Yogeswara, I.B.A.; Maneerat, S.; Haltrich, D. Glutamate Decarboxylase from Lactic Acid Bacteria—A Key Enzyme in GABA Synthesis. Microorganisms2020, 8, 1923.
Yogeswara, I.B.A.; Maneerat, S.; Haltrich, D. Glutamate Decarboxylase from Lactic Acid Bacteria—A Key Enzyme in GABA Synthesis. Microorganisms 2020, 8, 1923.
Glutamate decarboxylase (L-glutamate-1-carboxylase, GAD; EC 184.108.40.206) is a pyridoxal 5-phosphate-dependent enzyme, which catalyzes the irreversible α-decarboxylation of L-glutamic acid to γ-aminobutyric acid (GABA) and CO2. The enzyme is widely distributed in eukaryotes as well as prokaryotes, where it – together with its reaction product GABA - fulfils very different physiological functions. The occurrence of gad genes encoding GAD has been shown for many microorganisms, and GABA-producing lactic acid bacteria (LAB) have been a focus of research during recent years. A wide range of traditional foods produced by fermentation based on LAB offer the potential of providing new functional food products enriched with GABA that may offer certain health-benefits. Different GAD enzymes and genes from several strains of LAB have been isolated and characterized recently. GABA-producing LAB, biochemical properties of their GAD enzymes, and possible applications are reviewed here.
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