PYRIDOXAL PHOSPHATE AND GLUTAMATE DECARBOXYLASE IN SUBCELLULAR PARTICLES OF MOUSE BRAIN AND THEIR RELATIONSHIP TO CONVULSIONS

1973 ◽  
Vol 20 (6) ◽  
pp. 1575-1587 ◽  
Author(s):  
A. Feria-Velasco ◽  
R. Tapia
Keyword(s):  
Mouse Brain ◽  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate

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.

Seizure susceptibility in the developing mouse and its relationship to glutamate decarboxylase and pyridoxal phosphate in brain

1975 ◽  
Vol 6 (2) ◽  
pp. 159-170 ◽  
Author(s):  
Ricardo Tapia ◽  
Herminia Pasantes-Morales ◽  
Efrain Taborda ◽  
Miguel P�rez de la Mora
Keyword(s):  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Seizure Susceptibility

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

The inhibition of mouse brain glutamate decarboxylase by some structural analogues of L-glutamic acid

1977 ◽  
Vol 26 (4) ◽  
pp. 345-349 ◽  
Author(s):  
Peter V. Taberner ◽  
Martin J. Pearce ◽  
Jeffrey C. Watkins
Keyword(s):  
Glutamic Acid ◽  
Mouse Brain ◽  
Glutamate Decarboxylase ◽  
Structural Analogues

scholarly journals Interaction of L-threo and L-erythro isomers of 3-fluoroglutamate with glutamate decarboxylase from Escherichia coli

1985 ◽  
Vol 229 (3) ◽  
pp. 675-678 ◽  
Author(s):  
A Vidal-Cros ◽  
M Gaudry ◽  
A Marquet
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Glutamate Decarboxylase ◽  
Fluorine Atom ◽  
Pyridoxal Phosphate ◽  
Succinic Semialdehyde ◽  
E Coli ◽  
Rigid Conformation ◽  
The Difference ◽  
Hydrolysis Of

L-threo-3-Fluoroglutamate and L-erythro-3-fluoroglutamate were tested with glutamate decarboxylase from Escherichia coli. Both isomers were substrates: the threo isomer was decarboxylated into optically active 4-amino-3-fluorobutyrate, whereas the erythro isomer lost the fluorine atom during the reaction, yielding succinic semialdehyde after hydrolysis of the unstable intermediate enamine. The difference between the two isomers demonstrates that the glutamic acid-pyridoxal phosphate Schiff base is present at the active site under a rigid conformation. Furthermore, although the erythro isomer lost the fluorine atom, yielding a reactive aminoacrylic acid in the active site, no irreversible inactivation of E. coli glutamate decarboxylase was observed.

scholarly journals Effect of pyridoxal administration on the contents of pyridoxal phosphate and .GAMMA.-aminobutyric acid in mouse brain.

1978 ◽  
Vol 24 (3) ◽  
pp. 255-262 ◽  
Author(s):  
Kimiharu ETO ◽  
Yasuko TAKAHASHI ◽  
Michio HOSHINO ◽  
Tae SAKURAI ◽  
Makoto MATSUDA
Keyword(s):  
Mouse Brain ◽  
Pyridoxal Phosphate ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid
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