Effect of cations on the activity of L-glutamic acid dehydrogenase

Life Sciences ◽  
1963 ◽  
Vol 2 (11) ◽  
pp. 834-839 ◽  
Author(s):  
E. Schoffeniels ◽  
R. Gilles
Keyword(s):  
Glutamic Acid ◽  
Acid Dehydrogenase

scholarly journals Molecular Weight of Chicken Liver Glutamic Acid Dehydrogenase in Relation to the Activating Effect of Methylmercuric Bromide

1963 ◽  
Vol 238 (1) ◽  
pp. PC481-PC482
Author(s):  
Kenneth S. Rogers ◽  
Paul J. Geiger ◽  
Thomas E. Thompson ◽  
Leslie Hellerman
Keyword(s):  
Molecular Weight ◽  
Glutamic Acid ◽  
Chicken Liver ◽  
Acid Dehydrogenase

METHODS OF PROTEIN EXTRACTION FROM NEUROSPORA CRASSA

1964 ◽  
Vol 10 (1) ◽  
pp. 29-35 ◽  
Author(s):  
G. J. Stine ◽  
W. N. Strickland ◽  
R. W. Barratt
Keyword(s):  
Glutamic Acid ◽  
Neurospora Crassa ◽  
Total Protein ◽  
Extraction Method ◽  
Protein Extraction ◽  
Specific Activity ◽  
Dry Weight ◽  
Acid Dehydrogenase ◽  
Total Enzyme

Nine methods for disrupting the mycelium of Neurospora crassa have been compared. Protein percentages are calculated per gram dry weight of mycelium. A TPN-specific glutamic acid dehydrogenase was extracted and the efficiency of each extraction method is given as total enzyme extracted and specific activity. In terms of total protein, total enzyme, and practicality of the method, the Hughes Press, the French Press and the Raper–Hyatt Press were found to be the most efficient. The advantages and limitations of each method are considered.

Some aspects of the nitrogen metabolism of Nodularia spumigena (Cyanophyceae)

1974 ◽  
Vol 52 (4) ◽  
pp. 719-726 ◽  
Author(s):  
E. L. Camm ◽  
J. R. Stein
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Growth Inhibition ◽  
Glutamic Acid ◽  
Nitrogen Metabolism ◽  
Free Medium ◽  
Nodularia Spumigena ◽  
Whole Cells ◽  
Acid Dehydrogenase ◽  
Reducing Ability

Nitrate-reducing ability, NO2−-reducing ability, and glutamic acid dehydrogenase levels were measured in two clones of Nodularia spumigena Mertens. Measurements with whole cells of both clones show that NO3− reduction is stimulated by NO3−, and that NO2− reduction is probably stimulated by NO2−. The NO3−-reducing system is stimulated by light and inhibited by NH4+. These controls and possible control over NH4+ incorporation into amino acids are compared to systems operative in other organisms.Differences in growth and physiology of the clones in growth rate on N-free medium, growth inhibition by urea, and NO2− accumulation in the medium are discussed.

Alpha-ketoglutarate as an intermediate in glutamate metabolism by Peptococcus aerogenes

1972 ◽  
Vol 18 (6) ◽  
pp. 875-880 ◽  
Author(s):  
W. M. Johnson ◽  
D. W. S. Westlake
Keyword(s):  
Potential Energy ◽  
Glutamic Acid ◽  
Tca Cycle ◽  
The Other ◽  
Glutamate Metabolism ◽  
Fermentation Products ◽  
Acid Dehydrogenase ◽  
Specific Distribution ◽  
The Tca Cycle ◽  
Hydroxyglutaric Acid

The pathway from glutamic acid to α-hydroxyglutaric acid in Peptococcus aerogenes proceeds via α-ketoglutaric acid and is mediated by two NAD-dependent enzymes. One enzyme, an NAD-dependent glutamic acid dehydrogenase, oxidatively deaminates glutamic acid to α-ketoglutaric acid. The other enzyme, α-ketoglutaric acid reductase, reduces α-ketoglutaric acid to α-hydroxyglutaric acid in the presence of NADH. The demonstration of a very low level of α-ketoglutaric acid dehydrogenase activity in crude cell-free extracts indicates that the primary metabolic pathway for glutamic acid carbons proceeds via α-hydroxyglutaric acid and not via the TCA cycle. Potential energy-yielding mechanisms are discussed relative to the known specific distribution of glutamic acid carbon atoms in fermentation products.

Purification and characterization of glutamic acid dehydrogenase and α-ketoglutaric acid reductase from Peptococcus aerogenes

1972 ◽  
Vol 18 (6) ◽  
pp. 881-892 ◽  
Author(s):  
W. M. Johnson ◽  
D. W. S. Westlake
Keyword(s):  
Glutamic Acid ◽  
Kinetic Data ◽  
Acid Metabolism ◽  
The Other ◽  
Keto Acid ◽  
Glutamate Metabolism ◽  
Purification And Characterization ◽  
Acid Dehydrogenase ◽  
Acid Reduction

Two NAD-dependent enzymes involved in glutamic acid metabolism have been isolated from cell-free extracts of P. aerogenes. One enzyme, glutamic acid dehydrogenase, was shown to oxidatively deaminate glutamic acid yielding α-ketoglutaric acid in the presence of NAD but not NADP. The other enzyme, an NADH-requiring α-ketoglutarate reductase, reduced the α-keto acid to α-hydroxy-glutarate. The two NAD-dependent enzymes were separated, purified, and characterized. The results indicate that glutamic acid dehydrogenase, an enzyme not frequently implicated in anaerobic glutamate metabolism, is a predominating protein in extracts of P. aerogenes grown in the presence of glutamate. Kinetic data showed that the equilibrium of the latter reaction favored the direction of keto acid reduction.

Some enzymic syntheses of 15N-L-aspartic acid and 15N-L-glutamic acid

1969 ◽  
Vol 47 (3) ◽  
pp. 411-415 ◽  
Author(s):  
J. A. Zintel ◽  
A. J. Williams ◽  
R. S. Stuart
Keyword(s):  
Glutamic Acid ◽  
Aspartic Acid ◽  
Fumaric Acid ◽  
Aspartate Aminotransferase ◽  
Efficient Utilization ◽  
E Coli ◽  
Acid Dehydrogenase ◽  
Acid Catalyzed ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions

Some methods for the preparation of 15N-L-aspartic acid and 15N-L-glutamic acid using enzyme catalyzed reactions are described. 15N-L-Aspartic acid is prepared by the addition of ammonia to fumaric acid, catalyzing the reaction with aspartase which was partially purified from E. coli. 15N-L-Glutamic acid with a high 15N/14N ratio is prepared by transamination with 15N-L-aspartic acid catalyzed by aspartate aminotransferase. 15N-L-Glutamic acid with a low 15N/14N ratio is prepared by a glutamic acid dehydrogenase catalyzed exchange of L-glutamic acid with 15N-ammonia. These enzymes are commercially available. Since efficient utilization of 15N is obtained, aspartic acid or glutamic acid may be prepared with any desired 15N/14N ratio.

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