Synthesis ◽  
System L ◽  
Acyl Derivatives

The role of N-carbamyl, N-acetyl, and L-glutamic acids with and without fumaric acid on the "in vitro" synthesis of citrulline was studied by using a particulate fraction obtained from a rat liver homogenate and a partially purified citrulline-synthesizing enzyme system. In the presence of a particulate fraction of rat liver homogenate, N-carbamyl and N-acetyl-L-glutamic acids are unable to replace L-glutamic acid, which is essential for citrulline biosynthesis. However, in the presence of fumaric acid, they both give a better synthesis of citrulline than L-glutamic acid alone. It is postulated that the acyl derivatives serve only in the transport of "activated CO2" whereas fumaric acid enters the citric acid to furnish the essential ATP molecules. Glutamic acid would be able to perform both functions. However, in the presence of a system containing partially purified citrulline-synthesizing enzymes, L-glutamic acid is unable to replace N-carbamyl and N-acetyl-L-glutamic acids with or without fumaric acid. In such a system, L-glutamic acid cannot serve in the transport of "activated CO2". It is postulated that L-glutamic acid must be acetylated prior to its utilization in this respect.With the particulate fraction of rat liver homogenate, N-allyl aspartic acid inhibits totally the synthesis of citrulline both in the presence and absence of fumaric acid with or without glutamic or N-acetyl glutamic acids. It probably interferes with the transport of "activated CO2".

Vitamin K Dependent Carboxylaticn Of Peptide Bound Glutamic Acid Residues

1981 ◽  
Author(s):  
D P Kosow ◽  
M P Esnouf ◽  
A I Gainey ◽  
H A O Hill ◽  
P J Thornally
Keyword(s):  
Carbon Dioxide ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Vitamin K ◽  
Active Carbon ◽  
Synthetic Peptide ◽  
Alcoholic Solution ◽  
Chemical Mechanism ◽  
Peptide Substrates ◽  
Rapid Formation

The chemical mechanism by which vitamin K promotes the posttranslational carboxylation of specific glutamic acid residues in the N-terminal region of prothrombin has not yet been elucidated. We have previously suggested that vitamin K reacts with dioxygen and carbon dioxide to form a species of active carbon. In this study we have investigated the reaction of reduced vitamin K in alcoholic solution with dioxygen in the presence and absence of carbon dioxide. We find that carbon dioxide is necessary for the rapid formation of vitamin K oxide. Vitamin K oxide was formed when either cis or trans vitamin K was used. However, trans vitamin K is specifically required in enzymatic carboxylation studies. We propose that in rat liver microsomal preparations the carboxylation of synthetic peptide substrates is coupled to the chemical epoxidation of vitamin K by the carboxylase.

Effect of ethanol on the metabolism of alanine, glutamic acid, and proline in rat liver

1975 ◽  
Vol 24 (2) ◽  
pp. 199-204 ◽  
Author(s):  
Hertta-Maija Häkkinen ◽  
Eino Kulonen
Keyword(s):  
Glutamic Acid ◽  
Rat Liver
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