Wei_2021_J.Agric.Food.Chem__

Reference

Title : The alpha-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket - Wei_2021_J.Agric.Food.Chem__
Author(s) : Wei X , Wang YL , Wen BT , Liu SJ , Wang L , Sun L , Gu TY , Li Z , Bao Y , Fan SL , Zhou H , Wang F , Xin F
Ref : Journal of Agricultural and Food Chemistry , : , 2021
Abstract :

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 alpha-helical domain comprising five alpha-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.

PubMedSearch : Wei_2021_J.Agric.Food.Chem__
PubMedID: 33979121
Gene_locus related to this paper: 9bact-d4inh0

Related information

Gene_locus 9bact-d4inh0
Structure 7DQ9

Citations formats

Wei X, Wang YL, Wen BT, Liu SJ, Wang L, Sun L, Gu TY, Li Z, Bao Y, Fan SL, Zhou H, Wang F, Xin F (2021)
The alpha-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket
Journal of Agricultural and Food Chemistry :

Wei X, Wang YL, Wen BT, Liu SJ, Wang L, Sun L, Gu TY, Li Z, Bao Y, Fan SL, Zhou H, Wang F, Xin F (2021)
Journal of Agricultural and Food Chemistry :