Metabolic shift in the production of corrinoid compounds by Lactobacillus coryniformis in the absence of purines

Torres, Andrea Carolina; Elean, Mariano; Hébert, Elvira María; Saavedra, Lucila; Taranto, María Pía

doi:10.1016/j.biochi.2019.11.003

Cited by 5 publications

(5 citation statements)

References 27 publications

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“…Collectively, the results from this study suggest that the specificity of CblS in Firmicutes is broad in the sense that the protein can assimilate diverse α-ribosides for the purpose of synthesizing cobamides that can be used by the cell. This idea would be consistent with the recent reports that the CblS-utilizing L. coryniformis synthesizes both Cbl and psCbl, depending on the presence or absence of specific bases in the environment . This broad specificity of CblS would be crucial in natural environments, where the availability of α-ribosides or even nucleobases may vary over time and place.…”

Section: Concluding Remarkssupporting

confidence: 89%

“…This idea would be consistent with the recent reports that the CblSutilizing L. coryniformis synthesizes both Cbl and psCbl, depending on the presence or absence of specific bases in the environment. 32 This broad specificity of CblS would be crucial in natural environments, where the availability of α-ribosides or even nucleobases may vary over time and place.…”

Section: ■ Concluding Remarksmentioning

confidence: 99%

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Functional Studies of α-Riboside Activation by the α-Ribazole Kinase (CblS) from Geobacillus kaustophilus

2021

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We report the initial characterization of the αribazole (α-R) kinase enzyme of Geobacillus kaustophilus (GkCblS), which converts α-R to α-R-phosphate (α-RP) during the synthesis of cobamides. We implemented a continuous spectrophotometric assay to obtain kinetic parameters for several potential substrates and to study the specificity of the enzyme for α-N-linked ribosides. The apparent K m values for α-R and ATP were 358 and 297 μM, respectively. We also report methods for synthesizing and quantifying non-commercially available α-ribosides and β-ribazole (β-R). Purified GkCblS activated α-R and other α-ribosides, including α-adenosine (α-Ado). GkCblS did not phosphorylate β-N-linked glycosides like β-adenosine or β-R. Expression of G. kaustophilus cblS + in a Salmonella enterica subsp. enterica sv Typhimurium LT2 (S. enterica) strain lacking the nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyl transferase (CobT) enzyme resulted in the activation of various benzimidazole α-ribosides, and the synthesis of benzimidazolyl cobamides to levels that supported robust growth. Notably, α-Ado did not support growth under similar conditions, in spite of the fact that GkCblS phosphorylated α-Ado in vitro. When α-Ado was provided at a very high concentration, growth was observed. This result suggested that in S. enterica α-Ado transport may be inefficient. We conclude that GkCblS has specificity for α-N-glycosidic bonds, but not for the base in α-ribosides.

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Section: Concluding Remarkssupporting

confidence: 89%

Section: ■ Concluding Remarksmentioning

confidence: 99%

Functional Studies of α-Riboside Activation by the α-Ribazole Kinase (CblS) from Geobacillus kaustophilus

2021

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“…Beyond their role in fermented food production, some strains of L. brevis also hold substantial promise as probiotics ( Fang et al, 2018 ; Cataldo et al, 2020b ; Kaur et al, 2023 ). Furthermore, certain metabolites produced by LAB, such as γ-aminobutyric acid (GABA), are increasingly being marketed as postbiotics constituents ( Hebert et al, 2015 ; Torres et al, 2020 ; Kaur et al, 2023 ); offering proven health benefits to the host, including anxiety reduction and improved sleep quality ( Salminen et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Comprehensive characterization of γ-aminobutyric acid (GABA) production by Levilactobacillus brevis CRL 2013: insights from physiology, genomics, and proteomics

Cataldo,

Urquiza Martínez,

Villena

et al. 2024

Front. Microbiol.

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IntroductionLevilactobacillus brevis CRL 2013, a plant-derived lactic acid bacterium (LAB) with immunomodulatory properties, has emerged as an efficient producer of γ-aminobutyric acid (GABA). Notably, not all LAB possess the ability to produce GABA, highlighting the importance of specific genetic and environmental conditions for GABA synthesis. This study aimed to elucidate the intriguing GABA-producing machinery of L. brevis CRL 2013 and support its potential for safe application through comprehensive genome analysis.MethodsA comprehensive genome analysis of L. brevis CRL 2013 was performed to identify the presence of antibiotic resistance genes, virulence markers, and genes associated with the glutamate decarboxylase system, which is essential for GABA biosynthesis. Then, an optimized chemically defined culture medium (CDM) was supplemented with monosodium glutamate (MSG) and yeast extract (YE) to analyze their influence on GABA production. Proteomic and transcriptional analyses were conducted to assess changes in protein and gene expression related to GABA production.ResultsThe absence of antibiotic resistance genes and virulence markers in the genome of L. brevis CRL 2013 supports its safety for potential probiotic applications. Genes encoding the glutamate decarboxylase system, including two gad genes (gadA and gadB) and the glutamate antiporter gene (gadC), were identified. The gadB gene is located adjacent to gadC, while gadA resides separately on the chromosome. The transcriptional regulator gadR was found upstream of gadC, with transcriptional analyses demonstrating cotranscription of gadR with gadC. Although MSG supplementation alone did not activate GABA synthesis, the addition of YE significantly enhanced GABA production in the optimized CDM containing glutamate. Proteomic analysis revealed minimal differences between MSG-supplemented and non-supplemented CDM cultures, whereas YE supplementation resulted in significant proteomic changes, including upregulation of GadB. Transcriptional analysis confirmed increased expression of gadB and gadR upon YE supplementation, supporting its role in activating GABA production.ConclusionThese findings provide valuable insights into the influence of nutrient composition on GABA production. Furthermore, they unveil the potential of L. brevis CRL 2013 as a safe, nonpathogenic strain with valuable biotechnological traits which can be further leveraged for its probiotic potential in the food industry.

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“…Beyond their role in fermented food production, some strains of L. brevis also hold substantial promise as probiotics (Fang et al, 2018;Cataldo et al, 2020b;Kaur et al, 2023). Furthermore, certain metabolites produced by LAB, such as γ-aminobutyric acid (GABA), are increasingly being marketed as postbiotics constituents (Hebert et al, 2015;Torres et al, 2020;Kaur et al, 2023); offering proven health benefits to the host, including anxiety reduction and improved sleep quality (Salminen et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

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Metabolic shift in the production of corrinoid compounds by Lactobacillus coryniformis in the absence of purines

Cited by 5 publications

References 27 publications

Functional Studies of α-Riboside Activation by the α-Ribazole Kinase (CblS) from Geobacillus kaustophilus

Functional Studies of α-Riboside Activation by the α-Ribazole Kinase (CblS) from Geobacillus kaustophilus

Comprehensive characterization of γ-aminobutyric acid (GABA) production by Levilactobacillus brevis CRL 2013: insights from physiology, genomics, and proteomics

Table_4.CSV

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