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Glutamate Decarboxylase from Lactic Acid Bacteria-A Key Enzyme in GABA Synthesis.

ABSTRACT: Glutamate decarboxylase (l-glutamate-1-carboxylase, GAD; EC 4.1.1.15) is a pyridoxal-5'-phosphate-dependent enzyme that catalyzes the irreversible ?-decarboxylation of l-glutamic acid to ?-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, the biochemical properties of their GAD enzymes, and possible applications are reviewed here.

SUBMITTER: Yogeswara IBA

PROVIDER: S-EPMC7761890 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Glutamate Decarboxylase from Lactic Acid Bacteria-A Key Enzyme in GABA Synthesis.

Yogeswara Ida Bagus Agung IBA Maneerat Suppasil S Haltrich Dietmar D

Microorganisms 20201203 12

Glutamate decarboxylase (l-glutamate-1-carboxylase, GAD; EC 4.1.1.15) is a pyridoxal-5'-phosphate-dependent enzyme that catalyzes the irreversible α-decarboxylation of l-glutamic acid to γ-aminobutyric acid (GABA) and CO<sub>2</sub>. 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 <i>gad</i> genes encoding GAD has been shown for many microorganisms, and GABA-p ...[more]

PMID: 33287375

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Project description:Glutamate decarboxylase (GAD) pathway (GDP) is a major acid resistance mechanism enabling microorganisms' survival in low pH environments. We aimed to study the molecular evolution and population genetics of GDP in Lactic Acid Bacteria (LAB) to understand evolutionary processes shaping adaptation to acidic environments comparing species where the GDP genes are organized in an operon structure (Levilactobacillus brevis) versus lack of an operon structure (Lactiplantibacillus plantarum). Within species molecular population genetic analyses of GDP genes in L. brevis and L. plantarum sampled from diverse fermented food and other environments showed abundant synonymous and non-synonymous nucleotide diversity, mostly driven by low frequency changes, distributed throughout the coding regions for all genes in both species. GAD genes showed higher level of replacement polymorphism compared to transporter genes (gadC and YjeM) for both species, and GAD genes that are outside of an operon structure showed even higher level of replacement polymorphism. Population genetic tests suggest negative selection against replacement changes in all genes. Molecular structure and amino acid characteristics analyses showed that in none of the GDP genes replacement changes alter 3D structure or charge distribution supporting negative selection against non-conservative amino acid changes. Phylogenetic and between species divergence analyses suggested adaptive protein evolution on GDP genes comparing phylogenetically distant species, but conservative evolution comparing closely related species. GDP genes within an operon structure showed slower molecular evolution and higher conservation. All GAD and transporter genes showed high codon usage bias in examined LAB species suggesting high expression and utilization of acid resistance genes. Substantial discordances between species, GAD, and transporter gene tree topologies were observed suggesting molecular evolution of GDP genes do not follow speciation events. Distribution of operon structure on the species tree suggested multiple independent gain or loss of operon structure in LABs. In conclusion, GDP genes in LABs exhibit a dynamic molecular evolutionary history shaped by gene loss, gene transfer, negative and positive selection to maintain its active role in acid resistance mechanism, and enable organisms to thrive in acidic environments.

Dataset Information

Glutamate Decarboxylase from Lactic Acid Bacteria-A Key Enzyme in GABA Synthesis.

Publications

Glutamate Decarboxylase from Lactic Acid Bacteria-A Key Enzyme in GABA Synthesis.

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