Formation of L-Glutamic Acid from γ-Aminobutyric Acid by Plant Enzyme
TAKAO SUZUKI, Akio Maekawa, Tadao Hasegawa, Munetsugu Ito, Hiroshi HONDA, T. Nagano, Susumu Saito, YOSHIKAZU SAHASHI
Abstract
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TAKAO SUZUKI, Akio Maekawa, Tadao Hasegawa, Munetsugu Ito, Hiroshi HONDA, T. Nagano, Susumu Saito, YOSHIKAZU SAHASHI
Abstract
Open-access reader
In the course of studies concerning the reverse action of L-glutamic acid decarboxylase, the authors have asserted the inhibition of ƒ¿-ketoglutaric acid and the presence of L-glutamic acid and ƒÁ-aminobutyric acid in the enzyme preparations.Finally, evidence for the inter conversion of ƒ¿-ketoglutaric-ƒÁ-aminobutyric transaminase and L-glutamic acid decarboxylase preparations isolated from plant tissue was established in our laboratory.
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In the course of studies concerning the reverse action of L-glutamic acid decarboxylase, the authors have asserted the inhibition of ƒ¿-ketoglutaric acid and the presence of L-glutamic acid and ƒÁ-aminobutyric acid in the enzyme preparations.Finally, evidence for the inter conversion of ƒ¿-ketoglutaric-ƒÁ-aminobutyric transaminase and L-glutamic acid decarboxylase preparations isolated from plant tissue was established in our laboratory.
Key concepts: Glutamate decarboxylase, Glutamic acid, Transaminase, Aminobutyric acid, Biochemistry, Chemistry, Pyridoxal phosphate, Enzyme