Premium
HYDRAZINOPROPIONIC ACID: A NEW INHIBITOR OF AMINOBUTYRATE TRANSAMINASE AND GLUTAMATE DECARBOXYLASEI
Author(s) -
Gelder N. M.
Publication year - 1968
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1968.tb10319.x
Subject(s) - glutamate decarboxylase , transaminase , pyridoxal phosphate , pyridoxal , pyridoxine , biochemistry , enzyme , gaba transaminase , chemistry , glutamate receptor , inhibitory postsynaptic potential , incubation , pharmacology , biology , cofactor , endocrinology , receptor
— This paper deals with the synthesis of 3‐pyrazolidone and the biochemical action of hydrazinopropionic acid. The latter compound is formed upon alkaline hydrolysis of 3‐pyrazolidone. Hydrazinopropionic acid was found in vitro to be a very potent inhibitor of bacterial aminobutyrate transaminase as well as of aminobutyrate transaminase and glutamate decarboxylase from mouse brain. This inhibition was shown to occur despite the presence of high concentrations of pyridoxal phosphate in the incubation media. Injections of 20 mg hydrazinopropionic acid/kg into mice resulted in complete inhibition of aminobutyrate transaminase in brain and approximately 20 per cent inactivation of glutamate decarboxylase. This inhibition could not be prevented or antagonized by administration of pyridoxine to the animals. Addition of pyridoxal phosphate to homogenates of brain from animals treated with hydrazinopropionic acid also failed to reactivate the enzymes. The tentative conclusion reached from these results is that hydrazinopropionic acid has inhibitory action because of its close similarity to GABA with respect to molecular size, structural configuration and molecular charge distribution. This can be demonstrated by comparing a Dreiding model of hydrazinopropionic acid with that representing GABA.