A novel feruloyl esterase with high rosmarinic acid hydrolysis activity from Bacillus pumilus W3

Liang, Wei-Yue; Xiong, Tianzhen; Wang, Xiaomei; Deng, Huaxiang; Bai, Yajun; Fan, Tai-Ping; Zheng, Xiaohui; Cai, Yujie

doi:10.1016/j.ijbiomac.2020.06.038

Cited by 8 publications

(3 citation statements)

References 37 publications

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“…18 Other esterases from gut bacteria such as Lactobacilli and Bif idobacteria also exhibited higher catalytic efficiencies and a higher affinity toward pNPA than that of AsFAE. 21,30 The distinct activities suggested different catalytic mechanisms of gut microbe-derived FAEs.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Another FAE from Bacteroides species, Bi Fae1A, exhibited similar K m to As FAE but higher catalytic efficiencies for p NPA ( K m and k cat / K m values of 1.43 mM and 714 mM –1 min –1 , respectively) . Other esterases from gut bacteria such as Lactobacilli and Bifidobacteria also exhibited higher catalytic efficiencies and a higher affinity toward p NPA than that of As FAE. , The distinct activities suggested different catalytic mechanisms of gut microbe-derived FAEs.…”

Section: Resultsmentioning

confidence: 99%

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The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

Wei

Wang

Wen

et al. 2021

J. Agric. Food Chem.

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The human gut microbiota regulates nutritional metabolism, especially by encoding specific ferulic acid esterases (FAEs) to release functional ferulic acid (FA) from dietary fiber. In our previous study, we observed seven upregulated FAE genes during in vitro fecal slurry fermentation using wheat bran. Here, a 29 kDa FAE (AsFAE) from Alistipes shahii of Bacteroides was characterized and identified as the type-A FAE. The X-ray structure of AsFAE has been determined, revealing a unique α-helical domain comprising five α-helices, which was first characterized in FAEs from the gut microbiota. Further molecular docking analysis and biochemical studies revealed that Tyr100, Thr122, Tyr219, and Ile220 are essential for substrate binding and catalytic efficiency. Additionally, Glu129 and Lys130 in the cap domain shaped the substrate-binding pocket and affected the substrate preference. This is the first report on A. shahii FAE, providing a theoretical basis for the dietary metabolism in the human gut.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

Wei

Wang

Wen

et al. 2021

J. Agric. Food Chem.

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“…In plants of the Lamiaceae family, the biosynthesis of RA is catalyzed by rosmarinate synthase from Caffeoyl‐CoA and DSS (Levsh et al 2019 ) and is created by an ester bond between CA and DSS (Figure S4 ). The ester bond in RA may be hydrolyzed and degraded under various conditions (Bel‐Rhlid et al 2009 ; Liang et al 2020 ; Papaemmanouil et al 2020 ). Sik et al ( 2021 ) reported that hydrolysis could occur in both the tincture (ethanol) and aqueous solutions of RA during storage, which thus produces CA and DSS.…”

Section: Discussionmentioning

confidence: 99%

Molecular mechanism of Fe³⁺ binding inhibition to Vibrio metschnikovii ferric ion‐binding protein, FbpA, by rosmarinic acid and its hydrolysate, danshensu

Lu,

Jiang,

Liu

et al. 2024

Protein Science

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Global warming has increased the growth of pathogenic Vibrio bacteria, which can cause foodborne illnesses and death. Vibrio bacteria require iron for growth and survival. They utilize a ferric ion‐binding protein (FbpA) to bind and transport Fe3+ into the cell. FbpA from V. metschnikovii (Vm) is a potential target for inhibiting its growth. Rosmarinic acid (RA) can block the binding of VmFbpA to Fe3+; however, the molecular mechanism of Fe3+ binding and RA inhibition to VmFbpA is unclear. In this study, we used X‐ray crystallography to determine the Fe3+ binding mode of VmFbpA and the mechanism of RA inhibition. The structures revealed that in the Fe3+ bound form, Fe3+ was coordinated to VmFbpA by two Tyr residues, two HCO3− ions, and two water molecules in a six‐coordinated geometry. In contrast, in the inhibitor bound form, RA was initially bound to VmFbpA following gel filtration purification, but it was hydrolyzed to danshensu (DSS), which occupied the binding site as shown in an electron density map and reverse phase chromatography (RPC) analysis. Both RA and DSS exhibited a stronger binding affinity to VmFbpA, higher Fe3+ reduction capacity, and more potent bacteriostatic effect on V. metschnikovii compared with caffeic acid (CA), another hydrolysis product of RA. These results provide insight into the mechanism of iron acquisition by V. metschnikovii and inhibition by RA and DSS. Our findings offer clues on the development of effective strategies to prevent Vibrio infections.This article is protected by copyright. All rights reserved.

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Enzyme Assisted Food Processing

Famiglietti¹,

Mirpoor²,

Giosafatto³

et al. 2023

Sustainable Food Science - A Comprehensive Approach

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A novel feruloyl esterase with high rosmarinic acid hydrolysis activity from Bacillus pumilus W3

Cited by 8 publications

References 37 publications

The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

Molecular mechanism of Fe³⁺ binding inhibition to Vibrio metschnikovii ferric ion‐binding protein, FbpA, by rosmarinic acid and its hydrolysate, danshensu

Enzyme Assisted Food Processing

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A novel feruloyl esterase with high rosmarinic acid hydrolysis activity from Bacillus pumilus W3

Cited by 8 publications

References 37 publications

The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket

Molecular mechanism of Fe3+ binding inhibition to Vibrio metschnikovii ferric ion‐binding protein, FbpA, by rosmarinic acid and its hydrolysate, danshensu

Enzyme Assisted Food Processing

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Molecular mechanism of Fe³⁺ binding inhibition to Vibrio metschnikovii ferric ion‐binding protein, FbpA, by rosmarinic acid and its hydrolysate, danshensu