Activation by adenosine-5′-triphosphate of glutamic decarboxylase from a subcellular fraction of mouse brain

1979 ◽  
Vol 57 (8) ◽  
pp. 873-877 ◽  
Author(s):  
Godfrey Tunnicliff ◽  
That T. Ngo
Keyword(s):  
Mouse Brain ◽  
Glutamate Decarboxylase ◽  
Subcellular Fraction ◽  
Pyridoxal Phosphate ◽  
Control Mechanism ◽  
Decarboxylase Activity

Glutamate decarboxylase from a mouse brain P2 fraction undergoes a twofold activation in the presence of 0.5 mM ATP. No such stimulation by ATP occurs if the enzyme is assayed in the presence of excess pyridoxal phosphate as cofactor. The ATP-induced stimulation is almost completely eliminated if the enzyme is dialysed before its assay. [γ-32P]ATP present during the enzyme measurement is converted to [32P]pyridoxal phosphate. These results demonstrate that the activation produced by ATP is the result of the generation of cofactor during the course of the assay. This phenomenon may be a reflection of a control mechanism of glutamate decarboxylase activity.

Modifications of brain glutamate decarboxylase activity by pyridoxal phosphate-γ-glutamyl hydrazone

1967 ◽  
Vol 16 (7) ◽  
pp. 1211-1218 ◽  
Author(s):  
Ricardo Tapia ◽  
Miguel Pérez De La Mora ◽  
Guillermo H. Massieu
Keyword(s):  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Decarboxylase Activity

scholarly journals Effect of undernutrition in early life on glutamate decarboxylase activity in the adult brain

1972 ◽  
Vol 130 (1) ◽  
pp. 12P-12P ◽  
Author(s):  
B P F Adlard ◽  
J Dobbing ◽  
A Lynch ◽  
R Balázs ◽  
A P Reynolds
Keyword(s):  
Glutamate Decarboxylase ◽  
Early Life ◽  
Adult Brain ◽  
Decarboxylase Activity

scholarly journals Role of pyridoxal phosphate in mammalian polyamine biosynthesis. Lack of requirement for mammalian S-adenosylmethionine decarboxylase activity

1977 ◽  
Vol 166 (1) ◽  
pp. 81-88 ◽  
Author(s):  
A E Pegg
Keyword(s):  
Ornithine Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Vitamin B ◽  
Decarboxylase Activity ◽  
Deficient Diet ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Ornithine Decarboxylase Activity

1. Polyamine concentrations were decreased in rats fed on a diet deficient in vitamin B-6. 2. Ornithine decarboxylase activity was decreased by vitamin B-6 deficiency when assayed in tissue extracts without addition of pyridoxal phosphate, but was greater than in control extracts when pyridoxal phosphate was present in saturating amounts. 3. In contrast, the activity of S-adenosylmethionine decarboxylase was not enhanced by pyridoxal phosphate addition even when dialysed extracts were prepared from tissues of young rats suckled by mothers fed on the vitamin B-6-deficient diet. 4. S-Adenosylmethionine decarboxylase activities were increased by administration of methylglyoxal bis(guanylhydrazone) (1,1′-[(methylethanediylidine)dinitrilo]diguanidine) to similar extents in both control and vitamin B-6-deficient animals. 5. The spectrum of highly purified liver S-adenosylmethionine decarboxylase did not indicate the presence of pyridoxal phosphate. After inactivation of the enzyme by reaction with NaB3H4, radioactivity was incorporated into the enzyme, but was not present as a reduced derivative of pyridoxal phosphate. 6. It is concluded that the decreased concentrations of polyamines in rats fed on a diet containing vitamin B-6 may be due to decreased activity or ornithine decarboxylase or may be caused by an unknown mechanism responding to growth retardation produced by the vitamin deficiency. In either case, measurements of S-adenosylmethionine decarboxylase and ornithine decarboxylase activity under optimum conditions in vitro do not correlate with the polyamine concentrations in vivo.

Two approaches to the determination of glutamate decarboxylase activity in vivo

1979 ◽  
Vol 4 (5) ◽  
pp. 702
Author(s):  
L.P. Miller ◽  
J.R. Walters ◽  
D.L. Martin ◽  
N. Eng
Keyword(s):  
Glutamate Decarboxylase ◽  
Decarboxylase Activity
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