Regulation of gamma-aminobutyric acid degradation in Escherichia coli by nitrogen metabolism enzymes.
AUTOR(ES)
Zaboura, M
RESUMO
The possible role of glutamate dehydrogenase, glutamate synthase, and glutamine synthetase in the regulation of enzyme formation in the gamma-aminobutyric acid (GABA) catabolic pathway of Escherichia coli K-12 was investigated. Evidence is presented indicating that glutamine synthetase acts as a positive regulator in the E. coli GABA control system. Mutations impairing glutamate synthase activity prevent the depression of the enzymes of the GABA pathway in ammonia-limited glucose media. However, mutations resulting in constitutive synthesis of glutamine synthetase (GlnC) restore the ability of the glutamate synthase-less mutants to grow in glucose-GABA media and result in depressed synthesis of the GABA enzymes. It is suggested that the loss of glutamate synthesis activity affects the GABA control system indirectly by lowering glutamine synthetase levels.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=222043Documentos Relacionados
- Stimulation of benzodiazepine receptor binding by gamma-aminobutyric acid.
- A comparison of the enzymes and substrates of gamma-aminobutyric acid metabolism in lobster excitatory and inhibitory axons.
- gamma-Aminobutyric acid stimulates ethylene biosynthesis in sunflower.
- The gamma-aminobutyric acid system in rabbit cerebellum.
- Isolation and identification of gamma-aminobutyric acid in Streptomyces lincolnensis.
