1978European Journal of BiochemistryOpen access

Isolation of 4.5‐Dihydroxyisophthalic Acid, an Inhibitor of Brain Glutamate Decarboxylase, Produced by a Streptomyces Species

Akira Endo, Nobuaki Kitahara, Hidehiko Oka, Yumi MIGUCHI‐FUKAZAWA, Akira Terahara

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Abstract

A potent inhibitor of brain glutamate decarboxylase (L-glutamate 1-carboxy-lyase, EC 4.1.1.15) was isolated from cultures of a Streptomyces species, and its structure was found to be 4,5-dihydroxyisophthalic acid. The metabolite inhibited beef brain glutamate decarboxylase 50% at a concentration of 0.12 microgram/ml (0.61 micron). The kinetic analysis indicated that 4,5-dihydroxyisophthalic acid was a competitive inhibitor having a Ki value of 0.18 micron.

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A potent inhibitor of brain glutamate decarboxylase (L-glutamate 1-carboxy-lyase, EC 4.1.1.15) was isolated from cultures of a Streptomyces species, and its structure was found to be 4,5-dihydroxyisophthalic acid. The metabolite inhibited beef brain glutamate decarboxylase 50% at a concentration of 0.12 microgram/ml (0.61 micron). The kinetic analysis indicated that 4,5-dihydroxyisophthalic acid was a competitive inhibitor having a Ki value of 0.18 micron.

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Available abstract

A potent inhibitor of brain glutamate decarboxylase (L-glutamate 1-carboxy-lyase, EC 4.1.1.15) was isolated from cultures of a Streptomyces species, and its structure was found to be 4,5-dihydroxyisophthalic acid. The metabolite inhibited beef brain glutamate decarboxylase 50% at a concentration of 0.12 microgram/ml (0.61 micron). The kinetic analysis indicated that 4,5-dihydroxyisophthalic acid was a competitive inhibitor having a Ki value of 0.18 micron.

Key concepts: Glutamate decarboxylase, Streptomyces, Biochemistry, Metabolite, Carboxy-lyases, Enzyme, Glutamate receptor, Chemistry

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