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Enzymology
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- EnzymologyOpen Access
Structural and functional analyses of glycoside hydrolase 138 enzymes targeting chain A galacturonic acid in the complex pectin rhamnogalacturonan II
Journal of Biological ChemistryVol. 294Issue 19p7711–7721Published online: March 15, 2019- Aurore Labourel
- Arnaud Baslé
- Jose Munoz-Munoz
- Didier Ndeh
- Simon Booth
- Sergey A. Nepogodiev
- and others
Cited in Scopus: 11The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiome. The selection pressures in this environment have spurred the evolution of a complex reservoir of microbial genes encoding carbohydrate-active enzymes (CAZymes). Previously, we have shown that the human gut bacterium Bacteroides thetaiotaomicron (Bt) can depolymerize the most structurally complex glycan, the plant pectin rhamnogalacturonan II (RGII), commonly found in the human diet. Previous investigation of the RGII-degrading apparatus in Bt identified BT0997 as a new CAZyme family, classified as glycoside hydrolase 138 (GH138).